Author

M. N. Isupov

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· 4 Microbiology· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Research Focus:protein structure prediction· 4 Assay:cryo-EM· 3 Assay:structural biology· 3 Research Focus:cell type annotation· 2 Approach:deep learning· 2 Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1

Frequent Co-Authors

B. Daum· 4 shared M. McLaren· 4 shared V. Gold· 3 shared C. Hanus· 2 shared L. Gambelli· 2 shared M. C. Gaines· 2 shared R. Conners· 2 shared R. U. Haque· 2 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 32 mutual co-author links

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4 shared papersMicrobiology

B. Daum

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Author profile →

8 papers

Recent·Most cited

CryoEM reveals the structure of an archaeal pilus involved in twitching motility

M. C. Gaines, S. Sivabalasarma, M. N. Isupov, R. U. Haque, M. McLaren, C. Hanus, V. A. M. Gold, S.-V. Albers, B. Daum

The paper presents a cryoEM structure of the archaeal adhesive pilus (Aap) from Sulfolobus acidocaldarius, revealing three distinct conformations of the subunit AapB.

bioRxiv · Aug 7, 2023Microbiology

Structure of the two-component S-layer of the archaeon Sulfolobus acidocaldarius

L. Gambelli, M. McLaren, R. Conners, K. Sanders, M. C. Gaines, L. Clark, V. Gold, D. Kattnig, M. Sikora, C. Hanus, M. N. Isupov, B. Daum

The paper determines the atomic structure of the two-component S-layer in Sulfolobus acidocaldarius using cryoEM, cryoET, and AlphaFold2.

bioRxiv · Oct 7, 2022Microbiology

Structural study of UFL1-UFC1 interaction uncovers the importance of UFL1 N-terminal helix for ufmylation

S. Banerjee, J. K. Varga, M. Kumar, G. Zoltsman, M. N. Isupov, R. Rosenzweig, O. Schueler-Furman, R. Wiener

This study reveals the role of UFL1's N-terminal helix in binding UFC1 and ufmylation, uncovering a helix-mediated regulatory mechanism in the E1-E2-E3 cascade.

bioRxiv · Sep 15, 2022 · PreprintBiochemistry

Donor strand complementation, isopeptide bonds and glycosylation stabilise highly resilient archaeal thread filaments

M. Gaines, M. N. Isupov, S. Sivabalasarma, R. U. Haque, M. McLaren, P. Tripp, A. Neuhaus, V. Gold, S.-V. Albers, B. Daum

The paper identifies and characterizes the structure of archaeal thread filaments, revealing their stabilization through glycosylation, donor strand complementation, and isopeptide bonds.

bioRxiv · Apr 26, 2022Microbiology

Spinning sugars in antigen biosynthesis: a direct study of the Coxiella burnetii and Streptomyces griseus TDP-sugar epimerases

A. R. Cross, S. Roy, M. Vivoli Vega, M. Rejzek, S. A. Nepogodiev, M. Cliff, D. Salmon, M. N. Isupov, R. A. Field, J. L. Prior, N. J. Harmer, Glycoengineering of Veterinary Vaccines (GoVV)

This paper studies the TDP-sugar epimerases in Coxiella burnetii and Streptomyces griseus, showing they perform the RmlC 3,5 double epimerisation activity and support TDP-rhamnose biosynthesis.

bioRxiv · Oct 25, 2021 · PreprintBiochemistry

New insights into the architecture and dynamics of archaella

L. Gambelli, M. N. Isupov, R. Conners, M. McLaren, A. Bellack, V. Gold, R. Rachel, B. Daum

The paper presents the structure of the Methanocaldococcus villosus archaellum filament, revealing it is composed of two alternating archaellins and contains structural elements that enable movement.

bioRxiv · Oct 1, 2021 · PreprintMicrobiology

Structure and function of N-acetylglucosamine kinase illuminates the catalytic mechanism of ROK kinases

S. Roy, M. V. Vega, J. R. Ames, N. Britten, K. Evans, A. Kent, M. N. Isupov, N. Harmer

The paper determines the structure of NagK from Plesiomonas shigelloides in complex with GlcNAc and ATP analogue, revealing conformational changes and a sequential random mechanism.

bioRxiv · Sep 30, 2021 · PreprintBiochemistry

The Structural Basis for SARM1 Inhibition, and Activation Under Energetic Stress

M. Sporny, J. Guez-Haddad, T. Khazma, A. Yaron, M. Dessau, C. Mim, M. N. Isupov, R. Zalk, M. Hons, Y. Opatowsky

This paper presents cryo-EM structures of SARM1 showing how NAD+ inhibits its NADase activity and how NAD+ depletion activates it, leading to cell death.

bioRxiv · Aug 5, 2020Biochemistry