G. Marius Clore

{{Short description|Molecular biophysicist, structural biologist}}

{{Infobox scientist

| name = G. Marius Clore

| birth_name = Gideon Marius Clore

| honorific_suffix = {{Post-nominals|country=GBR|MAE|FRSC|FMedSci|FRS|size=100%}}

| image = Photo of Dr. G. Marius Clore.jpg

| birth_date =

| birth_place = London, U.K.

| citizenship = British, American

| fields = Molecular Biophysics, Nuclear Magnetic Resonance, Structural Biology, Chemistry

| workplaces = {{Plainlist|

MRC National Institute for Medical Research, London.
Max Planck Institute of Biochemistry, Martinsried, Germany.
National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, U.S.}}

| education = University College London and University College Hospital Medical School, London, U.K.

| thesis_title =

| thesis_url =

| doctoral_advisor = Sir Arnold Burgen FRS

| academic_advisors =

| doctoral_students =

| notable_students = {{plainlist|

| website = {{URL|https://gmclore.org/clore}}

| known_for = Laying the foundations for three-dimensional protein structure determination in solution by NMR, developing innovative approaches for extending NMR to larger and more complex systems, and using NMR to uncover invisible states of proteins

| awards = •Member of the National Academy of Sciences
•Fellow of the Royal Society
•Fellow of the American Academy of Arts and Sciences
•Foreign Member of the Academia Europaea
•Royal Society of Chemistry Centenary Prize (2011)
•Biochemical Society Centenary Award (2013)
•Royal Society of Chemistry Khorana Prize (2021)

| father=Leon Clore

}}

G. Marius Clore MAE, FRSC, FMedSci, FRS is a British-born, Anglo-American molecular biophysicist and structural biologist. He was born in London, U.K. and is a dual U.S./U.K. Citizen.{{cite journal |vauthors=Samoray C|title=Profile of Marius Clore |journal=Proceedings of the National Academy of Sciences of the United States of America |volume=113 |issue=45 |pages=12604–12606 |year=2016 |pmid=27799541 |pmc=5111653 |doi=10.1073/pnas.1616528113|bibcode=2016PNAS..11312604S |doi-access=free }}{{cite web|last1=Clore|first1=G. Marius|title=Curriculum Vitae|url=https://gmclore.org/clore/CV/Clore_CV_biblio_2024.pdf|website=NIDDK|access-date=26 June 2020}}{{cite web|title=American Institute of Physics Oral History Interviews - Marius Clore interviewed by David Zierler|url=https://www.aip.org/history-programs/niels-bohr-library/oral-histories/44402|website=AIP|date=24 June 2020|access-date=26 June 2020}} He is a Member of the National Academy of Sciences,{{cite web|title=G. Marius Clore|url=http://www.nasonline.org/member-directory/members/20033168.html|website=Member Directory|publisher=National Academy of Sciences|access-date=12 March 2015}} a Fellow of the Royal Society,{{cite web|title=G. Marius Clore|url= https://royalsociety.org/people/G-Marius-Clore-25341/|website=Member Directory|publisher=Royal Society|access-date=29 April 2020}} a Fellow of the Academy of Medical Sciences, a Fellow of the American Academy of Arts and Sciences, a NIH Distinguished Investigator, and the Chief of the Molecular and Structural Biophysics Section in the Laboratory of Chemical Physics of the National Institute of Diabetes and Digestive and Kidney Diseases at the U.S. National Institutes of Health.{{cite web |title=G. Marius Clore, MD, Ph.D., NIH Distinguished Investigator |url=https://irp.nih.gov/pi/g-marius-clore|website=National Institutes of Health Intramural Research Program |access-date=14 August 2018}}{{cite web |title=G. Marius Clore, MD, Ph.D., FRS, NIH Distinguished Investigator |url=https://www.niddk.nih.gov/about-niddk/staff-directory/biography/c/clore-marius|website=National Institute of Diabetes and Digestive and Kidney Diseases |access-date=14 August 2018}} He is known for his foundational work in three-dimensional protein and nucleic acid structure determination by biomolecular NMR spectroscopy,{{cite journal |title=New Members and Foreign Associates of the National Academy of Sciences: G. Marius Clore, Gregory C. Fu, Sir J. Fraser Stoddart, Ei-ichi Negishi |journal=Angewandte Chemie International Edition |volume=53 |issue=26 |page=6598 |year=2014 |doi=10.1002/anie.201405510}} for advancing experimental approaches to the study of large macromolecules and their complexes by NMR,{{cite journal |author=Ringe D |title=Protein structure: an extra dimension to NMR |journal=Nature |volume=332 | issue=6162 | page=303 |year=1988 |pmid=3352729 |doi=10.1038/332303a0|bibcode=1988Natur.332..303R |s2cid=32312775 |doi-access=free }} and for developing NMR-based methods to study rare conformational states in protein-nucleic acid{{cite journal |author=Dahlquist FW |title=Slip sliding away: new insights into DNA-protein recognition |journal=Nature Chemical Biology |volume=2 |issue=7 |pages=353–354 |year=2006 |pmid=16783338 |doi=10.1038/nchembio0706-353|s2cid=12357797 }} and protein-protein{{cite journal |vauthors=Blundell TL, Fernandez-Recio J |title=Cell biology: brief encounters bolster contacts |journal=Nature |volume=444 | issue=7117 |pages=279–280 | year=2006 |pmid= 17051147 |doi=10.1038/nature05306|bibcode=2006Natur.444..279B |s2cid=4397989 }} recognition.{{cite web |title=Clore named Royal Society Fellow |url=https://www.asbmb.org/asbmb-today/people/060120/clore-named-royal-society-fellow-remembering-paul |access-date=1 June 2020}} Clore's discovery of previously undetectable, functionally significant, rare transient states of macromolecules has yielded fundamental new insights into the mechanisms of important biological processes, and in particular the significance of weak interactions and the mechanisms whereby the opposing constraints of speed and specificity are optimized. Further, Clore's work opens up a new era of pharmacology and drug design as it is now possible to target structures and conformations that have been heretofore unseen.{{cite journal|vauthors=Deshmukh, L, Tugarinov V, Appella DH, Clore GM | title=Targeting a dark excited state of HIV-1 nucleocapsid by anti-retroviral thioesters revealed by NMR spectroscopy| journal=Angewandte Chemie International Edition|volume=57|pages=2687–2691|year=2018| issue=10|pmid=29345807|doi=10.1002/anie.201713172|pmc=6034507}}

Biography

Clore received his undergraduate degree with first class honours in biochemistry from University College London in 1976 and medical degree from UCL Medical School in 1979. After completing house physician and house surgeon appointments at University College Hospital and St Charles' Hospital (part of the St. Mary's Hospital group), respectively, he was a member of the scientific staff of the Medical Research Council National Institute for Medical Research from 1980 to 1984. He received his PhD from the National Institute for Medical Research in Physical Biochemistry in 1982. He was awarded a joint Lister Institute Research Fellowship from the Lister Institute of Preventive Medicine which he held from 1982 to 1984 at the Medical Research Council.{{cite web |title=Former Fellows of the Lister Institute of Preventive Medicine|url=https://www.lister-institute.org.uk/former-fellows/|access-date=27 June 2020}} In 1984 he joined the Max Planck Institute for Biochemistry in Martinsried, Germany, where he headed the Biological NMR department from 1984 to 1988.

In 1988, Clore was recruited to the National Institutes of Health (NIH) Laboratory of Chemical Physics (National Institute of Diabetes and Digestive and Kidney Diseases) located in Bethesda, Maryland, U.S., where he interacted closely in the late 1980s and early 1990s with NIH colleagues Ad Bax, Angela Gronenborn and Dennis Torchia on the development of multidimensional heteronuclear NMR spectroscopy and a structural biology effort aimed at proteins involved in the pathogenesis of HIV/AIDS.{{cite book|last1=Clore|first1=Marius G|editor2-first=Roderick L|editor2-last=Wasylishen|editor1-first=Robin K|editor1-last=Harris|title=Encyclopedia of Magnetic Resonance|date=2011|publisher=John Wiley & Sons|isbn=978-0-470-03459-0|chapter-url=http://spin.niddk.nih.gov/clore/Pub/pdf/432.pdf|chapter=Adventures in Biomolecular NMR|doi=10.1002/9780470034590|hdl=11693/53364|access-date=2015-03-14|archive-date=2016-03-05|archive-url=https://web.archive.org/web/20160305131346/http://spin.niddk.nih.gov/clore/Pub/pdf/432.pdf|url-status=dead}} He has remained at the NIH ever since and is currently a NIH Distinguished Investigator and Chief of the Section on Molecular and Structural Biophysics at the NIH. He is an elected Member of the United States National Academy of Sciences,{{cite web|url=http://www.nasonline.org/news-and-multimedia/news/april-29-2014-NAS-Election.html|title=2014 Press release of National Academy of Sciences Members and Foreign Associates Elected|archive-url=https://web.archive.org/web/20150818062140/http://www.nasonline.org/news-and-multimedia/news/april-29-2014-NAS-Election.html|archive-date=2015-08-18}} a Fellow of the Royal Society,{{cite web|url=https://royalsociety.org/news/2020/04/outstanding-scientists-elected-as-fellows-and-foreign-members-of-the-royal-society/|title=2020 Royal Society press release of outstanding scientists elected as Fellows and Foreign Members}} a Fellow of the Academy of Medical Sciences, a Fellow of the American Academy of Arts and Sciences,{{cite web|title=Book of Members, 1780-2014: Chapter B|url=https://www.amacad.org/multimedia/pdfs/publications/bookofmembers/ChapterC.pdf|publisher=American Academy of Arts and Sciences}}{{cite web|title=American Academy of Arts and Sciences Fellows|url=https://members.amacad.org/G.Clore}} and a Foreign Member of the Academia Europaea (Biochemistry and Molecular Biology Section).{{cite web|url=http://www.ae-info.org/ae/Acad_Main/News/Elected%20members%202015|title=Elected Members of Academia Europaea 2015}} Clore's citation upon election to the Royal Society reads: {{blockquote|"Clore pioneered the development of NMR for determining three-dimensional structures of biological macromolecules and has consistently extended the frontiers of NMR to ever more complex systems. His work on the development of paramagnetic and other relaxation-based NMR experiments to detect and visualize transient, rare states of macromolecules, invisible to conventional structural and biophysical techniques, has shed unique insights into how macromolecules efficiently locate their binding partners, provided the first atomic view of the dynamic amyloid Aß assembly process from disordered peptides into protofibrils, and directly demonstrated that the apo state of the chaperonin GroEL possesses intrinsic foldase/unfoldase activities."}}

Research

=3D structure determination in solution by NMR=

Clore played a pivotal role in the development of three- and four-dimensional NMR spectroscopy,{{cite journal |vauthors=Clore GM, Gronenborn AM |title=Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy |journal=Science |volume=252 |issue=5011 |pages=1390–1399 |year=1991 |pmid=2047852 |doi=10.1126/science.2047852|bibcode=1991Sci...252.1390M |osti=83376 }} the use of residual dipolar couplings for structure determination,{{cite journal |vauthors=Clore GM |title=Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear Overhauser enhancement data and dipolar couplings by rigid body minimization |journal=Proceedings of the National Academy of Sciences USA |volume=97 |issue=16 |pages=9021–9025 |year=2000 |pmid=10922057 |doi=10.1073/pnas.97.16.9021 |pmc=16814|bibcode=2000PNAS...97.9021C |doi-access=free }} the development of simulated annealing and restrained molecular dynamics for three-dimensional protein and nucleic acid structure determination,{{cite journal |vauthors=Clore GM, Gronenborn AM |title=New methods of structure refinement for macromolecular structure determination by NMR |journal=Proceedings of the National Academy of Sciences of the United States of America |volume=95 |issue=11 |pages=5891–5898 |year=1998 |pmid=9600889 |doi=10.1073/pnas.95.11.5891 |pmc=34492|bibcode=1998PNAS...95.5891M |doi-access=free }} the solution NMR structure determination of large protein complexes,{{cite journal |vauthors=Clore GM, Venditti V |title=Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate:sugar phosphotransferase system |journal=Trends in Biochemical Sciences |volume=38 |issue=10 |pages=515–530 |year=2013 |pmid=24055245 |doi=10.1016/j.tibs.2013.08.003 |pmc=3831880}} the development of the combined use of NMR and small-angle X-ray scattering in solution structure determination,{{cite journal |vauthors=Schwieters CD, Clore, GM |title=Using small angle solution scattering data in Xplor-NIH structure calculations. |journal=Progress in Nuclear Magnetic Resonance Spectroscopy |volume=80 |pages=1–11|year=2014 | pmid=24924264 |doi=10.1016/j.pnmrs.2014.03.001 |pmc=4057650|bibcode=2014PNMRS..80....1S }} and the analysis and characterization of protein dynamics by NMR.{{cite journal |vauthors=Clore GM, Driscoll PC, Wingfield PT, Gronenborn AM |title=Analysis of backbone dynamics of interleukin-1beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy |journal=Biochemistry |volume=29 |issue=32 |pages=7387–7401 |year=1990 |pmid=2223770 |doi=10.1021/bi00484a006}} Clore's work on complexes of all the cytoplasmic components of the bacterial phosphotransferase system (PTS) led to significant insights into how signal transduction proteins recognize multiple, structurally dissimilar partners by generating similar binding surfaces from completely different structural elements and exploiting side chain conformational plasticity. Clore is also one of the main authors of the very widely used XPLOR-NIH NMR structure determination program{{cite journal |vauthors=Schwieters CD, Kuszewski JJ, Tjandra N, Clore GM |title=The Xplor-NIH NMR molecular structure determination package |journal=Journal of Magnetic Resonance |volume=160 |issue=1 |pages=65–73 |year=2003 |pmid=12565051 |doi=10.1016/S1090-7807(02)00014-9|bibcode=2003JMagR.160...65S |url=https://zenodo.org/record/1260200 }}

=Detection and visualization of excited and sparsely-populated states =

Clore's recent work has focused on developing new NMR methods (such as paramagnetic relaxation enhancement, dark state exchange saturation transfer spectroscopy and lifetime line broadening) to detect, characterize and visualize the structure and dynamics of sparsely-populated states of macromolecules, which are important in macromolecular interactions but invisible to conventional structural and biophysical techniques.{{cite journal |vauthors=Anthis NJ, Clore GM |title=Visualizing transient dark states by NMR spectroscopy |journal=Quarterly Reviews of Biophysics |volume=48 | issue=1| pages=35–116|year=2015 |pmid=25710841|pmc=6276111 | doi=10.1017/S0033583514000122}} Examples of include the direct demonstration of rotation-coupled sliding and intermolecular translocation as mechanisms whereby sequence-specific DNA binding proteins locate their target site(s) within an overwhelming sea of non-specific DNA sequences;{{cite journal |vauthors=Iwahara J, Clore GM |title=Detecting transient intermediates in macromolecular binding by paramagnetic NMR |journal=Nature |volume=440 |issue=7088 |pages=1227–1230 |year=2006 | pmid=16642002 |doi=10.1038/nature04673|bibcode=2006Natur.440.1227I |s2cid=4427016 }} the detection, visualization and characterization of encounter complexes in protein-protein association;{{cite journal |vauthors=Tang C, Iwahara J, Clore GM |title=Visualization of transient encounter complexes in protein-protein association |journal=Nature |volume=444 |issue=7117 |pages=383–386 |year=2006 |pmid=17051159 |doi=10.1038/nature05201|bibcode=2006Natur.444..383T |s2cid=4422087 }} the analysis of the synergistic effects of conformational selection and induced fit in protein-ligand interactions;{{cite journal |vauthors=Tang C, Schwieters CD, Clore GM |title=Open-to-closed transition in apo-maltose-binding protein visualized by paramagnetic NMR |journal=Nature |volume=449 |issue=7165 |pages=1078–1082 |year=2007 |pmid=17960247 |doi=10.1038/nature06232|bibcode=2007Natur.449.1078T |s2cid=4362128 }} and the uncovering of "dark", spectroscopically invisible states in interactions of NMR-visible proteins and polypeptides (including intrinsically disordered states) with very large megadalton macromolecular assemblies.{{cite web |url=http://neurosciencenews.com/neuroimaging-groel-beta-amyloid-electrophysiology-258/ |title=NMR advance brings proteins into the open |work=Neurosciencenews.com|date=25 June 2013 }} The latter includes an atomic-resolution view of the dynamics of the amyloid-β aggregation process.{{cite journal |vauthors=Fawzi NL, Ying J, Ghirlando R, Torchia DA, Clore GM |title=Atomic resolution dynamics on the surface of amyloid beta protofibrils probed by solution NMR |journal=Nature |volume=480 |issue=7376 |pages=268–272 |year=2011 |pmid=22037310 |doi=10.1038/nature10577 |pmc=3237923|bibcode=2011Natur.480..268F }} and the demonstration of intrinsic unfoldase/foldase activity of the macromolecular machine GroEL.{{cite journal|vauthors=Libich DS, Tugarinov V, Clore GM |title=Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR|journal=Proc. Natl. Acad. Sci. U.S.A.| volume=112| pages=8817–8823 |year=2015|issue=29|pmid=26124125|doi=10.1073/pnas.1510083112|pmc=4517251|bibcode=2015PNAS..112.8817L|doi-access=free}} These various techniques have also been used to uncover the kinetic pathway of pre-nucleation transient oligomerization events and associated structures involving the protein encoded by huntingtin exon-1, which may provide a potential avenue for therapeutic intervention in Huntington's disease, a fatal autosomal dominant, neurodegenerative condition.{{cite journal|vauthors=Kotler SA, Tugarinov V, Schmidt T, Ceccon A, Libich DS, Ghirlando R, Schwieters CD, Clore GM | title=probing the initial transient oligomerization events facilitating Huntingtin fibril nucleation at atomic resolution by relaxation-based NMR| journal=Proc. Natl. Acad. Sci. U.S.A.|volume=116| pages=3562–3571|year=2019| issue=9|pmid=30808748| doi=10.1073/pnas.1821216116| pmc=6397591| bibcode=2019PNAS..116.3562K|doi-access=free}}{{cite journal|vauthors=Ceccon A, Tugarinov V, Ghirlando R, Clore GM |title=Abrogation of prenucleation, transient oligomerization of the huntingtin exon-1 protein by human profilin | journal=Proc. Natl. Acad. Sci. U.S.A.|volume=117|pages=5844–5852|year=2020|issue=11 |pmid=32127471|doi=10.1073/pnas.1922264117|pmc=7084121 |bibcode=2020PNAS..117.5844C |doi-access=free}}

=Scientific impact=

Clore is one of the most highly cited scientists in the fields of molecular biophysics, structural biology, biomolecular NMR and chemistry{{cite web|url=http://www.timeshighereducation.co.uk/news/top-10-researchers-in-chemistry-based-on-total-citations/403915.article|title=Top 10 researchers in chemistry based on total citations|work=Times Higher Education|date=9 October 2008}}{{cite web|url=http://diyhpl.us/~bryan/papers2/H-index%20ranking%20of%20living%20chemists%20%28April%202010%29.pdf |title=Royal Society of Chemistry h-index ranking of living chemists}} with over 550 published scientific articles and an h-index (number of papers cited h or more time) of 144.{{cite web |url=https://scholar.google.com/citations?user=5KmWmkEAAAAJ&hl=en |title=Google scholar profile}} Clore is also one of only five NIH scientists to have been elected to both the United States National Academy of Sciences and The Royal Society, the other four being Julius Axelrod, Francis Collins, Harold Varmus and Ad Bax.

Personal life

Marius Clore was educated at the Lycee Francais Charles de Gaulle in Kensington, London, University College London and UCL Medical School. He holds a 3rd degree black belt in Tae Kwon Do and was an avid cave diver. Marius Clore's father was the film producer Leon Clore whose credits include The French Lieutenant's Woman.

Awards and honors

2024: Elected Fellow of the UK Academy of Medical Sciences{{cite web| title=Academy of Medical Sciences announces new Fellows of 2024|url=https://acmedsci.ac.uk/more/news/academy-of-medical-sciences-fellows-2024}}
2021: Murray Goodman Memorial Prize{{cite web| title=G. Marius Clore 2021 Murray Goodman Memorial Prize Winner|url=https://onlinelibrary.wiley.com/page/journal/10970282/homepage/murray_goodman_memorial_prize.htm}}
2021: Honorary Doctorate of Science (DSc) from University College London{{cite web| title=UCL Awards 2021 Honorary Degrees and Fellowships|date=15 July 2021|url=https://www.ucl.ac.uk/news/2021/jul/ucl-awards-2021-honorary-degrees-and-fellowships}}
2021: Royal Society of Chemistry Khorana Prize{{cite web| title=G. Marius Clore 2021 Royal Society of Chemistry Khorana Prize Winner|url=https://www.rsc.org/prizes-funding/prizes/2021-winners/dr-g-marius-clore/}}
2020: Elected Fellow of the Royal Society
2020: Biophysical Society Innovation Award{{cite web| title=G. Marius Clore to Receive Biophysical Society 2020 Innovation Award|url=https://www.biophysics.org/news-room/g-marius-clore-to-receive-2020-innovation-award}}{{cite web|title=Biophysical Society September 2019 Press Release|url=https://www.biophysics.org/news-room/acat/1/archive/9-2019}}
2015: Elected Foreign Member of the Academia Europaea.
2014: Elected Member of the United States National Academy of Sciences (Biophysics and Computational Biology section)
2012: Biochemical Society 2013 Centenary Award (previously known as the Jubilee Medal) and Sir Frederick Gowland Hopkins Memorial Lecture (U.K.){{cite web| title=Biochemical Society Award Winners for 2013 - Biochemist e-volution |url=http://www.biochemist.org/bio/03403/0060/034030060.pdf|publisher=Biochemical Society}}{{cite web|url=http://www.biochemistry.org/Awards/TheCentenaryAward.aspx|title=The Centenary Award|work=biochemistry.org}}
2011: Royal Society of Chemistry Centenary Prize{{cite web|url=http://www.rsc.org/ScienceAndTechnology/Awards/CentenaryPrizes/2011winnerclore.asp|title=Centenary Prize Winner 2011|work=rsc.org}}
2011: Elected Fellow of the International Society of Magnetic Resonance{{cite web|url=https://wws.weizmann.ac.il/ISMAR/ismar-organization#ismar-fellows/ |title=List of elected ISMAR fellows |archive-url=https://web.archive.org/web/20151027164057/https://wws.weizmann.ac.il/ISMAR/ismar-organization |archive-date=2015-10-27 }}
2010: Elected Fellow of the American Academy of Arts and Sciences
2010: Hillebrand Award of the Washington Chemical Society{{Cite web |url=http://csw.sites.acs.org/hillebrand.htm |title=Chemical Society of Washington Hillebrand Award |access-date=2015-03-09 |archive-date=2011-03-06 |archive-url=https://web.archive.org/web/20110306083008/http://csw.sites.acs.org/hillebrand.htm |url-status=dead }}{{cite web|url=http://www.asbmb.org/uploadedFiles/ASBMBToday/Content/Archive/Archived%20Issue%20052011.pdf|title =American Society of Biochemistry and Molecular Biology Today, May 2011, ASBMB member update p. 6}}
2009: Elected Fellow of the Biophysical Society{{cite web|url=http://www.biophysics.org/AwardsFunding/SocietyAwards/FellowoftheBiophysicalSocietyAward/tabid/501/Default.aspx|title=Fellow of the Biophysical Society Award|work=biophysics.org}}
2003: Elected Member of the Lister Institute of Preventive Medicine (U.K.){{cite web|url=http://www.lister-institute.org.uk/fellows/members/|title=Members/Former Fellows|work=lister-institute.org.uk|access-date=2015-02-19|archive-url=https://web.archive.org/web/20150805033200/http://www.lister-institute.org.uk/fellows/members/|archive-date=2015-08-05}}
2001: Original member, Institute for Scientific Information (ISI) Highly Cited Researchers Database (in Biology & Biochemistry and Chemistry sections).
1999: Elected Fellow of the American Association for the Advancement of Science.{{cite web|url=https://www.aaas.org/fellows/listing |title=Fellows of the American Associastion for the Advancement of Science}}
1993: Dupont-Merck Young Investigator Award of the Protein Society{{Cite web |url=http://www.proteinsociety.org/protein-society-awards/young-investigator-award/ |title=Protein Society Young Investigator Award |access-date=2015-02-19 |archive-url=https://web.archive.org/web/20150214011313/http://www.proteinsociety.org/protein-society-awards/young-investigator-award/ |archive-date=2015-02-14 }}{{cite web|url=http://nihrecord.nih.gov/PDF_Archive/1993%20PDFs/19930817.pdf |title=NIDDK scientists share award |publisher=The NIH Record (1993) volume 45(17), page 12}}
1990: Elected Fellow of the Royal Society of Chemistry (FRSC) (U.K).

References

External links

[https://gmclore.org G. Marius Clore personal homepage]
[https://www.aip.org/history-programs/niels-bohr-library/oral-histories/44402 Oral history interview transcript with Marius Clore on 23 March 2020, American Institute of Physics, Niels Bohr Library & Archives]
[http://www.nasonline.org/member-directory/members/20033168.html Listing on the United States National Academy of Sciences web site]
[https://royalsociety.org/people/G-Marius-Clore-25341/ Listing on the Royal Society web site]
[https://acmedsci.ac.uk/fellows/fellows-directory/ordinary-fellows/fellow/G.%20Marius-Clore-0033z00002qIMnyAAG/ Listing on the Academy of Medical Sciences (United Kingdom) web site]
[https://www.amacad.org/person/g-marius-clore/ / Listing on the American Academy of Arts and Sciences web site]
[http://www.ae-info.org/ae/User/Clore_G._Marius Listing on the Academia Europaea web site]
[https://www.niddk.nih.gov/about-niddk/staff-directory/biography/clore-marius Listing on NIDDK/NIH web site]
[http://irp.nih.gov/pi/g-marius-clore Listing on NIH Intramural Research Program web site]
{{google scholar id|5KmWmkEAAAAJ}}
[https://orcid.org/0000-0003-3809-1027 G. Marius Clore Orcid ID]
[https://www.youtube.com/watch?v=pmrDK_IOZKc Marius Clore on Landmark Article in the Journal of Magnetic Resonance]
[https://www.youtube.com/watch?v=k7kJcljKOCo Marius Clore Lecture on "Transient Prenucleation Oligomerization of Huntingtin" at the ICMRBS Webinar on Emerging Topics in Biomolecular Resonance (4/15/2021)]
[https://www.ucl.ac.uk/governance-compliance/honorary-awards/list-honorary-graduates List of University College London Honorary Graduates]