Author

C. S. Craik

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

Biology Disciplines

Click to filter author papers

Microbiology· 4 Biochemistry· 3 Biophysics· 2 Immunology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 8 Research Focus:drug response / drug discovery· 5 Organism:human· 5 Assay:proteomics· 4 Research Focus:host-pathogen & immune response· 3 Approach:deep learning· 2 Organism:virus· 2 Assay:bulk RNA-seq· 1

Frequent Co-Authors

A. J. O'Donoghue· 3 shared A. L. Lourenco· 3 shared C. Bardine· 3 shared B. K. Shoichet· 2 shared P. Fajtova· 2 shared A. A. da Silva· 1 shared A. C. Thwin· 1 shared A. D. JOHNSON· 1 shared

Activity by Year

2020-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiophysics

A. J. O'Donoghue

Mutual co-authors in cluster

Author profile →

10 papers

Recent·Most cited

Phosphorylation of a Cleaved Tau Proteoform at a Single Residue Inhibits Binding to the E3 Ubiquitin Ligase, CHIP

C. M. Nadel, K. Wucherer, A. Oehler, A. C. Thwin, K. Basu, M. D. Callahan, D. R. Southworth, D. A. Mordes, C. S. Craik, J. E. Gestwicki

This study identifies phosphorylation at residue S416 on tauC3 as a mechanism that inhibits its degradation by CHIP, contributing to its accumulation in Alzheimer's disease.

bioRxiv · Aug 16, 2023 · PreprintBiochemistry

Perturbations in podocyte transcriptome and biological pathways induced by FSGS associated circulating factors.

P. Rashmi, T. K. Sigdel, D. Rychkov, I. Damm, A. A. da Silva, F. Vincenti, A. L. Lourenco, C. S. Craik, J. Reiser, M. M. Sarwal

This paper investigates how circulating factors like suPAR and CD40 autoantibodies induce podocyte injury in FSGS and identifies therapeutic targets for rFSGS.

Annals of Translational Medicine · Jun 1, 2023Peer-reviewedImmunology

Large library docking for novel SARS-CoV-2 main protease non-covalent and covalent inhibitors

E. A. Fink, C. Bardine, S. Gahbauer, I. Singh, K. White, S. Gu, X. Wan, B. Ary, I. Glenn, J. O'Connell, H. O'Donnell, P. Fajtova, J. Lyu, S. Vigneron, N. J. Young, , C. S. Craik

The paper identifies novel non-covalent and covalent inhibitors of SARS-CoV-2 main protease through virtual docking and experimental validation.

bioRxiv · Jul 5, 2022Biophysics

Structure-based identification of naphthoquinones and derivatives as novel inhibitors of main protease Mpro and papain-like protease PLpro of SARS-CoV-2

L. H. Santos, T. Kronenberger, R. G. Almeida, E. Barbosa da Silva, R. E. O. Rocha, J. C. Oliveira, L. V. Barreto, D. Skinner, P. Fajtova, M. A. Giardini, B. Woodworth, C. Bardine, A. L. Lourenco, C. S. Craik, A. Poso, , R. Ferreira

This study identifies naphthoquinone derivatives as inhibitors of SARS-CoV-2 proteases Mpro and PLpro through virtual screening and biochemical assays.

bioRxiv · Jan 5, 2022Biochemistry

Colloidal aggregators in biochemical SARS-CoV-2 repurposing screens

H. R. O'Donnell, T. A. Tummino, C. Bardine, C. S. Craik, B. K. Shoichet

This study identifies colloidal aggregators in SARS-CoV-2 drug repurposing screens, showing that many drugs form colloids at therapeutic concentrations, potentially leading to false positive results.

bioRxiv · Aug 31, 2021Biochemistry

A novel class of TMPRSS2 inhibitors potently block SARS-CoV-2 and MERS-CoV viral entry and protect human epithelial lung cells

M. Mahoney, V. C. Damalanka, M. Tartell, D. H. Chung, A. L. Lourenco, D. Pwee, A. E. Mayer Bridwell, M. Hoffmann, J. Voss, P. Karmakar, N. P. Azouz, A. M. Klinger, P. W. Rothlauf, C. E. Thompson, M. Lee, , J. W. Janetka

This paper identifies a novel class of TMPRSS2 inhibitors that effectively block SARS-CoV-2 and MERS-CoV entry and show promise as a therapeutic for COVID-19.

bioRxiv · May 6, 2021Microbiology

Characterisation of protease activity during SARS-CoV-2 infection identifies novel viral cleavage sites and cellular targets with therapeutic potential

B. Meyer, J. Chiaravalli, S. Gellenoncourt, P. Brownridge, D. P. Bryne, L. A. Daly, A. Grauslys, M. Walter, F. Agou, L. A. Chakrabarti, C. S. Craik, C. E. Eyers, P. A. Eyers, Y. Gambin, A. R. Jones, , E. Emmott

This study identifies novel SARS-CoV-2 protease cleavage sites and cellular targets using mass spectrometry, showing that targeting these proteins can inhibit viral replication.

bioRxiv · Sep 16, 2020Microbiology

Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients

L. E. Miller-Vedam, B. Bräuning, K. D. Popova, N. T. Schirle Oakdale, J. L. Bonnar, J. R. Prabu, E. A. Boydston, N. Sevillano, M. J. Shurtleff, R. M. Stroud, C. S. Craik, B. Schulman, A. Frost, J. S. Weissman

The paper reveals the structural and mechanistic basis of EMC's role in biogenesis of distinct transmembrane proteins through cryo-EM structures and functional studies.

bioRxiv · Sep 2, 2020Biophysics

Bivalent binding of a fully human IgG to the SARS-CoV-2 spike proteins reveals mechanisms of potent neutralization

B. Wang, D. Asarnow, W.-H. Lee, C.-W. Huang, B. Faust, P. M. L. Ng, E. Z. X. Ngoh, M. Bohn, D. Bulkley, A. Pizzorno, H. C. Tan, C. Y. Lee, R. A. Minhat, O. Terrier, M. K. Soh, , C.-I. Wang

This study identifies a potent SARS-CoV-2 neutralizing antibody, 5A6, that binds bivalently to two RBDs on the spike protein, showing resistance to key mutations.

bioRxiv · Jul 14, 2020 · PreprintMicrobiology

Combination of antifungal drugs and protease inhibitors prevent Candida albicans biofilm formation and disrupt mature biofilms

M. B. Lohse, M. Gulati, C. S. Craik, A. D. JOHNSON, C. J. Nobile

This study identifies combinations of antifungal drugs and protease inhibitors that inhibit C. albicans biofilm formation and disrupt mature biofilms.

bioRxiv · Feb 11, 2020Microbiology