Hondal Robert cv2019 - uvm.edu · My professional effort is split more like a faculty member from CAS as it has a 40:45:15 split between teaching, research, and service, respectively

Larner College of Medicine Prepared: 2/1/2020

Robert J. Hondal CURRICULUM VITAE

Position: Associate Professor Department of Biochemistry Department of Chemistry – secondary appointment Address: Given Building B413, 89 Beaumont Ave Department of Biochemistry The Robert Larner, M.D. College of Medicine University of Vermont Burlington, VT 05405 Voice: (802) 656-8282 email: [email protected] website: https://www.med.uvm.edu/biochemistry/lab_hondal_research EDUCATION Year Instituition Degree Area of Degree,

Accolades 1999-2002 University of Wisconsin-Madison Post-Doc NIH Post-Doctoral

Fellow, 1 F32 GM20180

1997-1998 Vanderbilt Univesity Post-Doc selenoprotein function 1991-1997 The Ohio State University Ph. D. chemistry 1989-1991 University of Pittsburgh B. S. chemistry LICENSES, CERTIFICATION - none FACULTY POSITIONS HELD Years Institution Academic Title Department 2010- University of Vermont Assoc. Prof. Chemistry Chemistry 2008- University of Vermont Assoc. Prof. Biochemistry Biochemistry 2002-2008 University of Vermont Assistant Prof. Biochemistry OTHER POSITIONS AND MAJOR ADMINISTRATIVE POSITIONS HELD [optional-add duties/description] Years Location/Program Name Role 2010- Chemistry Associate Professor, secondary

appointment 2004-2009 Larner College of Medicine Director, UVM Protein Core

Facility

Date First Name Last Name

2

HONORS AND AWARDS [All inclusive, most recent last] Year Name of Award 2009 The 2009 Journal of Peptide Science Best Publication Award 2016 Nomination for LCOM Research Mentorship Award 2017 Office of Undergraduate Research Student Mentoring Award KEYWORDS/AREAS OF INTEREST [Please provide a set of MESH indexing terms to describe your research and/or clinical interests.] selenocysteine, selenoprotein, oxidative inactivation, thioredoxin reductase, enzyme mechanism, protein engineering, semisynthesis, cysteine, regioselective disulfide bond formation, orthogonal deprotection, cysteine deprotection, chemoselectivity, sulfenic acid, sulfinic acid, sulfonic acid, selenenic acid, selenininc acid, glutathione peroxidase, enzyme mimic, ascorbate SUMMARY OF PROFESSIONAL ACTIVITIES- OVERALL

My professional effort is split more like a faculty member from CAS as it has a 40:45:15 split between teaching, research, and service, respectively.

I have strongly contributed to the teaching mission of the Department of Biochemistry by developing two new undergraduate courses that did not exist in my department before my arrival. These are BIOC 263 (Nutritional Biochemistry) and BIOC 207 (Biochemistry Laboratory). I have taught, in whole or part, most of the undergraduate and graduate courses my department offers. I have received nominations for teaching awards from both the graduate and undergraduate students.

I also have made significant contributions to my department and LCOM as a whole. Since becoming a faculty member in 2002, I have published 39 research articles (52 in total), 6 review articles, and one book chapter. I have a Google Scholar H-index of 27, with 2,355 total citations. The standing of my research in the fields of selenium biochemistry, redox biochemistry, protein engineering, and peptide chemistry is evidenced by my invitations to national and international symposia and the three NIH grants that have been awarded to me during my tenure at UVM.

Last, I have performed service at the Departmental, College and University levels throughout my 17 years at UVM. In addition, I have performed served on various grant agency review panels and served as a review for numerous publications both at the national and international levels. My service to the Department of Biochemistry stands out as I have served for many years as the Chair of the Graduate Student Recruitment and Admissions Committee as well as the Faculty Advisor for the UVM Biochemical Society, where I helped organize numerous events such as trips to biotech companies such as New England Biolabs. I have strong service commitments to the College of Medicine as exemplified by my membership on the LCOM Internal Grant Program Committee and my leadership of the Peptide Core Facility. At the University level, I have served roles on undergraduate awards committees, and have served on both the Faculty Senate Curriculum Affairs Committee and the Faculty Senate itself. At the national level, I have served as an ad-hoc reviewer for many journals as indicated.


3

SUMMARY OF ACCOMPLISHMENTS

•Internationally recognized expert in the areas of selenium biochemistry and cysteine-peptide chemistry. •Strong publication record as evidenced by 56 published papers including reviews with an H-index of 27. •Excellence in teaching as evidenced by numerous nomintations for teaching awards at the undergraduate and graduate levels. •Excellence in mentoring undergraduates as evidenced by award given by the Office of Undergraduate Research. •NIH funding for 13 years (non-consecutive). PROFESSIONAL SERVICE DEPARTMENTAL SERVICE [at least last 5 years, more as appropriate; subdivide as necessary] Years Department Committee Role 2003-2012 Biochemistry Graduate Student Admission

and Recruitment member

2007-2012 Biochemistry Graduate Student Admission and Recruitment

Chair

2005-2012 Biochemistry Graduate Teaching Assistant Chair 2010-2011 Biochemistry Chair Search member 2011-2012 Chemistry Faculty Search member 2013-2014 Chemistry Faculty Search member 2013-2015 Biochemistry/

Chemistry Admitted Student Day faculty representative

2014 Biochemistry Business Manager Search member 2014-2015 Biochemistry Faculty Search co-Chair 2014-2015 Biochemistry Departmental Seminar Chair 2014-2018 Biochemistry/

Chemistry Proposed Cross-College Biochemistry Ph.D Program

Chair

2018-2019 Nutrition & Food Science

Faculty Search member

COLLEGE SERVICES Years Service Committee Role 2004-2009 Peptide Synthesis Core Facility (LCOM) Director 2005-2008 Faculty Nominating (LCOM) member 2009-2012 LCOM Internal Grant Program (LCOM) member 2012-present Teaching Assistant Assignment (GRAD) member 2012 Graduate Student Research Day (CMB) faculty judge (posters) 2013 Graduate Student Research Day (CMB) faculty judge (presentations) 2015 Norman Alpert Research Prize (LCOM) member


4

UNIVERSITY SERVICE Years Service Committee Role 2007-2012 Faculty Senate: Curricular Affairs member 2011-2015 UVM Biochemical Society Faculty Advisor 2014 Office of Undergraduate Research Review

Panel member

2015-present Faculty Senate Biochemistry Senator 2018 Vermont Genetic Network Review Panel member 2018-2019 Summer Undergraduate Research Fellowship

Review Panel member

2019 UVM Fulbright Nominating Committee Interviewer GOVERNMENT [list all as appropriate, at least 5 years] Years Service Committee Role 2017 Florida Department of Health Ad-hoc reviewer 2018 Vermont Genetics Network Ad-hoc reviewer SOCIETY MEMBERSHIPS [list all] Years Society 1994-present American Chemical Society SERVICE TO PROFESSIONAL PUBLICATIONS [list all as appropriate] Years Journal/Publication/Board 2002-present Ad-hoc reviewer Journal of the American Chemical Society 2002-present Ad-hoc reviewer Biochemistry 2002-present Ad-hoc reviewer Chemistry: A European Journal 2002-present Ad-hoc reviewer Journal of Organic Chemistry 2002-present Ad-hoc reviewer Journal of Peptide Science 2002-present Ad-hoc reviewer Organic Letters 2002-resent Ad-hoc reviewer Nucleic Acids Research 2002-present Ad-hoc reviewer FEBS Letters 2002-present Ad-hoc reviewer Tetrahedron 2002-present Ad-hoc reviewer Tetrahedron Letters 2002-present Ad-hoc reviewer PLos ONE 2002-present Ad-hoc reviewer Biochem. Biophys. Acta 2002-present Ad-hoc reviewer Cellular and Molecular Life Sciences 2002-present Ad-hoc reviewer Life Sciences 2002-present Ad-hoc reviewer Antioxidants and Redox Signaling 2002-present Ad-hoc reviewer Free Radicals in Biology and Medicine


5

SUMMARY OF SERVICE ACTIVITIES

My service has been diverse and broad as I have significant service at the Departmental, College, University, and national levels. My current service to permanent standing committees consists of representing the Department of Biochemistry in the Faculty Senate, and as a member of the GTA Assignment Committee, which is a committee of the Graduate College. However, as can be seen in the tables above, I have recently served on multiple, ad-hoc committees in service to undergraduate endeavors such as a member of the Summer Undergraduate Research Fellowship Review Panel (decides which undergraduate grants are funded by FOUR), and the UVM Fulbright Nominating Committee.

I would like to specifically highlight my past service as the Faculty Advisor to the UVM Biochemical Society (2005-2007 and again from 2011-2015), an undergraduate club, mainly for biochemistry majors (open to all). The purpose of this club is for undergraduates to facilitate their own education by learning about: undergraduate research opportunities, internships, careers in sales and the biotech industry, and science beyond the classroom. To help assist with these goals, I helped to organize the following events: publication of a biochemistry major newsletter, academic advising sessions, career advising sessions, hosted speakers about careers and medical school (for example Faith Rushford and Ann Kroll Lerner), Department of Biochemistry open house, outside seminar speakers from the biotech industry and academia, and field trips to local biotech companies such as Green Mountain Antibodies, New England Biolabs, and BioTek. While it is very visibly recognized at UVM that LCOM educates medical students, the role of LCOM in educating undergraduates receives low visibility. I am proud of my role in helping undergraduates further their education and advance to careers, medical school, and graduate school. TEACHING FORMAL SCHEDULED CLASSES [list classes taught since last promotion.]

Year

Course Title Course R E

Hours Number

of Learners

Learner Level

2008 BIOC 381: Graduate Seminar x 14 15 Grad 2008 BIOC 191: Undergraduate Research x NA 2 Ugrad 2009 BIOC 351: Proteins I x 12 ~10 Grad 2009 BIOC 192: Undergraduate Research x NA 2 Ugrad 2009 BIOC 371: Physical Biochemistry x 10.5 ~10 Grad 2009 BIOC 191: Undergraduate Research x NA 2 Ugrad 2010 BIOC 353: Proteins II - Enzymes x 18 ~10 Grad 2010 BIOC 192: Undergraduate Research x NA 1 Ugrad 2010 CHEM 040: Introduction to Research x NA 1 Ugrad 2010 BIOC 205: Biochemistry I x 40 ~100 Ugrad 2010 MMG 199: Undergraduate Research x NA 1 Ugrad 2011 BIOC 351: Proteins I x 21 ~10 Grad 2011 BIOC 192: Undergraduate Research x NA 1 Ugrad 2011 BIOC 205: Biochemistry I x 40 ~100 Ugrad 2011 BIOC 191: Undergraduate Research x NA 3 Ugrad 2012 BIOC 353: Proteins II - Enzymes x 21 ~10 Ugrad


6

2012 BiOC 207: Biochemistry Laboratory x 10 16 Ugrad 2012 BIOC 192: Undergraduate Research x NA 3 Ugrad 2012 BIOC 205: Biochemistry I x 40 ~100 Ugrad 2012 BIOC 191: Undergraduate Research x NA 4 Ugrad 2012 CHEM 291: Undergraduate Research x NA 1 Ugrad 2012 PATH 305: Molecular Mech. Environ. Disease x 1.5 ~10 Grad 2013 BIOC 192: Undergraduate Research x NA 4 Ugrad 2013 PHRM 303: Pharmacological Technique x NA 1 Ugrad 2013 BIOC 212: Biochemistry of Human Disease x 1 10 Ugrad 2013 BIOC 284: Senior seminar x 2 15 Ugrad 2013 BIOC 205: Biochemistry I x 40 ~100 Ugrad 2013 BIOC 191: Undergraduate Research x NA 4 Ugrad 2014 BIOC 351: Proteins I x 28.5 ~10 Grad 2014 BIOC 212: Biochemistry of Human Disease x 1 10 Ugrad 2014 PATH 395: Special Topics x 1 10 Grad 2014 HON 196B: Honors College Research x NA 1 Ugrad 2014 BIOC 192: Undergraduate Research x NA 4 Ugrad 2014 CHEM 040: Introduction to Research x NA 1 Ugrad 2014 BIOC 301: Biochemistry I for graduate students x 31 40 Grad 2014 BIOC 191: Undergraduate Research x NA 2 Ugrad 2014 HON 196B: Honors College Research x NA 1 Ugrad 2015 BIOC 296B: Nutritional Biochemistry x 43 50 Ugrad 2015 BIOC 192: Undergraduate Research x NA 3 Ugrad 2015 HON 196B: Honors College Research NA 1 Ugrad 2015 CHEM 292: Undergraduate Research x NA 1 Ugrad 2015 HLTH 095: Exploring Anatamoy & Physiology x 2 40 Ugrad 2015 BIOC 195: Preparation for Biochemistry x 1.5 ~10 Ugrad 2016 BIOC 263: Nutritional Biochemistry x 43 50 Ugrad 2016 BIOC 192: Undergraduate Research x NA 3 Ugrad 2016 CHEM 291: Undergraduate Research x NA 1 Ugrad 2016 HON 196B: Honors College Research x NA 1 Ugrad 2017 BIOC 263: Nutritional Biochemistry x 43 50 Ugrad 2017 BIOC 302: Biochemistry II for graduate students x 43 40 Grad 2017 BIOC 191: Undergraduate Research NA 3 Ugrad 2018 BIOC 263: Nutritional Biochemistry x 43 50 Ugrad 2018 BIOC 302: Biochemistry II for graduate students x 43 40 Grad 2018 BIOC 192: Undergraduate Research x NA 4 Ugrad 2018 BIOC 191: Undergraduate Research x NA 4 Ugrad 2019 BIOC 263: Nutritional Biochemistry x 43 40 Ugrad 2019 BIOC 192: Undergraduate Research x NA 4 Ugrad 2020 BIOC 263: Nutritional Biochemistry x 43 50 Ugrad 2020 BIOC 191: Undergraduate Research NA 5 Ugrad R-required; E-elective; Hours-approx. per semester; G-graduate studies (instruction as per the LCOM Teaching Academy Portfolio)

TEACHING: GRADUATE RESEARCH ROTATIONS In addition to my teaching duties listed in the table above, I have served as a rotation advisor for 20 graduate students both in the Department of Biochemistry and the UVM CMB program. Graduate students in both of these programs are required to perform three research rotations, write a research report on the accomplished research, and in some cases give an oral presentation about the reseach.


7

CURRICULUM DEVELOPMENT I have developed two courses de novo during my tenure at UVM. I first developed BIOC 207 (Biochemistry Laboratory for majors). The Undergraduate Biochemistry Program is a collaboration between three colleges within the University, LCOM, CALS, and CAS. During my first year I was assigned the task of developing this course for deployment in the Fall of 2003. There was no existing infrastructure for this course at UVM prior to my arrival. This required that I determine the curriculum for the course, the equipment that needed to be purchased for the experiments, and then to test each experiment. We spent nearly $100,000 in the first year to properly equip the laboratory. For the first semester we opted for a hybrid-laboratory model in which 3/4 of the semester used a traditional laboratory manual with lab reports handed in each week and the last 1/4 of the semester formed a module of experiments centered on ATP phosphoribosyltransferase. Part of their course grade was based on a scientific paper the students had to write. he assigned teaching assistant and I spent significant time in the Summer of 2003 testing and refining each experiment. Later, the lab was refined so that all of the experiments revolved around characterization of lactate dehydrogenase. The course culminated with each student having to write a Biochemistry-style paper summarizing all of their results. The course is designed to provide a “real world” experience for our students. In the fall of 2015, the Department of Biochemistry was approached by the Chair of Nutrition and Food Sciences about taking over NFS 263 – Nutritional Biochemistry, as a NFS faculty member had recently retired and NFS did not have anyone to teach the course. I volunteered for the job. The course is now listed as BIOC 263 – Nutritional Biochemistry. While I had the old syllabus, it only provided a rough guide about how to approach topics in the course. I decided to completely revamp the course and it is now taught on a thematic basis in terms of various popular diets such as the Mediterranean Diet and the Atkins Diet. These popular diets provide a platform to teach about fundamentals of human metabolism. Along the way, the biochemistry of all of the vitamins and many of the important minerals are discussed. I have now taught the course from 2015 until the present time with very strong student reviews. PREDOCTORAL STUDENTS SUPERVISED OR MENTORED

Dates Name Program School

Role Current Position

2002 Ethan Guth Biochemistry Doctoral student Research Rotation Mentor

Assoc. Prof. Biochem. Norwich University

2003 Marquis St. John Biochemistry Doctoral student Research Rotation Mentor

Instructor of Chemistry, St. Michael’s College, VT

2003-2007 Brian Eckenroth Biochemistry Doctoral student Ph.D. Thesis Advisor

Faculty Scientist, UVM MMG

2003 Brian Eckenroth Biochemistry Doctoral student Research Rotation Mentor

Faculty Scientist, UVM MMG

Summer 2003 & 2004

Adam Lothrop St. Michael’s College, VT summer student - Research Mentor

high school teacher, MA

2004 Brian Lacey Biochemistry Doctoral student Research Rotation Mentor

Lab manager, Merck Laboratories

2004-2007 Brian Lacey Biochemistry M.S. student M.S. Thesis Lab manager, Merck


8

Advisor Laboratories Summer 2004

Kevin Laxton Oregon State University undergraduate

summer student - Research Mentor

unknown

2004 Jon Ramsey Biochemistry Doctoral student Research Rotation Mentor

Faculty Scientist, UVM Biochemistry

2004 Shaina Byrne Biochemistry Doctoral student Research Rotation Mentor

unknown

2004 Nicolas James Biochemistry Doctoral student Research Rotation Mentor

Assist. Prof. Univ. Hawaii

2005-2006 Erin Chicoine Undergraduate student, UVM Biochemistry

Research Mentor Graduated from University of Texas Health Sciences Center at San Antonio, M.D. 2016

2005-2006 Dov Pechenick Undergraduate student, UVM Biochemistry

Undergraduate Thesis Advisor

Dartmouth University, Ph. D. candidate

2005-2011 Adam Lothrop Biochemistry Doctoral student Ph.D. Thesis Advisor

high school teacher, MA

2006 Amy Brannagan Biochemistry Doctoral student Research Rotation Mentor

unknown

2007 Todd Byrne Biochemistry Doctoral student Research Rotation Mentor

unknown

SP 2007 Alejandro Lopez Undergraduate student, UVM Biochemistry

Research Mentor unknown

2007-2008 Christine Fitzsimmons

Undergraduate student, UVM MMG

Research Mentor Graduated from University of New England 2012, D.O.

2008 Sarah Abdallah Biochemistry Doctoral student Research Rotation Mentor

unknown

2008-2009 Lauren Kopec Undergraduate student, UVM Biochemistry


2008 Gregg Snyder Biochemistry Doctoral student Research Rotation Mentor

Anesthesiology assistant, GA

2008-2012 Gregg Snyder Biochemistry Doctoral student Ph.D. Thesis Advisor

Anesthesiology assistant, GA

2009-2010 Adam Wespiser Undergraduate student, UVM Biochemistry

Research Mentor Ph.D. candidate, University of Massachusetts

2010 Adam Mirando Biochemistry Doctoral student Research Rotation Mentor

unknown

F 2010 Alysha Desrosiers

Undergraduate student, UVM MMG


unknown

Summer 2009

Leah Grout Undergraduate student, UVM Biochemistry


unknown

2010-2012 Evan Cooper Undergraduate student, UVM Chemistry


2010-2012 Andrew Geissler Undergraduate student, UVM Biochemistry


Graduated from University of New England 2016, D.O.

SP 2011 Elizabeth Lagasse

Undergraduate student, UVM Biochemistry


2011 Francis Ayombil Biochemistry Doctoral student Research Rotation Mentor

Post-doc, University of Pennsylvania

2011 Chase Haven Biochemistry Doctoral student Research Rotation unknown


9

Mentor 2011-2012 Katherine

Steblenko Undergraduate student, UVM Biochemistry


2011-2013 Patrick Plociennik



F 2012 Matt Henry Undergraduate student, UVM Biochemistry


2012-2014 Tiffany Dessain Undergraduate student, UVM Biochemistry


2013-2014 David Chen Undergraduate student, UVM, Chemistry

Research Mentor Ph.D. candidate University of Pittsburgh, chemistry

2013-2015 Zach Ehret Undergraduate student, UVM Biochemistry

Research Mentor Currently 4th year medical student at UVM LCOM

2013 Andrew Little CMB Doctoral student Research Rotation Mentor

unknown

2013 Vy Cao Undergraduate student, UVM Biochemistry

Research Mentor Currently employed as lab technician UVM LCOM

2013 Marcella Melloni Undergraduate student, UVM Biochemistry


2013 Drew Barber CMB Doctoral student Research Rotation Mentor

Post-doctoral scientist, SUNY-Buffalo

2013-2018 Drew Barber CMB Doctoral student Ph.D. Thesis Advisor

Post-doctoral scientist, SUNY-Buffalo

2014 Christopher Dustin

CMB Doctoral student Research Rotation Mentor

Ph.D. candidate UVM CMB

F 2014 Anes Karic Undergraduate student, UVM Biochemistry


Sp 2014 Riley Harding Undergraduate student, UVM Biochemistry


2014-2015 John O’Keefe Undergraduate, UVM Biohemistry Undergraduate Thesis Advisor

Currently 2nd year medical student at UVM LCOM

2014-2017 Connor Payne Undergraduate, UVM Chemistry Undergraduate Thesis Advisor

Harvard University, chemistry Ph.D. candidate

2015-present

Emma Ste.Marie Chemistry Doctoral student Ph.D. Thesis Advisor

Current student

2016-2017 Patrick Stroble Undergraduate student, UVM Chemistry

Research Mentor Currently high school teacher in Vermont

2016-2018 Aileen Button Undergraduate student, UVM Biochemistry


Ph.D.student at UCSD

Sp 2017 Hannah Aube Undergraduate student, UVM Chemistry

Research Mentor Unknown

Sp & Summer 2017

Andrew Fuchs Undergraduate student, UVM Chemistry

Research Mentor Current UVM student


10

2016-2018 Leonid Povolotskiy


Research Mentor Currently Ph.D. candidate in biochemistry at University of New Hampshire

2017-2018 Roshi Brooklyn Undergraduate student, UVM Biochemistry


2017-2018 Lucas Bennet Undergraduate student, UVM Chemistry


2017-2018 Matthew Murphy Undergraduate student, UVM Biochemistry


2017-2019 Aiden Collentine Undergraduate student, UVM Biochemistry


2017-2019 Mike Hoaglund Undergraduate student, UVM Biochemistry


2017 - current

Kaelyn Jenny Undergraduate student, UVM Chemistry

Research Mentor Current student

2018 Sean Lenahan CMB Doctoral student Research Rotation Mentor


2018 - current

Gracyn Mose Undergraduate student, UVM Biochemistry


Current UVM student

2018 - current

Linnea Saunders Undergraduate student, UVM Biochemistry


Current UVM student

2018 - current

Ian Sturm Undergraduate student, UVM MMG


2019 - current

Riley Forbes Undergraduate student, UVM Biochemistry


2019 Emily Joyce CMB Doctoral student Research Rotation Mentor


2019 Michelle Wheater

Biochemistry M.S. student Research Rotation Mentor

Current UVM student

2020 Daniel Haupt Chemistry M.S. student Research Mentor Current UVM student DISSERTATION/THESIS COMMITTEE MEMBERSHIP

Dates Name Program School

Role Current Position

2004 Kevin DeSisto Ph.D. candidate UVM Chemistry Committee Chair unknown 2004 Peter Halbrooks Ph.D. candidate UVM

Biochemistry Committee Member unknown

2005 Joon-Hee Han Ph.D. candidate UVM MMG Committee Chair unknown 2005 Matthew Hogg Ph.D. candidate UVM CMB Committee Chair unknown 2006 Alexander

Wurthman Ph.D. candidate UVM Chemistry Committee Chair Chemistry Instructor,

UVM Chemistry 2006 Elise Piscitelli Honors thesis UVM Biochemistry Committee Member unknown 2007 Snigdha Roy Ph.D. candidate UVM MMG Committee Chair unknown 2008 Ethan Guth Ph.D. candidate UVM

Biochemistry Committee Member Assoc. Prof.

Biochem. Norwhich University

2010 Krista Brooks Ph.D. candidate UVM MMG Committee Chair unknown 2012 Amy Brannagan Ph.D. candidate UVM


2012 Matthew Randall M.S. candidate UVM Pathology Committee Chair unknown


11

2012 Matthew Whelihan

Ph.D. candidate UVM Biochemistry

Committee Member Unknown

2012 Sunandan Banerjee

Ph.D. candidate UVM Chemistry Committee Member unknown

2012 Sara Abdalla M.S. candidate UVM Biochemistry

Committee Member unknown

2012 Phillip Laquer Honors thesis UVM Biochemistry Committee Member unknown 2014 Brian Cunniff Ph.D. candidate UVM CMB Committee Chair Assist. Prof. UVM

Pathology 2015 Adam Mirando Ph.D. candidate UVM


2016 Liam Kelley Honors thesis UVM Biochemistry Committee Member Medical Resident UVMMC

2017 Jared Hammer M.S. candidate UVM Biochemistry


2018 Patrick Wiencek M.S. candidate UVM Biochemistry


2020 (expected)

Christopher Dustin

Ph.D. candidate UVM CMB Committee Chair Current student

2020 (expected)

Daniel Haupt M.S. candidate UVM Chemistry Committee Member Current student

2020 (expected)

Robert Wehrle Ph.D. candidate USM Chemistry Committee Member Current student

UNDERGRADUATE ACADEMIC ADVISEES

Academic Year Name Major 2005-2006 Dolgin, Rachel L. BS Chemistry

2005-2006 Fabricant, Seth A. BS Biochemistry

2005-2006 Izzo, Cheri B. BS Biochemistry

2005-2006 Sackheim, Adrian M. BS Biochemistry

2006-2007 Dolgin, Rachel L. BA Anthropology

2006-2007 Fabricant, Seth A. BS Biochemistry


2006-2007 Sackheim, Adrian M. BS Biochemistry



2007-2008 Wolanski, Lisa J. BS Biochemistry


2008-2009 Kirkpatrick, Caroline V. BS Biological Sciences

2008-2009 Kopec, Lauren L. BS Biochemistry

2008-2009 Lamprey, Hannah, E. BS Biochemistry

2008-2009 Maile, Nicole M. BS Biochemistry

2009-2010 Benn, Robert Austin B. BS Biochemistry


12

2009-2010 Cason, Christopher BS Biochemistry



2010-2011 Cluett, Cordelia Z. BS Biochemistry

2010-2011 Foelber, Veronica L. BS Biochemistry


2010-2011 Tran, Huy Q. BS Biochemistry

2010-2011 Webb, Rebecca L. BA Biology


2011-2012 Foelber, Veronica L. BS Biochemistry

2011-2012 Geissler, Andrew W. BS Biochemistry

2011-2012 Gorruso, Robert E. Undeclared

2011-2012 Hannan, Taylor C. Undeclared

2011-2012 Lane, Joshua M. BS Biochemistry

2011-2012 Plociennik, Patrick C. BS Biochemistry




2013-2014 Duncan, Jack C. BS Biochemistry

2013-2014 Harding, Riley S. BS Biochemistry



2014-2015 Button, Aileen C. BS Biochemistry

2014-2015 Ehret, Zachary W. BS Biochemistry

2014-2015 Hanna, Sebastian S. BS Biochemistry


2014-2015 von Eynern, Addi BS Biochemistry





2016-2017 Crymble, Hanna BS Biochemistry

2016-2017 Goodrich, Emily BS Biochemistry




13




POSTDOCTORAL FELLOWS AND RESIDENTS DIRECTLY SUPERVISED OR MENTORED

Dates Name Fellow Faculty Role Current Position 2003-2007 Dr. Erik Rugles Postdoctoral Fellow Research Mentor Instructor, UVM

Chemistry 2004-2005 Dr. P. Bruce Deker Postdoctoral Fellow Research Mentor retired FACULTY MENTORED Years Names University/College Role 2005 Dr. Roger Sandwick Middlebury College VGN Mentor OTHER VISITING FACULTY SUPERVISED Years Names University/College Role 2006-2007 Dr. Alayne Schroll St. Michael’s College, VT Sabbatical Mentor 2018 Dr. Kathleen Rein Florida International University Sabbatical Mentor TEACHING AWARDS AND NOMINATIONS Year Award 2011 Nominee for the UVM Graduate Student Senate Excellence in Teaching Award 2015 Nominee for the Kroepsch-Maurice Excellence in Teaching Award 2018 Nominee for the Kroepsch-Maurice Excellence in Teaching Award Teaching portfolio avaialable on request or attached (if appropriate)

SUMMARY OF TEACHING ACTIVITIES

As detailed in the Tables above, I have taught nearly every undergraduate and graduate course that the Department of Biochemistry has to offer. I have developed two of our course offerings de novo (e.g. these courses didn’t exist prior to my efforts). I have been nominated for teaching awards at both the undergraduate and graduate levels, but have not won an award for teaching. Besides didactic courses, I have taught at the lab bench as evidenced by the many undergraduate and graduate students who have trained under my directions (especially undergraduates). I have also supervised post-doctoral scientists and visiting faculty. In addition I have served as the faculty academic advisor for numerous undergraduate students as listed above.


14

RESEARCH AND SCHOLARLY ACTIVITIES

RESEARCH AWARDS AND GRANTS Ongoing Research Support R01 HL141146 Hondal and Day (multi-PI) 01/01/19 – 11/30/22 Selenocyanate as a novel treatment of cystic fibrosis lung disease The proposal has three specific aims: (i) Specific aim 1 will determine the chemical mechanism by which Sec-containing TrxR resists inactivation by HOSCN/HOSeCN oxidation and Cys-containing TrxR are inactivated by HOSCN/HOSeCN. (ii) Specific aim 2 will examine CFTR’s and Sec-TrxR’s role in the importance of –SCN/HOSCN -mediated lung host defense against bacterial infection. (iii) Specific aim 3 is designed to examine –SeCN as a potential therapy for treatment of lung inflammation and infection using wild type and CFTR KO and β-ENaC Tg mouse models Role: PI Direct Costs Year 1: $16007 Total Period: $424,028 Completed Research Support R01 ES021476-01 van der Vliet (PI) 07/01/12 – 06/30/17 Cigarette smoke-derived electrophilic aldehydes in airway inflammation The goal of this project is to clarify the cellular mechanisms by which acrolein inhalation alters innate or adaptive immune responses in the lung, by application of proteomic strategies to identify direct molecular targets for acrolein and/or alterations in redox signaling pathways. Role: Co-PI UVM REACH Bouchard (PI) 01/01/16 – 08/31/17 Development of a Novel Therapy for Hemophilia A The goal of this project are to: (i) Develop a sequence alignment map of orthologs to human factor V to identify important regions, (ii) Identify E9:factor V interactions by limited proteolysis, and (iii) Synthesize a peptide library of overlapping E9 and factor V peptides that will help further refine binding interactions. My role as the co-PI is to help synthesize peptides for the third aim. Role: Co-PI UVM LCOM Bridge Funding Hondal(PI) 01/01/16 – 12/31/17 The Role of Selenium-Thioredoxin Reductase in Cystic Fibrosis The goal of this project was to build enough preliminary data to fund a NIH grant application on the function of thioredoxin reductase in cystic fibrosis. This award led to the my current R01 funding. Role: PI Total Award: $50,000


15

Contract with Cornell College

Hondal (PI) 10/01/16

Synthesis of selenopeptides to treat stroke The goal of this project is to synthesize the contracted peptides. Role: PI Direct Costs: $4,000 R01 GM094172 Hondal (PI) 9/1/10 – 8/31/14 The Biological and Chemical Function of Selenium in Enzymes The major goals of this project are: (1) compare the ability of Sec-enzymes and Cys-enzymes to resist inactivation by oxidation, (2) determine the rate limiting step of the enzymatic reaction mechanism in TR and, (3) determine the ability of Sec-TR and Cys-TR to resist oxidation in vivo. Role: PI Direct Costs Year 1: $210,000 Total Period: $840,000 Supplement to R01 GM070742 Hondal (PI) 9/28/09 – 3/31/10 Selenium-Thioredoxin Reductase Studies by Semisynthesis

The goals of this supplement are to (1) characterize how cis/trans isomerization of a Cys-Cys dyad effects ligand binding to the nicotine acetylcholine receptor (2) determine the conformation of the C-terminal disulfide of PfTR by NMR. Role: PI Direct Costs Year 1: $51,500 Total Period: $51,500 R01 GM070742 Hondal (PI) 4/1/04 – 3/31/09 Selenium-Thioredoxin Reductase Studies by Semisynthesis

The major goals of this project are (i) make small molecule mimics of TR active site (ii) produce a semisynthetic TR (iii) characterize a cysteine-TR. Role: PI Direct Costs Year 1: $187,500 Total Period: $750,000


16

DE-FG02-00ER45828 Wallace (PI) 08/01/02 - 06/30/03 DOE EPSCoR Initiative in Structural Biology and Computational Biology/Bioinformatics This project was part of the structural biology initiative at UVM. My role was to start projects related to NMR spectroscopy. Role: co-PI Direct Costs Year 1: $112,000 Total Period: $112,000 DE-FG02-00ER45828 Wallace (PI) 7/1/03 – 6/30/05 Structural Studies of Mammalian Thioredoxin Reductase The goal of this project was to crystallize a truncated form of TR with a synthetic peptide substrate. We published the structure of D. melanogaster TR in Biochemistry as a result of these funds. Role: co-PI Direct Costs Year 1: $70,000 Total Period: $70,000 NIH/NIGMS NRSA F32 GM20180 Raines (PI) 7/1/99 – 12/31/02 Synthesis of PDI Mimics This project involved synthesizing small molecules that mimicked the action of the enzyme protein disulfide isomerase (PDI). These molecules were then characterized by various biophysical techniques and subsequently tested for their ability to replace PDI in yeast knockouts. Role: post-doctoral fellow

Instrumentation Grants •S10 RR017743-01 (Mann, PI) 03/01/04 NIH Shared Instrumentation Grant – Symphony Multiplex Peptide Synthesizer w/VISION Workstation NIH $179,094 This money was used to purchase a Symphony peptide synthesizer and two HPLC systems. This instrumentation was used to starte the UVM Peptide Core Facility. I was the director of this facility until 2009. Role: co-PI

•Small Equipment Grant from Vermont EPSCoR (Hondal, PI) 10/01/05 Vermont EPSCoR $12,079 Lyophilizer for Use in Making Proteins by Total Chemical Synthesis.


17

•CHE – MAJOR RESEARCH INSTRUMENTATION (Matthews, PI) 08/01/11 NSF $535,000 MRI: Acquisition of a 500 MHz NMR Spectrometer for Chemistry at the University of Vermont Project 3: Effect of cis/trans isomerization of a Vicinal Disulfide Bond on the Nicotinic Acetylcholine Receptor (nAChR) Role: Project leader

•S10 OD018126-01 (Matthews, PI) 07/01/14 NIH Shared Instrumentation Grant – A Waters Xevo G2-S QTOF LC/MS for UVM NIH $461,000 Project 3: Biological and Chemical Function of Selenium in Enzymes Role: Major user •CHE – MAJOR RESEARCH INSTRUMENTATION (Waterman, PI) 09/01/19 NSF $387,260 MRI: Acquisition of an EPR Spectrometer at the University of Vermont Project 7: One-electron reactions of selenium-compounds. Role: Part-time user

Mentored Grants – These are grants awarded to students for research under my direction and mentorship.

•DOE/EPSCoR Graduate Research Fellowship 07/01/05 – 06/30/07 $40,100 Structure Determination of Mouse Thioredoxin Reductase-3 and the Thioredoxin Reductase/Thioredoxin Complex by X-Ray Crystallography. Brian E. Eckenroth was awarded a two-year graduate fellowship by the Structural Biology Initiative of DOE/EPSCoR to continue work on the crystal structure of mTR3 and the mTR3/thioredoxin complex.

•RUBY Summer 2004 $5,000 Synthesis of a Phosphorothioate Substrate Analog to Investigate the Role of His119 of RNase A in Catalysis. This grant was funded for $5,000 dollars to Adam Lothrop (St. Michael’s College, Colchester, VT) The program was entitled RUBY, which stands for Research Undergraduates in your Back Yard. This grant paid Adam a salary of $3,500 for the summer and my lab received $1,500 for supplies for this project. The purpose of this program was to attract Vermont students to UVM for graduate studies. Adam was required to write a mini-grant in order to obtain funding.


18

•HELiX Summer 2005 $5,000 Crystallization of Thioredoxin Reductase/Thioredoxin Complex. This grant was funded by HELiX for Ms. Erin Chicoine (UVM) to work in my lab for the summer of 2005. Erin worked on crystallizing the TR/Trx complex. HELiX stands for Hughes Endeavor for Life Science Excellence. The HELiX program is designed to support students doing undergraduate research and provides funding for the summer and academic year research. This is a highly competitive program and students are required to write a mini-grant that is reviewed by a panel to obtain funding.

•URECA! Spring 2006 $4,000 Biosynthesis of Selenocysteine using O-Acetylserine Sulfhydrylase. Dov Pechenick was funded by URECA! (Undergraduate Research Endeavors Competitive Awards) to do his his honors thesis in my laboratory. The goals of this project were to: (i) clone O-acetylserine sulfhydrylase, (ii) Use this enzyme to make the amino acid selenocysteine biosynthetically. The entire award was used for supplies for this project.

•VGN 06/01/06 – 05/31/07 $10,000 Synthesis, Characterization, and Use of New Selenocysteine Derivatives. Dr. Alayne Schroll, St. Michael’s College applied for sabbatical research support to work in my laboratory during the 2006-07 academic year from the Vermont Genetics Network (VGN). Dr. Schroll and I worked jointly on this proposal as part of a broader proposal we subsequently submitted to the National Science Foundation (NSF). This grant was funded for $10,000.

•URECA! Summer 2013 $2,902 Making Sulfur Behave Like Selenium: The Synthesis of Trifluoromethionine. Patrick Polciennik was funded by URECA! (Undergraduate Research Endeavors Competitive Awards) to do research in the summer of 2013. The goal of the project is to show that a sulfur-containing compound can behave like a selenium-containing compound with respect to redox behavior by making the sulfur atom electron deficient. This has applications for uses as a peptide based redox sensor.

•UVM Office of Undergraduate Research Summer 2015 $1,791 Summer Research Award: A possible treatment for cystic fibrosis and COPD: Development of new mucolytic agents based on a recombinant enzyme and diselenide compounds. Neil Connor Payne was funded by UVM OUR for the summer of 2015 for a project to develop a new mucolytic system for depolymerizing mucin proteins using thioredoxin reductase and diselenide compounds. It is hoped that this system will be catalytic and superior to standard exogenous thiol depolymerization of mucin proteins.

UVM Office of Undergraduate Research Summer 2017 $5,000 Summer Research Award: The Importance of a Structural Hydrogen-Bond to Catalysis in Thioredoxin Reductase Leonid Povolotskiy was funded by UVM OUR for the summer of 2017 to test the hypothesis that an important hydrogen bond in a b-turn-b motif stabilizes the cis form of the vicinal disulfide ring, enabling efficient catalysis to occur.


19

UVM Office of Fellowships, Opportunities, and Undergraduate Research Summer 2018 $4,915 Summer Research Award: Effect of the Antibiotic Thiostrepton on Thioredoxin Reductase Activity Aiden Collentine was funded by UVM FOUR for the summer of 2018 to determine the site of thiostrepton binding to mammalian thioredoxin reductase by growing crystals of the enzyme in the presence of thiostrepton and then attempting to solve the X-ray crystal structure. Pending

American Heart Association: 2020 Collaborative Sciences Award - 20CSA35320087

Bouchard and Hondal (co-PIs)

7/1/20 – 6/30/23

Development of appropriate, targeted therapies to prevent thrombosis by modulation of platelet FV/Va levels The major goal of this project is to develop appropriate, targeted therapies to prevent thrombosis by modulation of platelet factor V/Va levels. Role: co-PI Direct Costs Year 1: $250,000 Total Period: $750,000 Selected Unfunded Grant Submissions NSF 1607666 Hondal and Masteron (co-PIs) Submitted: 10/28/15 – declined Applications of a selenocysteine derivative: peptide technologies and enzyme mechanism The goals of this application were to: (i) Develop a chemoselective method for deprotecting S-5-nitro-2-pyridine-sulfenyl-cysteine (Cys(5-Npys)) and Se-5-nitro-2-pyridine-sulfenyl-selenocysteine (Sec(5-Npys)), (ii) Develop a scalable, facile synthetic procedure for the production of αMeSec, (iii) Use αMeSec to determine the redox state of the active site Sec residue of mammalian thioredoxin reductase (TR) that the enzyme uses to avoid oxidative inactivation, and (iv) Address the question of how do Cys-orthologs of Sec-enzymes function (compensate) without the presence of the more reactive selenium atom? Role: co-PI $700,161


20

NSF 1708569 Hondal and Sheng (co-PIs) Submitted: 10/28/16 – declined The function of selenium in RNA The goal of this application was to test the following hypotheses: (i) Oxidation of 2-thiouridine by H2O2 results in desulfurization and conversion of 2-thiouridine to uridine, leading to impaired function of the tRNA and transduction of a stress signal. In contrast 2-selenouridine resists deselenization when oxidized by H2O2, (ii) Selenium protects tRNA from strand scission by •OH because the selanyl radical is more stabile and more readily repaired than the corresponding thiyl radical, (iii) E. coli responds to oxidative stress by increasing the ratio of selenouridine to thiouridine as an antioxidant defense mechanism, (iv) 2-selenouridine is important for translating important antioxidant proteins. Role: co-PI $782,970 NSF 1904485 Hondal and Wargo (co-PIs) Submitted: 10/30/18 – declined Biology and chemistry of cyclic selenoureas The goal of this application was to test the hypotheses that: (i) analogous to enzymes, selenium in 2-selenouridine and selenoneine, confers resistance to oxidative inactivation such that the biological function of the molecule is maintained and, (ii) oxidation of selenium in 2-selenouridine and selenoneine leads to much faster elimination of selenium from the selenourea compared to sulfur from thiourea. Elimination of selenium would serve to alter the structure and biological function of the molecule, possibly in a type of signaling pathway Role: co-PI $810,893 R01 ES031159 Hondal and Rein (multi-PI) Submitted: 02/05/19 unscored Exposure to brevetoxins, thioredoxin reductase effectors from the Florida Red Tide as a model for electrophilic stress: Molecular mechanism of collateral effects and reactivity based intervention. The goal of this application was to: (i) Determine the chemical mechanism by which PbTx-2 inhibits/activates hTrxR-1/-2 and K. brevis TrxR, (ii) Test the hypothesis that Sec-containing TrxR resists permanent inactivation by electrophiles such as PbTx-2, (iii) Test the alternate hypotheses that PbTx-2 induces inflammatory pathways in human alveolar macrophages and pulmonary epithelial cells via (i) TrxR induced oxidative stress or (ii) sodium channel activation, and (iv) Evaluate the effectiveness of acrolein scavengers, including three approved drugs and derivatives, in reducing the cytotoxicity of PbTx-2. Role: multi-PI $1,829,636


21

SCHOLARSHIP Original Research

1. Hondal RJ & Ulsh RC. (1992) Studies on the Coprophageal Behavior of the Domestic Rabbit Using Adiabatic Calorimetry. J. Penn. Acad. Sci. 66, 107-110.

2. Werneburg BG, Ahn J, Zhong X, Hondal RJ, Kraynov VS, & Tsai M.-D. (1996) DNA Polymerase b: Pre-Steady-State Kinetic Analysis and Roles of Arginine-283 in Catalysis and Fidelity: Biochemistry 35, 7041-50.

3. Hondal RJ, Zhao Z, Riddle SR, Kravchuk AV, Liao H, Bruzik KS, & Tsai. M.-D. (1997) Phosphatidylinositol-specific Phospholipase C. 3. Elucidation of the catalytic mechanism and comparison with ribonuclease A. J. Am. Chem. Soc. 119, 9933-9934.

4. Hondal RJ, Bruzik KS, Zhao Z, & Tsai M.-D. (1997) Mechanism of Phosphatidylinositol-Phospholipase C. 2. Reversal of a Thio Effect by Site-Directed Mutagenesis. J. Am. Chem. Soc. 119, 5477-5478.

5. Hondal RJ, Riddle SR, Kravchuk AV, Zhao Z, Liao H, Bruzik KS, & Tsai M.-D. (1997) Phosphatidylinositol phospholipase C: Kinetic and stereochemical evidence for an interaction between arginine-69 and the phosphate group of phosphatidylinositol. Biochemistry 36, 6633-6642.

6. Hondal RJ, Zhao Z, Kravchuk AV, Liao H, Riddle SR, Bruzik KS, & Tsai M.-D. (1998) Mechanism of phosphatidylinositol-specific phospholipase C: A unified view of the mechanism of catalysis" Biochemistry 37, 4568-4580.

7. Kubiak RJ, Hondal RJ, Yue X, Tsai M.-D., & Bruzik KS. (1999) Identification of a novel catalytic triad with dual functions in enzymatic cleavage of the P-O Bond. J. Am. Chem. Soc. 121, 488-489.

8. Hondal RJ, Motley AK, Hill KE, & Burk RF. (1999) Failure of selenomethionine residues in albumin and immunoglobulin G to protect against peroxynitrite. Arch. Biochem. Biophys. 371, 29-34.

9. Hondal RJ, Ma, S Caprioli RM, Hill KE, & Burk RF. (2001) Heparin-binding histidine and lysine residues of rat selenoprotein P. J. Biol. Chem. 276, 15823-15831.

10. Hondal RJ, Nilsson BL, & Raines RT, (2001) Selenocysteine in native chemical ligation and expressed protein ligation. J. Am Chem. Soc. 123, 5140-5141.

11. Kubiak RJ, Yue X, Hondal RJ, Mihai C, Tsai M.-D., & Bruzik K.S.(2001) Involvement of the Arg-Asp-His Catalytic Triad in Enzymatic Cleavage of the Phosphodiester Bond. Biochemistry 40, 5422-5432.

12. Hondal RJ, & Raines RT. (2002) Semisynthesis of proteins containing selenocysteine. Methods Enzymol. 347, 70-83.

13. Nilsson BL, Hondal RJ, Soellner MB, & Raines RT. (2003) Protein assembly by orthogonal chemical ligation methods. J. Am Chem. Soc. 125, 5268-5269.

14. Lacey BM, & Hondal RJ. (2006) Characterization of mitochondrial thioredoxin reductase from C. elegans. Biochem. Biophys. Res. Commun. 346, 629-636. PMCID: PMC3687220

15. Ruggles EL, & Hondal RJ. (2006) Synthesis and properties of disulfide-bond containing eight-membered rings. Tet. Lett. 47, 4281-4284. PMCID: PMC3698869


22

16. Eckenroth BE, Harris K, Turanov AA, Gladyshev VN, Raines RT, & Hondal, RJ. (2006)

Semisynthesis and characterization of mammalian thioredoxin reductase. Biochemistry 45, 5158-5170. PMCID: PMC2570056

17. Harris KM, Flemer S & Hondal RJ. (2007) Studies on deprotection of cysteine and selenocysteine side chain protecting groups. J. Pept. Sci 13, 81-93. PMCID: PMC3689433

18. Eckenroth BE, Rould MA, Hondal RJ, & Everse SJ (2007) Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases. Biochemistry 46, 4694-4705. PMCID: PMC3687216

19. Eckenroth BE, Lacey BM, Lothrop AP, Harris KM, & Hondal RJ (2007) Investigation of the C-terminal redox center of high Mr thioredoxin reductases by protein engineering and semisynthesis. Biochemistry 46, 9472-9483. PMCID: PMC3682222

20. Flemer SJ, Lacey BM & Hondal RJ (2008) Synthesis of peptide substrates for mammalian thioredoxin reductase. J. Pept. Sci. 14, 637-47. PMCID: PMC3690199

21. Ruggles EL, Flemer SJ, & Hondal RJ (2008) A viable synthesis of N-methyl cysteine. Biopolymers 90, 61-68. PMCID: PMC3691851

22. Lacey BM, Flemer SJ, Eckenroth BE, & Hondal RJ (2008) Selenium in thioredoxin reductase: A mechanistic perspective. Biochemistry 47, 12810-12821. PMCID: PMC3682215

23. Ruggles EL, Deker PB, & Hondal RJ. (2009) Synthesis, redox properties, and conformational analysis of vicinal disulfide ring mimics. Tetrahedron 65, 1257-1267. PMCID: PMC3653589

24. Lothrop, AP, Ruggles, EL, & Hondal RJ. (2009) No selenium required: Reactions catalyzed by mammalian thioredoxin reductase that are independent of a selenocysteine residue. Biochemistry.48, 6213–6223. PMCID: PMC2754045

25. Snider G, Grout L, Ruggles EL, & Hondal RJ (2010) Methaneseleninic acid is a substrate for truncated thioredoxin reductase: Implications for the catalytic mechanism and redox signaling. Biochemistry 49, 10329-10338. PMCID: PMC3018153

26. Spiess PC, Deng B, Matthews DE, Hondal RJ, van der Vliet A (2011) Proteomic profiling of acrolein adducts in human lung epithelial cells. J. Proteomics 74, 2380-2394. PMCID: PMC3196826

27. Schroll AL, Hondal RJ, & Flemer S. Jr (2012) 2,2’ Dithiobis(5-nitropyridine) (DTNP) as an effective and gentle deprotectant for common cysteine protecting groups. J. Pept. Sci. 18, 1-9. PMCID: PMC3289972

28. Schroll AL, Hondal RJ, & Flemer S. Jr (2012) The use of 2,2’ dithiobis(5-nitropyridine) (DTNP) for deprotection and diselenide formation in protected selenocysteine-containing peptides. J. Pept. Sci. 18, 155-162. PMCID: PMC3437994

29. Randall MJ, Spiess PC, Hristova M, Hondal RJ, & van der Vliet, A. (2013) Acrolein-induced activation of mitogen-activated protein kinase signaling is mediated by alkylation of thioredoxin reductase and thioredoxin 1. Redox Biology 1, 265-275. PMCID: PMC3757691


23

30. Chandler JD, Nichols DP, Nick JA, Hondal RJ, & Day, BJ. (2013) Selective metabolism

of hypothiocyanous acid by mammalian thioredoxin reductase promotes lung innate immunity and antioxidant defense. J. Biol. Chem.288, 18421-18428. PMCID: PMC3689984

31. Snider GW, Ruggles EL, Khan N, & Hondal RJ. (2013) Selenocysteine confers resistance to inactivation by oxidation in thioredoxin reductase: Comparison of selenium and sulfur enzymes. Biochemistry 52, 5472-5481. PMCID: PMC3760785

32. Cunniff B, Snider GW, Fredette N, Hondal RJ & Heintz N. (2013) A direct and continuous assay for the determination of thioredoxin reductase activity in cell lysates. Anal Biochem 443, 34-40. PMCID: PMC3839276

33. Lothrop AP, Snider GW, Flemer S. Jr., Ruggles EL, Davidson RS, Lamb A, & Hondal RJ. (2014) Compensating for the absence of selenocysteine in high Mr thioredoxin reductases: The electrophilic activation hypothesis, Biochemistry 53, 664-674. PMCID: PMC3931472

34. Cunniff B, Snider GW, Fredette N, Stumpff J, Hondal RJ & Heintz N. (2014) Resolution of oxidative stress by thioredoxin reductase: cysteine versus selenocysteine. Redox Biology 2, 475-484. PMCID: PMC3949094

35. Lothrop AP, Snider GW, Ruggles EL, & Hondal RJ. (2014) Why is mammalian thioredoxin reductase-1 so dependent upon the use of selenium? Biochemistry 53, 554-564. PMCID: PMC3957196

36. Snider GW, Dustin CM, Ruggles EL, & Hondal RJ. (2014) A mechanistic investigation of the C-terminal redox motif of thioredoxin reductase from Plasmodium falciparum. Biochemistry 53, 601-609. PMCID: PMC3957191

37. Lothrop AP, Snider GW, Ruggles EL, Patel AS, Lees WJ, & Hondal RJ. (2014) Selenium as an electron acceptor during the catalytic mechanism of thioredoxin reductase, Biochemistry 53, 654-663. PMCID: PMC3957198

38. Ruggles EL, Deker PB, & Hondal RJ. (2014) Conformational analysis of oxidized peptide fragments of the C-terminal redox center in thioredoxin reductases by NMR spectroscopy. J. Pept. Sci. 20, 349-360. PMCID: PMC4000577

39. Ste.Marie E, Ruggles EL & Hondal RJ. (2016) Removal of The 5-nitro-2-pyridine-sulfenyl protecting group from selenocysteine and cysteine by ascorbolysis. J. Pept. Sci. 22, 571-576. PMCID: PMC5098394

40. Gladyshev VN, Arnér ES, Berry MJ, Brigelius-Flohé R, Bruford EA, Burk RF, Carlson, BA Castellano S, Chavatte L, Conrad M, Copeland PR, Diamond AM, Driscoll DM, Ferreiro A, Flohé L, Green FR, Guigó R, Handy DE, Hatfield DL, Hesketh J, Hoffmann PR, Holmgren A, Hondal RJ, Howard MT, Huang K, Kim H-Y, Ick Young Köhrle KJ, Krol A, Kryukov GV, Lee BJ, Lee BC, Lei XG, Liu Q, Lescure A, Lobanov AL, Loscalzo J, Maiorino M, Mariotti M, K. Prabhu KS, Rayman MP, Rozovsky S, Salinas G, Schomburg L, Schweizer U, Simonovic M, Sunde RA, Tsuji PA, Tweedie S, Ursini F, & Zhang Y. (2016) Selenoprotein gene nomenclature. J. Biol. Chem. 291, 24036-24040. PMCID: PMC5104929

41. Payne NC, Geissler A, Button A, Sasuclark AR, Schroll AL, Ruggles EL, Gladyshev VN & Hondal RJ. (2017) Comparison of the redox chemistry of sulfur and selenium-containing analogs of uracil. Free Radic. Biol. Med. 104, 249-261. PMCID: PMC5328918


24

42. Fredericks GJ, Hoffmann FW, Hondal RJ, Rozovsky S, Urschitz J, & Hoffmann PR.

(2017) Selenoprotein K increases efficiency of DHHC6 catalyzed palmitoylation by stabilizing the acyl-DHHC6 intermediate. Antioxidants 7, E4. PMCID: PMC5789314

43. O’Keefe JP, Dustin CM, Barber DR, Snider GW, & Hondal RJ (2018) A “seleno-effect” differentiates the roles of redox active cysteine residues in Plasmodium falciparum thioredoxin reductase. Biochemistry 57, 1767-1778. PMCID: PMC5866731

44. Ste.Marie E, & Hondal RJ. (2018) Reduction of cysteine-S-protecting groups by triisopropylsilane. J. Pept. Sci. 24, e3130.

45. Tuladhar A, Hondal RJ, Colon R, Hernandez EL, & Rein KS. (2019) Effectors of thioredoxin reductase: I Brevetoxins and manumycin A. Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology 217, 76-86.

46. Payne NC, Barber DR, Ruggles EL, & Hondal RJ (2019) Can dimedone be used to study selenoproteins? An investigation into the reactivity of dimedone towards oxidized forms of selenocysteine. Protein Sci. 28, 41-55.

47. Barber DR, & Hondal RJ (2019) Gain of function conferred by selenocysteine: Catalytic enhancement of one-electron transfer reactions by thioredoxin reductase. Protein Sci. 28, 79-89.

48. Alim I, Caulfield JT, Chen Y, Swarup V, Geschwind DH, Ivanova E, Seravalli J, Ai Y, Sansing LH, Hondal RJ, Ste. Marie E, Cave JW, Sagdullaev BT, Karuppagounder SS, & Ratan RR. (2019) Selenium induces an adaptive transcriptional response to inhibit ferroptosis and improve recovery after brain hemorrhage. Cell 177, 1262-1279.

49. Wehrle RJ, Ste.Marie E, Hondal RJ, & Masterson DS. (2019) Synthesis of alpha-methyl selenocysteine and its utilization as a glutathione peroxidase mimic. J. Pept. Sci. 25, e3173.

50. Jenny KA, Ste.Marie EJ, Mose G, Ruggles EL, & Hondal RJ. (2019) Facile removal of 4-methoxybenzyl protecting group from selenocysteine. J. Pept. Sci. e3209.

51. Ste.Marie E, & Hondal RJ. (2020) 2,2´-Dipyridyl diselenide: A chemoselective tool for cysteine deprotection and disulfide bond formation. J. Pept. Sci. 26, e3236.

52. Day BJ, Bratcher PE, Chandler, J, Kilgore M, Min E, LiPuma JJ, Hondal RJ, & Nichols DP. (2020) The thiocyanate analog selenocyanate is a more potent antimicrobial pro-drug that also is selectively detoxified by the host. Free Radic. Biol. Med. 146, 324-332.

In Review

In Preparation (Be judicious-list only those that you will submit in the near term)

1. Dustin CM and Hondal RJ (2020) Insertion of N-methylcysteine into D. melanogaster thioredoxin reductase: Effects on catalysis. In Preparation for Biochemistry.

2. Colon R, Ste.Marie EJ, Tuladhar A, Hondal RJ, & Rein KS. (2020) Mitochondrial thioredoxin reductase (TrxR-2) is resistant to inactivation by curcumin relative to the cytosolic form (TrxR-1). Submitted to Free Radic. Biol. Med.


25

Non-Peer Reviewed Publications Review Articles

1. Hondal RJ. (2005) Incorporation of selenocysteine into proteins using peptide ligation. Protein and Peptide Letters 12, 757-764. PMCID: PMC3683319

2. Hondal, RJ (2009) Using chemical approaches to study selenoproteins – focus on thioredoxin reductases. Biochim. Biophys. Acta 1790, 1501-1512. PMCID: PMC2818346

3. Hondal RJ, & Ruggles EL (2011) Differing views of the role of selenium in thioredoxin reductase. Amino Acids 41, 73-89. PMCID: PMC2935959

4. Hondal RJ, Marino SM, & Gladyshev, VN. (2013) Selenocysteine in thiol-disulfide-like exchange reactions. Antioxid Redox Signal 18, 1675-1689. PMCID: PMC3613276

5. Reich HJ & Hondal RJ. (2016) Why Nature chose selenium. ACS Chem. Biol. 11, 821-841.

6. Maroney MJ, and Hondal RJ (2018) Selenium versus sulfur: reversibility of chemical reactions and resistance to permanent oxidation in proteins and nucleic acids. Free Radic. Biol. Med. 127, 228-237.

Books and Chapters 1. Hondal RJ, Zhao Z, Kravchuk AV, Liao H, Riddle SR, Bruzik KS, & Tsai, M.-D.

(1998) The Mechanism of Phosphatidylinositol-Specific Phospholipase C Revealed by Protein Engineering and Thio-PI Analogs. In Phosphoinositides: Chemistry, Biochemistry and Biomedical Applications, K. S. Bruzik, Ed. ACS Symp. Ser. 718, 109-120.

2. Ruggles EL, Snider GW, & Hondal RJ (2012) Chemical basis for the use of selenocysteine. In Selenium: Its Molecular Biology and Role in Human Health. 3rd ed, D.L. Hatfield, M.J. Berry, V.N. Gladyshev, Eds. Pgs 73-83. Springer, New York.

Other Scholarly Publications– (Conference Proceedings and Newsletters)

1. Hondal RJ, and Schaeffer C. (1995) Preparation of competent cells using transformation and storage solution, Epicentre Forum 2, 5.

2. Harris KM & Hondal RJ. Deprotection of the p-methoxybenzyl group of selenocysteine by neighboring group participation. Understanding Biology Using Peptides: Proceedings of the 19th American Peptide Symposium (Sylvie E. Blondelle, Ed.). American Peptide Society, 2006. Produced by Springer, New York, pgs 91-92.

3. Flemer S & Hondal RJ. An efficient on-resin protocol for on-resin, vicinal disulfide formation: Applications to thioredoxin reductase (2009) Adv. Exp. Med. Biol. 611, 93-94.

4. Schroll A & Hondal RJ. Further development of new deprotection chemistry for cysteine and selenocysteine side chain protecting groups (2009) Adv. Exp. Med. Biol. 611, 135-136.

5. Flemer S, Schroll A, & Hondal RJ DTNP as a gentle and effective method of deprotection for side-chain protectants on commercially available Cys and Sec SPPS derivatives. Building Bridges: The Proceedings of the 22nd American Peptide Symposium (Michal Lebl, Ed.). American Peptide Society, 2011. Produced by Prompt Scientific Publishing, San Diego, CA, pgs 24-25.


26

Abstracts

1. Liao, H., Hondal, RJ, & Tsai, M.-D. Site-directed mutagenesis studies of phosphoatidylinositol-specific phospholipase C: the substrate binding residues. 17th International Congress of Biochemistry and Molecular Biology. Annual Meeting of the American Society for Biochemistry and Molecular Biology. San Francisco, CA. Aug. 24-29, (1997). Abstract #2628, pg A1307, FASEB Abstracts.

2. Hondal, RJ, Kravchuk, AV, & Tsai, M.-D. Using Protein Engineering and Thio-PI Analogs to Probe the Mechanism of PI-PLC. ACS National Meeting, Las Vegas, Nevada. (1997), AN1997:485974.

3. Hondal, RJ, Kravchuk, AV, & Tsai, M.-D. Using Protein Engineering and Thio-PI Analogs to Probe the Mechanism of PI-PLC. ACS National Meeting, Las Vegas, Nevada. (1997), AN1997:485974.

4. Hondal, RJ, & Burk, R. F. Evidence for Thiol Redox States of Selenoprotein P. Annual Meeting of the American Society for Experimental Biology. San Francisco, CA. April 18-20, (1998), Abstract#3040, pg A523, FASEB Abstracts.

5. Hondal, RJ, Hill, KE, & Burk, RF. Identification of Heparin-Binding Histidine and Lysine Residues by Chemical Modification. Annual Meeting of the American Society for Experimental Biology. Washington D.C. July 17-21, (1999), Abstract #662.3, pg A875, FASEB Abstracts

6. Hill, KE, Ma, S., Hondal, RJ, & Burk, RF. Physical and Chemical Characterization of Rat Selenoprotein P Isoforms. Selenium 2000: 7th International Symposium On Selenium In Biology and Medicine. Venice, Italy. (2000).

7. Hill, KE, Ma, S., Hondal, RJ, & Burk, RF. Physical and Chemical Characterization of Rat Selenoprotein P Isoforms. Selenium 2000: 7th International Symposium On Selenium In Biology and Medicine. Venice, Italy. (2000).

8. Abel, RL, Hondal, RJ, & Raines, RT. Active Site Variants of Ribonuclease A. ACS National Meeting, Chicago, IL. Aug. 26-30, (2001), AN2001:637192.

9. Hondal, RJ, Abel, RL, & Raines, RT. Stereochemical Consequences of Catalysis by Ribonuclease A: Non-natural Variants and Phosphorothioate Substrates. ACS National Meeting, Chicago, IL. Aug. 26-30, (2001), AN2001:637183.

10. Hondal, RJ, Nilsson, BL, & Raines, RT. Incorporation of Unnatural Amino Acids into Ribonuclease A by Semisynthesis. 17th Enzyme Mechanism Conference, Marco Island, FL. (2001).

11. Hondal, RJ The mechanism of thioredoxin reductase studied by semisynthesis. (2003) Amino Acids 25, 185.

12. Hondal, RJ The Functional Role of the C-Terminus of Mammalian Thioredoxin Reductase Investigated by Peptide Complementation. Selenium Biochemistry 2003. Bethesda, MD. September 17-19, (2003)

13. Harris, KM & Hondal RJ. Deprotection of the p-methoxybenzyl group of selenocysteine by neighboring group participation.19th American Peptide Symposium. San Diego, CA. (2005).

14. Ruggles, EL, Deker, P.B., & Hondal, RJ. Synthesis and properties of disulfide-bond containing eight-membered rings. 230th Meeting of the American Chemical Society. Washington, D.C. Aug. 28-Sep. 1, (2005), AN2005:74088.


27

15. Eckenroth, BE, Everse, SJ, Adams, TE, & Hondal, RJ. Crystallization of mammalian thioredoxin reductase for structural studies using synthetic active site peptides. FASEB Meeting. April 2-6 (2005), San Diego, CA. Abstract #2600. FASEB Abstracts.

16. Lacey, B. & Hondal RJ. Purification and Characterization of Mitochondrial Thioredoxin Reductase from Caenorhabditis elegans: A Non-Selenium Containing Enzyme. Northeast Regional Meeting of the American Chemical Society, Fairfield, CT. July 14-17, (2005), AN2005:663401.

17. Eckenroth BE, Harris, KM, & Hondal RJ. Structure-Function Investigation of the C-terminal Redox-Active Tetrapeptide of Mammalian Thioredoxin Reductase by Semisynthesis. Gordon Research Conference – Enzymes, Coenzymes, and Metabolic Pathways. University of New England, July 16-21, (2006).

18. Eckenroth BE, & Hondal RJ. Structure-Function Relationships of the Conserved GCUG Tetrapeptide Motif of Thioredoxin Reductase Investigated by Protein Semisynthesis. The 8th International Symposium on Selenium in Biology and Medicine, Madison, WI. July 25-30, (2006).

19. P. Bruce Deker & Hondal RJ. Conformational Switching at the C-terminus of Thioredoxin Reductase? The 8th International Symposium on Selenium in Biology and Medicine, Madison, WI. July 25-30, (2006).

20. Ruggles EL, Hondal RJ, & Deker, PB. Synthesis and properties of cyclocystine subunits (CCS): Application to thioredoxin reductase and hepcidin. 233rd Meeting of the American Chemical Society. Chicago, IL. Mar 25th – 29th. (2007) AN2007: 295763

21. Alayne L Schroll & Hondal RJ. Further Development of New Deprotection Chemistry for Cysteine and Selenocysteine Side Chain Protecting Groups. 20th American Peptide Society Symposium: Peptides for Youth. Montreal, Canada. June 26-30, (2007).

22. Stevenson Flemer Jr. & Hondal RJ. An Efficient Protocol for On-Resin, Vicinal Disulfide Formation: Applications to Thioredoxin Reductase. 20th American Peptide Society Symposium: Peptides for Youth. Montreal, Canada. June 26-30, (2007).

23. Lacey BM, Flemer, S. & Hondal RJ. Contribution of ring strain to catalysis: Comparison of cyclic and acyclic forms of octapeptides as substrates for high Mr thioredoxin reductases. 234th Meeting of the American Chemical Society. Boston, MA. Aug 19th – 23rd. (2007) AN2007: 878899

24. Ruggles EL, & Hondal RJ. Viable construction of N-methyl cysteine and its use in peptide synthesis. 234th Meeting of the American Chemical Society. Boston, MA. Aug 19th – 23rd. (2007) AN2007: 884125

25. Hondal, RJ, Fitzsimmons, CK, Comparison of Different Oxidation Methods for Forming Disulfide Bonds In Peptides. 37th Northeast Regional Meeting of the American Chemical Society, Burlington, VT, United States, June 29-July 2 (2008), AN 2008:788526

26. Schroll, A, Hondal, RJ, Advances In 1) the Development of New Deprotection Chemistry for Cysteine and Selenocysteine Side Chain Protecting Groups and 2) the Synthesis of a New Selenocysteine Derivative That Have Applications In Peptide Synthesis. 37th Northeast Regional Meeting of the American Chemical Society, Burlington, VT, United States, June 29-July 2 (2008), AN 2008:788523

27. Flemer, S, Hondal, RJ. Native Chemical Ligation as An Important Tool in Protein Engineering. 37th Northeast Regional Meeting of the American Chemical Society, Burlington, VT, United States, June 29-July 2 (2008), AN 2008:788522


28

28. Lothrop, AP, Hondal, RJ. Effect of D-Cysteine Insertion on the Catalysis of Drosophila Melanogaster Thioredoxin Reductase. 37th Northeast Regional Meeting of the American Chemical Society, Burlington, VT, United States, June 29-July 2 (2008), AN 2008:788407

29. Ruggles, EL; Hondal, RJ. Conformational Analysis of N-Me Vicinal Disulfide Rings and Vicinal Diselenide Ring Reveal β-Turn Mimics. 37th Northeast Regional Meeting of the American Chemical Society, Burlington, VT, United States, June 29-July 2 (2008) AN 2008:788351

30. Hondal, RJ. From Sulfur Substrates to Selenium in Enzymes. 40th Central Regional Meeting of the American Chemical Society, Columbus, OH, United States, June 10-14 (2008), AN 2008:681404

31. Spiess PC, Deng B, Hondal RJ, Randall MJ, Matthews DE, & van der Vliet A, Use of a proteomics method to detect acrolein adduction: effects on redox proteins in human airway epithelial cells. 16th Annual Meeting of the Society for Free Radical Biology and Medicine, San Francisco, CA, November 18-22nd, 2009.

32. Spiess PC, Deng B, Hondal RJ, Randall MJ, Matthews DE, & van der Vliet A. A proteomics method to detect acrolein adduction: effects on redox proteins in vitro. 58th meeting of The American Society for Mass Spectrometry, Salt Lake City, Utah, May 23 – 27th, 2010.

33. Lothrop AP & Hondal RJ, How a Cys-Enzyme Can Compensate for the Lack of Sec. The 9th International Symposium on Selenium in Biology and Medicine (Selenium 2010), Kyoto, Japan, May 31 - June 4, 2010.

34. Snider GW & Hondal RJ. A chemico-biological rationale for the use of selenocysteine in a redox active enzyme: focus on mammalian thioredoxin reductase. 22nd Enzyme Mechanisms Conference, January 2nd – 6th, 2011, St. Pete Beach, Florida.

35. Lothrop AP, & Hondal RJ. The mechano-enzymatic function of selenocysteine in thioredoxin reductase. 22nd Enzyme Mechanisms Conference, January 2nd – 6th, 2011, St. Pete Beach, Florida.

36. Flemer S, & Hondal RJ. DTNP as a gentle and effective method of deprotection for side-chain protectants on commercially available Cys and Sec SPPS derivatives. 22nd American Peptide Symposium – Building Bridges. June 25th – June 30th, 2011. San Diego, CA.

37. Hondal, RJ The Selenium Paradox: The Chemical Basis for the Use of Selenocysteine in Enzymes. Gordon Research Conference – Enzymes, Coenzymes, and Metabolic Pathways. Waterville Valley Resort, NH. July 15-20, 2012.

38. Chandler JD, Hondal RJ, & Day, BJ. Selective detoxification of hypthiocyanate by mammalian thioredoxin reductase, the missing link in lung innate immunity and antioxidant defense. 52nd Society of Toxicology Meeting, March 10th – 14th, 2013. San Antonio, TX.

39. Payne NC, Geissler A, Button A, Sasuclark AR, Schroll AL, Ruggles EL, & Hondal RJ. Why are sulfur and selenium in RNA? Investigations into the redox chemistry of 2-thiouracil and 2-selenouracil derivatives. Gordon Research Conference: Thiol-Based Redox Regulation & Signaling. August 7-12, 2016, Stowe, VT.

40. St. Marie E, Ruggles EL, & Hondal RJ. Removal of benzyl groups from cysteine and selenocysteine using 2,2′-dithiobis-5-nitropyridine and ascorbolysis. 252nd American Chemical Society National Meeting & Exposition. August 21-25, 2016, Philadelphia, PA.


29

41. Payne NC, Barber DR, Ruggles EL, & Hondal RJ. The use of dimedone to study redox states of selenoproteins. Se2017, The 11th International Symposium on Selenium in Biology and Medicine. Stockholm, Sweden, August 13-17, 2017.

42. Wehrle R, Hondal RJ, & Masterson, DS. Synthesis of enantioenriched (R)-a-methylselenocysteine and its enantiomer. 2017 Southeast Regional Meeting of the American Chemical Society. Charlotte, NC. November 7-11, 2017.

43. St. Marie EJ & Hondal RJ. Pyridyl diselenide: A chemoselective tool for peptide synthesis. 26th American Peptide Society Meeting, June 22-27, 2019, Monterey, CA.

44. St. Marie EJ, Wehrle R, Masterson DS. & Hondal RJ. Utilization of alpha-methyl selenocysteine as a glutathione peroxidase mimic. 26th American Peptide Society Meeting, June 22-27, 2019, Monterey, CA.

Patents Issued or Pending

45. Direct assay of thioredoxin reductase activity (2014) US 20150050682 A1, Robert J. Hondal, Nicholas H. Heintz, Brian Cunniff, Nicholas Fredette, Gregg W. Snider.

46. Selenocystine Derivatives, Alpha-Methylselenocysteine, Alpha-Methylselenocysteine Derivatives, and Methods of Making and Using Same (2015) Provisional Patent# 62/110,943, Robert J. Hondal, Erik L Ruggles.

SUMMARY OF SCHOLARLY ACTIVITIES

As can be seen from my publication list, funded grants, and submitted grants, my research has three major foci: (i) chemistry and biochemistry of sulfur- and selenium-containing enzymes, (ii) peptide chemistry, especially disulfide-rich, bioactive peptides, and (iii) mechanistic enzymology, especially thioredoxin reductase and glutathione peroxidase.

A major driving force in my laboratory is to answer the question, “Why did nature choose selenium instead of sulfur?” in proteins, nucleic acids, and small molecule, vitamin-like compounds. I have championed the hypothesis that the reason selenium substitutes for sulfur in both proteins and nucleic acids is that selenium makes the biomolecule resistant to permanent oxidation. While this hypothesis at first struggled for acceptance, it is now becoming widely recognized. For example, see Ingold et al., (2018) Selenium utilization by GPX4 is required to prevent hydroperoxide-induced ferroptosis. Cell 172, 409-422. Because selenium-containing proteins are hard to study because the selenocysteine residue is encoded by a stop codon, we have pioneered the technique of producing these proteins by semisynthesis. This has necessitated the development of new methods for peptide synthesis as is evidenced by an award given to me by the Journal of Peptide Science. My lab continues to innovate new peptide technologies as evidenced by my patent applications. I have major collaborations with the following: Dr. Rajiv Ratan (Cornell College), Dr. Kathleen Rein (Florida International University), Dr. Brian Day (National Jewish Health), Dr. Douglas Masterson (University of Southern Mississippi), Dr. Jia Sheng (SUNY-Albany), Dr. Albert van der Vliet (UVM), Dr. Beth Bouchard (UVM), Dr. Yvonne Jansen-Heiniger (UVM) and Dr. Matthew Wargo (UVM) as evidenced by my publication list and funded and unfunded grant submissions. These collaborations evidence the impact of my work and demonstrates that my research is widely recognized.

I have been invited to symposia at the national and international levels as listed in the tables below.


30

INVITED PRESENTATIONS [list all as appropriate, at least 5 years] Regional [past 5 years or as appropriate]

Years Host Organization “Title of Talk”

City, State

2011 University of Kansas, “The Chemical and Biological Function of Selenium in Enzymes”

Lawrence, Kansas

2012 Brown University, “The Chemical and Biological Function of Selenium in Enzymes”

Providence, Rhode Island

2012 Hobart and William Smith Colleges, “Selenium: It’s Chemistry and Biology Among the Elements of Life”

Geneva, New York

2012 Florida International University, “The Selenium Paradox: The Chemical Basis for the Use of Selenocysteine in Enzymes”

Miami, Florida

2013 SUNY-Potsdam, “The Selenium Paradox: The Chemical Basis for the Use of Selenocysteine in Enzymes”

Potsdam, New York

2013 Stonehill College, “The Selenium Paradox: The Chemical Basis for the Use of Selenocysteine in Enzymes”

Eaton, Massachusetts

2016 St. Michael’s College, “Why Nature Chose Selenium”

Colchester, Vermont

2016 University of Southern Mississippi, “Why Nature Chose Selenium”

Hattiesburg, Mississippi

2016 Northeast Regional Meeting of the American Chemical Society, “Selenium in proteins and RNA: A chemical and biological rationale”

Binghamton, New York

2017 SUNY-Albany, “Selenium in enzymes and RNA: Is there a common chemical connection?”

Albany, New York

2017 Florida International University, “Why Nature Uses Selenium in Enzymes and tRNA”

Miami, Florida

2017 Yale University, “Selenium in enzymes and RNA: Is there a common chemical connection?”

New Haven, Connecticut

2019 Massachusetts Institute of Technology, “Everything I learned about thiol/disulfide exchange, I learned from selenium (and Ron)”

Cambridge, Massachusetts

2019 University of New Hampshire, “The chemical advantage of selenium in enzymes and RNA”

Durham, New Hampshire


31

National Years Host Organization

“Title of Talk” City, State

2012 Gordon Research Conference (Enzymes, Coenzymes, Metabolic Pathways). “The Chemical Basis for the use of Selenocysteine”

Watervliet Valley Resort, New Hampshire

2014 American Association for the Advancement of Science Annual Meeting. “The Essential Poison: Connecting the Chemistry of Selenium with Biology”

Chicago, Illinois

International Years Host Organization

“Title of Talk” City, State

2010 The 9th International Symposium on Selenium in Biology and Medicine. “A Chemico-Biological Rationale for the Use of Selenocysteine“

Kyoto, Japan

2017 The 11th International Symposium on Selenium in Biology and Medicine. “Selenium versus sulfur: reversibility of chemical reactions and resistance to permanent oxidation in proteins and nucleic acid”

Stockholm, Sweden

2017 10th International Peroxidase Meeting. “Selenium confers resistance to oxidative inactivation: Enzymes, model compounds, and molecular mechanisms”

Breckenridge, Colorado

2020 Gordon Research Conference (Thiol-Based Redox Regulation and Signaling). “To be determined”

Barcelona, Spain

Documents

Hondal Robert cv2019 - uvm.edu · My professional effort is split more like a faculty member from CAS as it has a 40:45:15 split between teaching, research, and service, respectively