نتایج جستجو برای: phosphoprotein gene

تعداد نتایج: 1144108  

Journal: :The Biochemical journal 1985
M J Halikowski C C Liew

Three monoclonal antibody subclasses (IgG1, IgG2a, and IgM) were raised to the phosphoprotein B2 (Mr 68000, pI6.5-8.2) which has been shown previously to be associated with the nucleosomes of rat liver nuclei. These antibodies do not show any significant cross reactivity with CM-cellulose 'unbound' non-histone chromosomal proteins, bovine serum albumin or histones. Further verification of the s...

Journal: :The EMBO journal 1998
G Condorelli G Vigliotta C Iavarone M Caruso C G Tocchetti F Andreozzi A Cafieri M F Tecce P Formisano L Beguinot F Beguinot

We have used differential display to identify genes whose expression is altered in type 2 diabetes thus contributing to its pathogenesis. One mRNA is overexpressed in fibroblasts from type 2 diabetics compared with non-diabetic individuals, as well as in skeletal muscle and adipose tissues, two major sites of insulin resistance in type 2 diabetes. The levels of the protein encoded by this mRNA ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2003
Inger Carlberg Maria Hansson Thomas Kieselbach Wolfgang P Schröder Bertil Andersson Alexander V Vener

The characteristics of a phosphoprotein with a relative electrophoretic mobility of 12 kDa have been unknown during two decades of studies on redox-dependent protein phosphorylation in plant photosynthetic membranes. Digestion of this protein from spinach thylakoid membranes with trypsin and subsequent tandem nanospray-quadrupole-time-of-flight mass spectrometry of the peptides revealed a prote...

2011

Since first being proposed as a tandem gene family in 2001, the relatedness of the 5 SIBLING proteins (BSP, DMP1, DSPP, MEPE, and SPP1/OPN) has predominantly depended on arguments involving shared intron/exon properties as well as conserved protein biochemical properties (e.g. unstructured and acidic) and specific peptide motifs (e.g. phosphorylation and integrin-binding RGD). This report discu...

Journal: :The Journal of biological chemistry 1973
P V Sulakhe G I Drummond D C Ng

Isolated sarcolemma hydrolyzed ATP in the presence of Mg2+ and Ca2+. MgATPase was stimulated by low concentrations of Ca2+ and inhibited by high concentrations of this cation. Membranes hydrolyzed p-nitrophenylphosphate in the presence of Mg 2+; this activity was stimulated by Ca2f and K+. La3f stimulated MgATPase at low concentrations (up to 50 pM) and caused inhibition at higher concentration...

2001
Jack E. Dixon

A recombinant protein-tyrosine-phosphatase has been expressed in Escherichia coli and purified to a single band by sodium dodecyl sulfate-polyacrylamide gel electrophoresis using affinity chromatography. When the phosphatase was allowed to react with 32Plabeled substrates and then rapidly denaturated, a 32Plabeled phosphoprotein could be visualized by sodium dodecyl sulfate-polyacrylamide gel ...

Journal: :The Journal of biological chemistry 2000
E E Morrisey S Musco M Y Chen M M Lu J M Leiden M S Parmacek

Gene targeting studies have demonstrated that the zinc finger transcription factor GATA-6 lies upstream in a transcriptional cascade that controls differentiation of the visceral endoderm. To understand the function of GATA-6 in the visceral endoderm and to identify genes regulated by GATA-6 in this tissue, subtractive hybridization was performed using template cDNAs derived from differentiated...

Journal: :Journal of virology 2002
Yingguang Liu Bonita J Biegalke

The human cytomegalovirus (HCMV) virion is a complex structure that contains at least 30 proteins, many of which have been identified. We determined that the HCMV UL35 gene encodes two proteins, including a previously unidentified virion protein. A 22-kDa phosphoprotein (ppUL35(A)) was translated from a 1.2-kb UL35 transcript by 4 h postinfection; a second phosphoprotein of 75 kDa (ppUL35) was ...

Journal: :The Journal of Experimental Medicine 1959
Milton Kern Herman N. Eisen

Isolated lymph node cells incorporate inorganic orthophosphate into a protein fraction. The phosphorylated product is a phosphoprotein. The rate of phosphate incorporation into phosphoprotein was determined in cells isolated from regional lymph nodes at varying times after antigen injection. The rate was unaltered on the 3rd day, but was enhanced on the 4th day after injection. Parallel results...

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