Author

R. Chalk

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 6 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Organism:human· 3 Research Focus:protein structure prediction· 3 Assay:proteomics· 3 Assay:structural biology· 3 Research Focus:protein folding & dynamics· 2 Organism:virus· 2 Research Focus:cell type annotation· 1

Frequent Co-Authors

A. C. W. Pike· 2 shared A. Quigley· 2 shared E. P. Carpenter· 2 shared N. A. Burgess-Brown· 2 shared O. Borkowska· 2 shared O. Gileadi· 2 shared T. Moreira· 2 shared A. Borbas· 1 shared

Activity by Year

2018-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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2 shared papersBiochemistry

A. C. W. Pike

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Author profile →

7 papers

Recent·Most cited

Structural basis of the mechanism and inhibition of a human ceramide synthase

T. C. Pascoa, A. C. W. Pike, C. S. Tautermann, G. Chi, M. Traub, A. Quigley, R. Chalk, S. Stefanic, S. Thamm, A. Pautsch, E. P. Carpenter, G. Schnapp, D. B. Sauer

This study determines the structural mechanism of CerS6, a ceramide synthase, using cryo-EM and biochemical analysis, revealing a ping-pong reaction mechanism and insights into fumonisin B1 inhibition.

bioRxiv · Dec 2, 2023Biochemistry

Regulation of inositol 5-phosphatase activity by the C2 domain of SHIP1 and SHIP2

W. J. Bradshaw, E. C. Kennedy, T. Moreira, L. A. Smith, R. Chalk, V. L. Katis, J. L. Benesch, P. E. Brennan, E. J. Murphy, O. Gileadi

The paper determines structures of SHIP1 and SHIP2 phosphatase and C2 domains, showing the C2 domain modulates phosphatase activity more in SHIP2 than SHIP1, providing insights for drug development.

bioRxiv · Jul 31, 2023Biochemistry

Allosteric regulation and crystallographic fragment screening of SARS-CoV-2 NSP15 endoribonuclease

A. Schutzer Godoy, A. Minalli Nakamura, A. Douangamath, Y. Song, G. Dias Noske, V. Oliveira Gawriljuk, R. Sachetto Fernandes, H. D. Muniz Pereira, K. Irene Zagato Oliveira, D. Fearon, A. Dias, T. Krojer, M. Fairhead, A. Powell, L. Dunnet, , G. Oliva

This study characterizes SARS-CoV-2 NSP15 endoribonuclease, identifies its allosteric properties, and discovers new allosteric sites for inhibitor development.

Nucleic Acids Research · Apr 28, 2023Peer-reviewedBiochemistry

Identification, Mapping and Relative Quantitation of SARS-CoV-2 Spike Glycopeptides by Mass-Retention Time Fingerprinting

R. Chalk, W. Greenland, T. Moreira, J. Coker, S. Mukhopadhyay, E. Williams, C. Manning, T. Bohstedt, R. McCrorie, A. Fernandez-Cid, N. A. Burgess-Brown

The paper introduces a method to identify, map, and quantify SARS-CoV-2 Spike glycopeptides using mass-retention time fingerprinting with LC-TOF mass spectrometry.

bioRxiv · Jul 24, 2020Biochemistry

A new paradigm for Prelamin A proteolytic processing by ZMPSTE24: the upstream SY^LL cleavage occurs first and there is no CaaX processing by ZMPSTE24

L. Nie, E. Spear, T. D. Babatz, A. Quigley, Y. Y. Dong, A. Chu, B. Rotty, R. Chalk, S. M. M. Mukhopadhyay, N. A. Burgess-Brown, A. C. W. Pike, S. G. Young, S. Michaelis, E. P. Carpenter

This study challenges the established order of prelamin A processing by ZMPSTE24, showing that SY^LL cleavage occurs first and independently of C-terminal modifications.

bioRxiv · May 13, 2020 · PreprintBiochemistry

Electrospray Surface Charge Describes Protein Molecular Motion

R. Chalk, O. Borkowska, K. A. Azeez, S. Oerum, P. Born, O. Gileadi, N. Burgess-Brown

The paper examines how electrospray mass/charge distributions reflect protein surface area and molecular motion, showing differences between native and denatured proteins.

bioRxiv · Mar 8, 2019 · PreprintBiophysics

Structural basis of human 5,10-methylenetetrahydrofolate reductase (MTHFR) regulation by phosphorylation and S-adenosylmethionine inhibition

D. S. Froese, J. Kopec, E. Rembeza, G. A. Bezerra, A. Oberholzer, T. Suormala, S. Lutz, R. Chalk, O. Borkowska, M. Baumgartner, W. Yue

This study presents the 2.5 Å resolution crystal structure of human MTHFR, revealing its architecture and how phosphorylation and SAM binding regulate its activity.

bioRxiv · Feb 26, 2018Biochemistry