Author

N. H. Shah

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· 7 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Research Focus:protein folding & dynamics· 6 Assay:proteomics· 6 Organism:human· 4 Organism:E. coli· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

J. Kuriyan· 6 shared S. Marqusee· 3 shared C. L. Gee· 2 shared D. Karandur· 2 shared H. T. Hobbs· 2 shared R. Voleti· 2 shared A. C. Susa· 1 shared A. E. van Vlimmeren· 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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6 shared papersBiochemistry

J. Kuriyan

Mutual co-authors in cluster

Author profile →

9 papers

Recent·Most cited

The pathogenic T42A mutation in SHP2 rewires the interaction specificity of its N-terminal regulatory domain

A. E. van Vlimmeren, R. Voleti, C. A. Chartier, Z. Jiang, D. Karandur, P. A. Humphries, W.-L. Lo, N. H. Shah

This paper investigates the T42A mutation in SHP2, showing it alters ligand-binding specificity in the N-terminal SH2 domain, leading to biased activation and enhanced signaling.

bioRxiv · Jul 10, 2023Biochemistry

High-throughput profiling of sequence recognition by tyrosine kinases and SH2 domains using bacterial peptide display

A. Li, R. Voleti, M. Lee, D. Gagoski, N. H. Shah

This paper develops a platform to quantitatively profile sequence recognition by tyrosine kinases and SH2 domains using peptide libraries and deep sequencing, revealing phosphosite-specific mutations and binding affinities.

bioRxiv · Aug 1, 2022Biochemistry

Saturation mutagenesis of a predicted ancestral Syk-family kinase

H. T. Hobbs, N. H. Shah, S. R. Shoemaker, J. F. Amacher, S. Marqusee, J. Kuriyan

The paper generates a bacterial-expressible Syk-family kinase via ancestral sequence reconstruction and uses deep mutational scanning to identify functional mutations.

bioRxiv · Apr 24, 2022Biochemistry

A Saturation-Mutagenesis Analysis of the Interplay Between Stability and Activation in Ras

F. Hidalgo, L. M. Nocka, N. H. Shah, K. Gorday, N. R. Latorraca, P. Bandaru, S. Templeton, D. Lee, D. Karandur, J. G. Pelton, S. Marqusee, D. Wemmer, J. Kuriyan

This study shows that cancer hotspot mutations in Ras activate it regardless of stability, while non-hotspot mutations can be activating or deleterious depending on stability.

bioRxiv · Jan 6, 2022Biophysics

Differences in the dynamics of the tandem-SH2 modules of the Syk and ZAP-70 tyrosine kinases

H. T. Hobbs, N. H. Shah, J. M. Badroos, C. L. Gee, S. Marqusee, J. Kuriyan

This study compares the conformational dynamics of the tandem-SH2 modules in Syk and ZAP-70 kinases, revealing differences in their autoinhibited states and activation mechanisms.

bioRxiv · Jul 20, 2021Biochemistry

Differential ampicillin/ceftriaxone susceptibility among diverse Enterococcus faecalis from infective endocarditis

K. J. Westbrook, G. S. Chilambi, H. R. Nordstrom, A. Iovleva, N. H. Shah, C. E. Jones, E. G. Kline, Y. Doi, R. K. Shields, D. Van Tyne

This study examines antimicrobial susceptibility of E. faecalis isolates from infective endocarditis, finding reduced ceftriaxone activity in strains with PBP4 and IreP mutations.

bioRxiv · Jun 7, 2021 · PreprintMicrobiology

Variation in assembly stoichiometry in non-metazoan homologs of the hub domain of Ca2+/Calmodulin-dependent protein kinase II

E. D. McSpadden, Z. Xia, C. C. Chi, A. C. Susa, N. H. Shah, C. L. Gee, E. R. Williams, J. Kuriyan

The paper shows that hub domain assemblies of CaMKII-like proteins in green algae form larger oligomers than metazoan homologs, and that sequence changes can alter assembly stoichiometry.

bioRxiv · Jan 31, 2019Biochemistry

Deep mutational analysis reveals functional trade-offs in the sequences of EGFR autophosphorylation sites

A. J. Cantor, N. H. Shah, J. Kuriyan

The paper uses mutational analysis to show how EGFR phosphosite sequences balance phosphorylation efficiency and adapter protein binding.

bioRxiv · Feb 28, 2018Biochemistry

Fine-tuning of substrate preferences of the Src-family kinase Lck revealed through a high-throughput specificity screen

N. H. Shah, M. Löbel, A. Weiss, J. Kuriyan

The paper develops a high-throughput method to map tyrosine kinase specificities and identifies differences in substrate recognition between Lck and c-Src.

bioRxiv · Jan 19, 2018Biochemistry