Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Bryan M. Zhao"'
Autor:
Bryan M Zhao, Sarah L Keasey, Joseph E Tropea, George T Lountos, Beverly K Dyas, Scott Cherry, Sreejith Raran-Kurussi, David S Waugh, Robert G Ulrich
Publikováno v:
PLoS ONE, Vol 10, Iss 8, p e0134984 (2015)
Protein tyrosine phosphatases dephosphorylate tyrosine residues of proteins, whereas, dual specificity phosphatases (DUSPs) are a subgroup of protein tyrosine phosphatases that dephosphorylate not only Tyr(P) residue, but also the Ser(P) and Thr(P) r
Externí odkaz:
https://doaj.org/article/f687ef066e5f4c6595a050a153f0b35c
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2296
Mass spectrometry is a sensitive and specific analytical technique that is capable of providing qualitative and quantitative data to resolve the protein elements of biochemical pathways that are altered by antibiotics. Here we present methods to stud
Publikováno v:
Methods in Molecular Biology ISBN: 9781071613573
Mass spectrometry is a sensitive and specific analytical technique that is capable of providing qualitative and quantitative data to resolve the protein elements of biochemical pathways that are altered by antibiotics. Here we present methods to stud
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::89f72c5b701375c9e42b3310f2ed325a
https://doi.org/10.1007/978-1-0716-1358-0_22
https://doi.org/10.1007/978-1-0716-1358-0_22
The VH1 protein encoded by the highly conserved H1 locus of orthopoxviruses is a dual-specificity phosphatase (DUSPs) that hydrolyzes phosphate groups from phosphorylated tyrosine, serine, and threonine residues of viral and host cell proteins. Becau
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::06afbc5e795eda5669697108ad1a74d0
https://doi.org/10.1101/2020.05.26.100743
https://doi.org/10.1101/2020.05.26.100743
Autor:
Bryan M. Zhao, Sarah L. Keasey, Stefan Fernandez, Robert G. Ulrich, Anna P. Durbin, Jessica L. Smith
Publikováno v:
ACS Infectious Diseases. 4:1705-1717
Dengue is a mosquito-borne disease caused by four dengue virus serotypes (DENV1-4) that are loosely categorized by sequence commonalities and antibody recognition profiles. The highly variable envelope protein (E) that is prominently displayed on the
Autor:
David S. Waugh, Sreejith Raran-Kurussi, Bryan M. Zhao, Robert G. Ulrich, Beverly Dyas, Terrence R. Burke, George T. Lountos
Publikováno v:
Acta Crystallographica Section D Structural Biology. 74:1015-1026
Here, new crystal structures are presented of the isolated membrane-proximal D1 and distal D2 domains of protein tyrosine phosphatase epsilon (PTP∊), a protein tyrosine phosphatase that has been shown to play a positive role in the survival of huma
Autor:
Megan Hogan, Scott Cherry, Kohei Tsuji, Xue Zhi Zhao, Medhanit Bahta, Robert G. Ulrich, David S. Waugh, Joseph E. Tropea, Terrence R. Burke, Bryan M. Zhao, Trung Xuan Nguyen, George T. Lountos
Publikováno v:
ACS Comb Sci
Chemical library screening approaches that focus exclusively on catalytic events may overlook unique effects of protein-protein interactions that can be exploited for development of specific inhibitors. Phosphotyrosyl (pTyr) residues embedded in pept
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e59c6077cac0661da1ecb1605616855f
https://europepmc.org/articles/PMC8132114/
https://europepmc.org/articles/PMC8132114/
Autor:
Scott Cherry, Megan Hogan, George T. Lountos, Terrence R. Burke, Joseph E. Tropea, Bryan M. Zhao, Robert G. Ulrich, David S. Waugh, Medhanit Bahta
Publikováno v:
Chemical Biology & Drug Design. 81:323-333
We have developed competitive and direct binding methods to examine small-molecule inhibitors of protein tyrosine phosphatase activity. Focusing on the Yersinia pestis outer protein H, a potent bacterial protein tyrosine phosphatase, we describe how
Autor:
Sreejith Raran-Kurussi, Sarah L. Keasey, Bryan M. Zhao, Joseph E. Tropea, George T. Lountos, David S. Waugh, Robert G. Ulrich, Beverly Dyas, Scott Cherry
Publikováno v:
PLoS ONE
PLoS ONE, Vol 10, Iss 8, p e0134984 (2015)
PLoS ONE, Vol 10, Iss 8, p e0134984 (2015)
Protein tyrosine phosphatases dephosphorylate tyrosine residues of proteins, whereas, dual specificity phosphatases (DUSPs) are a subgroup of protein tyrosine phosphatases that dephosphorylate not only Tyr(P) residue, but also the Ser(P) and Thr(P) r
Autor:
Bryan M. Zhao, F. Michael Hoffmann
Publikováno v:
Molecular Biology of the Cell. 17:3819-3831
Overexpression of the inhibitory Smad, Smad7, is used frequently to implicate the Smad pathway in cellular responses to transforming growth factor beta (TGF-beta) signaling; however, Smad7 regulates several other proteins, including Cdc42, p38MAPK, a