Výsledky vyhledávání - "Zhang-Bao Xu"

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Novel Synthesis and Structural Characterization of a High-Affinity Paramagnetic Kinase Probe for the Identification of Non-ATP Site Binders by Nuclear Magnetic Resonance

Autor: Desiree H.H. Tsao, Arthur Lee, Lori Krim Gavrin, Franklin J. Moy, Zhang Bao Xu, John C. McKew, Lidia Mosyak, Elizabeth Kieras, Wayne Stochaj, Annette Sievers

Publikováno v: Journal of Medicinal Chemistry. 53:1238-1249

To aid in the pursuit of selective kinase inhibitors, we have developed a unique ATP site binder tool for the detection of binders outside the ATP site by nuclear magnetic resonance (NMR). We report here the novel synthesis that led to this paramagne

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f003cb00b2d9a32bb90459fe0d5ba83c
https://doi.org/10.1021/jm901525b

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Catalytic Domain Crystal Structure of Protein Kinase C-θ (PKCθ)

Autor: Christina Benander, William S. Somers, Laura Lin, Mark Stahl, Diane Joseph-McCarthy, Karl Malakian, Rita Greco, Stephane Olland, Lori Fitz, Lidia Mosyak, Robert M. Czerwinski, Zhang-Bao Xu, Scott Wolfrom, Divya Chaudhary

Publikováno v: Journal of Biological Chemistry. 279:50401-50409

A member of the novel protein kinase C (PKC) subfamily, PKCθ, is an essential component of the T cell synapse and is required for optimal T cell activation and interleukin-2 production. Selective involvement of PKCθ in TCR signaling makes this enzy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffec59ab2a6376bd6ad4fb5f33aab08b
https://doi.org/10.1074/jbc.m409216200

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Two N-Terminal Domains of Kv4 K+ Channels Regulate Binding to and Modulation by KChIP1

Publikováno v: Neuron. 41:587-598

The family of calcium binding proteins called KChIPs associates with Kv4 family K + channels and modulates their biophysical properties. Here, using mutagenesis and X-ray crystallography, we explore the interaction between Kv4 subunits and KChIP1. Tw

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f50525e0eddc63de4b13bdb0e126666c
https://doi.org/10.1016/s0896-6273(04)00049-2

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Molecular determinants of ERα and ERβ involved in selectivity of 16α-iodo-17β estradiol

Autor: Heather A. Harris, Zhang-Bao Xu, Barry S. Komm, Rayomand J Unwalla, Barbara Stauffer, Ramesh A. Bhat

Publikováno v: The Journal of Steroid Biochemistry and Molecular Biology. 88:17-26

The two known estrogen receptors, ER alpha and ER beta, are hormone inducible transcription factors that have distinct roles in regulating cell proliferation and differentiation. The natural ligand, 17 beta-estradiol (E2), binds with high affinity to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7cf9fa2e842a2ecbad92a1af7a9e869c
https://doi.org/10.1016/j.jsbmb.2003.10.009

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Synthesis and Structure−Activity Relationship of N-Substituted 4-Arylsulfonylpiperidine-4-hydroxamic Acids as Novel, Orally Active Matrix Metalloproteinase Inhibitors for the Treatment of Osteoarthritis

Publikováno v: Journal of Medicinal Chemistry. 46:2376-2396

The matrix metalloproteinases (MMPs) are a family of zinc-containing endopeptidases that play a key role in both physiological and pathological tissue degradation. In our preceding paper, we have reported on a series of novel and orally active N-hydr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93592dc8a1e6940279319e17ff2512ee
https://doi.org/10.1021/jm0205550

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Identification of Potent and Selective MMP-13 Inhibitors

Autor: Mary Geck, Zhang-Bao Xu, Rajeev Hotchandani, Jeremy I. Levin, Junjun Wu, Xuemei Du, Thomas S. Rush, J.S. Skotnicki, Elisabeth Collins, Frank Lovering

Publikováno v: ChemInform. 36

A potent, selective series of MMP-13 inhibitors has been derived from a weak (3.2 microM) inhibitor that did not bear a zinc chelator. Structure-based drug design strategies were employed to append a Zn-chelating group to one end of the molecule and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23b84593b836a26fe32ec51c336a0614
https://doi.org/10.1002/chin.200549111

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