نتایج جستجو برای: ژن tyr

تعداد نتایج: 22053  

Journal: :The Journal of biological chemistry 1999
M Huber L Izzi P Grondin C Houde T Kunath A Veillette N Beauchemin

Biliary glycoprotein (Bgp, C-CAM, or CD66a) is an immunoglobulin-like cell adhesion molecule and functions as a tumor suppressor protein. We have previously shown that the Bgp1 isoform responsible for inhibition of colonic, liver, prostate, and breast tumor cell growth contains within its cytoplasmic domain two tyrosine residues positioned in immunoreceptor tyrosine-based inhibition motif (ITIM...

Journal: :Biochemistry 1997
D L Sorkin D K Duong A F Miller

We have compared the magnetic resonance properties and pH dependence of wild-type and mutant Fe-containing superoxide dismutase (Fe-SOD) in which the conserved active site tyrosine (Tyr 34) is replaced by phenylalanine. The EPR spectrum of the oxidized state and the NMR spectrum of the paramagnetically shifted resonances of the reduced state indicate that in both states the active site is relat...

Journal: :The Journal of biological chemistry 2007
Ying Wang Kang Zhou Xianchun Zeng Jinxiu Lin Xi Zhan

Missing in metastasis gene, or MTSS1, encodes an intracellular protein that is implicated in actin cytoskeleton reorganization and often down-regulated in certain types of tumor cells. In response to platelet-derived growth factor (PDGF), green fluorescent protein (GFP)-tagged murine Mtss1 (Mtss1-GFP) underwent redistribution from the cytoplasm to dorsal membrane ruffles along with phosphorylat...

پایان نامه :وزارت علوم، تحقیقات و فناوری - دانشگاه گیلان - دانشکده علوم پایه 1392

مهم ترین هدف از این بررسی، توسعه الکترودهای حساس و گزینش پذیر اصلاح شده با نانومواد و کاربرد آنها در تعیین مقدار ولتامتری ترکیبات دارویی و بیولوژیکی است. در بخش اول، به معرفی نانومواد کربنی و خواص آنها جهت اصلاح سطح الکترود، نقش تکنیک های ولتامتری در آنالیز داروها و تئوری تکنیک های الکتروشیمیایی پرداخته شد. در بخش دوم، نانوکامپوزیت جدیدی متشکل از نانوذرات cu(oh)2، مایع یونی 1-اتیل-3-متیل ایمیدا...

Journal: :Molecular human reproduction 2005
L Liguori E de Lamirande A Minelli C Gagnon

Acrosome reaction (AR) is an exocytotic process of fundamental importance for the spermatozoon to fertilize the oocyte. The mechanisms mediating this process are only partially defined. The aim of the present study was to investigate the role of various kinases and the extracellular signal-regulated kinase (ERK) pathway in the induction of the AR and associated phosphorylation of tyrosine (Tyr)...

Journal: :Journal of cell science 1990
J R Jara J H Martinez-Liarte F Solano R Peñafiel

The uptake of L-Tyr by B16/F10 malignant melanocytes in culture has been studied. These melanoma cells can either be depleted of amino acids by 1 h preincubation in Hanks' isotonic medium or preloaded with a specific amino acid by 1 h preincubation in the same solution containing 2 mM of the amino acid to be preloaded. By means of these pretreatments, it is shown that the rate of L-Tyr uptake i...

Journal: :Organic & biomolecular chemistry 2008
Katharina Woithe Nina Geib Odile Meyer Tanja Wörtz Katja Zerbe John A Robinson

OxyB is a cytochrome P450 enzyme that catalyzes the first oxidative phenol coupling reaction during vancomycin biosynthesis. The preferred substrate is a linear peptide linked as a C-terminal thioester to a peptide carrier protein (PCP) domain of the glycopeptide antibiotic non-ribosomal peptide synthetase. Previous studies have shown that OxyB can efficiently oxidize a model hexapeptide-PCP co...

Journal: :The Biochemical journal 1987
R E Isaac

The hydrolysis of the insect neuropeptide proctolin (Arg-Tyr-Leu-Pro-Thr) by enzyme preparations from the nervous tissue of the desert locust (Schistocerca gregaria) was investigated. Neural homogenate degraded proctolin (100 microM) at neutral pH by cleavage of the Arg-Tyr and Tyr-Leu bonds to yield Tyr-Leu-Pro-Thr, Arg-Tyr and free tyrosine. Arg-Tyr was detected as a major metabolite when the...

Journal: :The Journal of biological chemistry 2014
Joseph A DiDonato Kulwant Aulak Ying Huang Matthew Wagner Gary Gerstenecker Celalettin Topbas Valentin Gogonea Anthony J DiDonato W H Wilson Tang Ryan A Mehl Paul L Fox Edward F Plow Jonathan D Smith Edward A Fisher Stanley L Hazen

We reported previously that apolipoprotein A-I (apoA-I) is oxidatively modified in the artery wall at tyrosine 166 (Tyr(166)), serving as a preferred site for post-translational modification through nitration. Recent studies, however, question the extent and functional importance of apoA-I Tyr(166) nitration based upon studies of HDL-like particles recovered from atherosclerotic lesions. We dev...

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