Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Neel H. Shah"'
Publikováno v:
eLife, Vol 12 (2023)
Tyrosine kinases and SH2 (phosphotyrosine recognition) domains have binding specificities that depend on the amino acid sequence surrounding the target (phospho)tyrosine residue. Although the preferred recognition motifs of many kinases and SH2 domai
Externí odkaz:
https://doaj.org/article/9fb71c8bdebb4de5a6da8cefd7a05a06
Autor:
Frank Hidalgo, Laura M Nocka, Neel H Shah, Kent Gorday, Naomi R Latorraca, Pradeep Bandaru, Sage Templeton, David Lee, Deepti Karandur, Jeffrey G Pelton, Susan Marqusee, David Wemmer, John Kuriyan
Publikováno v:
eLife, Vol 11 (2022)
Cancer mutations in Ras occur predominantly at three hotspots: Gly 12, Gly 13, and Gln 61. Previously, we reported that deep mutagenesis of H-Ras using a bacterial assay identified many other activating mutations (Bandaru et al., 2017). We now show t
Externí odkaz:
https://doaj.org/article/8fa21de2eb884f18b20d8654df44e43f
Autor:
Suk ho Hong, Neel H Shah
Publikováno v:
eLife, Vol 8 (2019)
Predicting ancestral sequences of protein kinases reveals the molecular details that underlie different modes of activation.
Externí odkaz:
https://doaj.org/article/7f823046184045c5ae68a93411765d42
Autor:
Suk ho Hong, Sarah Y. Xi, Andrew C. Johns, Lauren C. Tang, Allyson Li, Madeleine N. Hum, Cassandra A. Chartier, Marko Jovanovic, Neel H. Shah
Publikováno v:
Chembiochem
Protein tyrosine phosphatases (PTPs) are an important class of enzymes that modulate essential cellular processes through protein dephosphorylation and are dysregulated in various disease states. There is demand for new compounds that target the acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::301fb4585689c8eb55a3d762a8afbc23
https://europepmc.org/articles/PMC10192133/
https://europepmc.org/articles/PMC10192133/
Autor:
H. Tomas Rube, Chaitanya Rastogi, Siqian Feng, Judith F. Kribelbauer, Allyson Li, Basheer Becerra, Lucas A. N. Melo, Bach Viet Do, Xiaoting Li, Hammaad H. Adam, Neel H. Shah, Richard S. Mann, Harmen J. Bussemaker
Publikováno v:
Nature Biotechnology. 40:1520-1527
Protein–ligand interactions are increasingly profiled at high throughput using affinity selection and massively parallel sequencing. However, these assays do not provide the biophysical parameters that most rigorously quantify molecular interaction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ae4f5077e7f7c4609da2b02958cb7895
https://doi.org/10.1038/s41587-022-01307-0
https://doi.org/10.1038/s41587-022-01307-0
Autor:
Ella Doron-Mandel, Benjamin J. Bokor, Yanzhe Ma, Lena A. Street, Lauren C. Tang, Ahmed A. Abdou, Neel H. Shah, George A. Rosenberger, Marko Jovanovic
The majority of cellular proteins interact with at least one partner or assemble into molecular-complexes to exert their function. This network of protein-protein interactions (PPIs) and the composition of macromolecular machines differ between cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2cc62a0e355d1efd7e66866229e4f49f
https://doi.org/10.1101/2023.01.12.523793
https://doi.org/10.1101/2023.01.12.523793
Publikováno v:
eLife, Vol 7 (2018)
The specificity of tyrosine kinases is attributed predominantly to localization effects dictated by non-catalytic domains. We developed a method to profile the specificities of tyrosine kinases by combining bacterial surface-display of peptide librar
Externí odkaz:
https://doaj.org/article/63f68a36828a40eca43c4a728a3415a0
Autor:
Neel H. Shah, Christine L. Gee, John Kuriyan, Jean M. Badroos, Helen T. Hobbs, Susan Marqusee
Publikováno v:
Protein Science : A Publication of the Protein Society
The catalytic activity of Syk‐family tyrosine kinases is regulated by a tandem Src homology 2 module (tSH2 module). In the autoinhibited state, this module adopts a conformation that stabilizes an inactive conformation of the kinase domain. The bin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::838256900e2374647a4621bc4fc68d20
https://doi.org/10.1002/pro.4199
https://doi.org/10.1002/pro.4199
Autor:
Suk ho Hong, Sarah Y Xi, Andrew C Johns, Lauren C Tang, Allyson Li, Marko Jovanovic, Neel H Shah
Protein tyrosine phosphatases (PTPs) are an important class of enzymes that modulate essential cellular processes through protein dephosphorylation and are dysregulated in various disease states. There is demand for new compounds that target the acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6d5ed2a67db429e336d410d1e7395825
https://doi.org/10.26434/chemrxiv-2022-1rnqh
https://doi.org/10.26434/chemrxiv-2022-1rnqh