Výsledky vyhledávání - "M. J. Huddleston"

Identification of tyrosines 154 and 307 in the extracellular domain and 653 and 766 in the intracellular domain as phosphorylation sites in the heparin-binding fibroblast growth factor receptor tyrosine kinase (flg)

Autor: M. J. Huddleston, S. A. Carr, M. Kan, John W. Crabb, Jinzhao Hou, K. McKeehan, W. L. McKeehan

Publikováno v: Protein Science. 2:86-92

Four tyrosine residues have been identified as phosphorylation sites in the tyrosine kinase isoform of the heparin-binding fibroblast growth factor receptor flg (FGF-R1). Baculoviral-insect cell-derived recombinant FGF-R1 was phosphorylated and fragm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c8255a4e79d47d7781359b7438d987e7
https://doi.org/10.1002/pro.5560020109

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ChemInform Abstract: Arrivacins, Novel Pseudoguaianolide Esters with Potent Angiotensin II Binding Activity from Ambrosia psilostachya

Autor: Y. Chen, C. Chambers, M. F. Bean, M. J. Huddleston, John Westley, P. Offen, B. K. Carte, T. Francis

Publikováno v: ChemInform. 22

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::47734093895c92eae3f324653168127b
https://doi.org/10.1002/chin.199140213

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Mechanism of inhibition of cathepsin K by potent, selective 1, 5-diacylcarbohydrazides: a new class of mechanism-based inhibitors of thiol proteases

Autor: M J, Bossard, T A, Tomaszek, M A, Levy, C F, Ijames, M J, Huddleston, J, Briand, S, Thompson, S, Halpert, D F, Veber, S A, Carr, T D, Meek, D G, Tew

Publikováno v: Biochemistry. 38(48)

The nature of the inhibition of thiol proteases by a new class of mechanism-based inhibitors, 1,5-diacylcarbohydrazides, is described. These potent, time-dependent, active-site spanning inhibitors include compounds that are selective for cathepsin K,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5a6f7ece91586583a3481bd2f32db939
https://pubmed.ncbi.nlm.nih.gov/10625455

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Identification of the autophosphorylation sites in rhodopsin kinase

Autor: K, Palczewski, J, Buczyłko, P, Van Hooser, S A, Carr, M J, Huddleston, J W, Crabb

Publikováno v: The Journal of biological chemistry. 267(26)

Rhodopsin kinase (RK) is a second-messenger-independent protein kinase that is involved in deactivation of photolyzed rhodopsin (Rho*). We have developed a significantly improved method for isolation of RK based on the specific interactions of phosph

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::074518e65b963735cac04e0956f506b5
https://pubmed.ncbi.nlm.nih.gov/1527025

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Protein and carbohydrate structural analysis of a recombinant soluble CD4 receptor by mass spectrometry

Autor: S A, Carr, M E, Hemling, G, Folena-Wasserman, R W, Sweet, K, Anumula, J R, Barr, M J, Huddleston, P, Taylor

Publikováno v: The Journal of biological chemistry. 264(35)

The primary structure of a soluble form of the CD4 receptor (sCD4) expressed in Chinese hamster ovary cells has been confirmed by mass spectrometric peptide mapping and and tandem mass spectrometry. These studies corroborated 95% of the 369-amino aci

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c04a8c2cb21209e5d66ddb79c5a5eb6f
https://pubmed.ncbi.nlm.nih.gov/2592374

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