نتایج جستجو برای: نسخۀ cbl is 1417

تعداد نتایج: 7239389  

Journal: :The Journal of biological chemistry 2003
Yuko Miura-Shimura Lei Duan Navin L Rao Alagarsamy L Reddi Hideki Shimura Rob Rottapel Brain J Druker Alexander Tsygankov Vimla Band Hamid Band

The Cbl ubiquitin ligase has emerged as a negative regulator of receptor and non-receptor tyrosine kinases. Cbl is known to associate with the proto-oncogene product Vav, a hematopoietic-restricted Rac guanine nucleotide exchange factor, but the consequences of this interaction remain to be elucidated. Using immortalized T cell lines from Cbl(+/+) and Cbl(-/-) mice, and transfection analyses in...

Journal: :Development 2017
Bhopal Mohapatra Neha Zutshi Wei An Benjamin Goetz Priyanka Arya Timothy A Bielecki Insha Mustaq Matthew D Storck Jane L Meza Vimla Band Hamid Band

The ubiquitin ligases CBL and CBL-B are negative regulators of tyrosine kinase signaling with established roles in the immune system. However, their physiological roles in epithelial tissues are unknown. Here, we used MMTV-Cre-mediated Cbl gene deletion on a Cbl-b null background, as well as a tamoxifen-inducible mammary stem cell (MaSC)-specific Cbl and Cbl-b double knockout (Cbl/Cbl-b DKO) us...

Journal: :Archives of neurology 2003
David S Saperstein Gil I Wolfe Gary S Gronseth Sharon P Nations Laura L Herbelin Wilson W Bryan Richard J Barohn

BACKGROUND Diagnosing cobalamin (Cbl) deficiency as a cause of polyneuropathy (PN) is problematic, as the frequency of both disorders increases with age, and serum Cbl levels can be difficult to interpret. OBJECTIVES To identify unique clinical or laboratory features among PN patients with Cbl deficiency and to examine the role of testing of serum metabolite levels in the identification of Cb...

Journal: :Blood 2011
Lorena Buitrago Wallace Y Langdon Archana Sanjay Satya P Kunapuli

c-Cbl protein functions as an E3 ligase and scaffolding protein, where 3 residues, Y700, Y731, and Y774, upon phosphorylation, have been shown to initiate several signaling cascades. In this study, we investigated the role of these phospho-tyrosine residues in the platelet functional responses after integrin engagement. We observed that c-Cbl Y700, Y731 and Y774 undergo phosphorylation upon pla...

Journal: :Blood 2007
Bülent Sargin Chunaram Choudhary Nicola Crosetto Mirko H H Schmidt Rebekka Grundler Marion Rensinghoff Christine Thiessen Lara Tickenbrock Joachim Schwäble Christian Brandts Benjamin August Steffen Koschmieder Srinivasa Rao Bandi Justus Duyster Wolfgang E Berdel Carsten Müller-Tidow Ivan Dikic Hubert Serve

In acute myeloid leukemia (AML), mutational activation of the receptor tyrosine kinase (RTK) Flt3 is frequently involved in leukemic transformation. However, little is known about a possible role of highly expressed wild-type Flt3 in AML. The proto-oncogene c-Cbl is an important regulator of RTK signaling, acting through its ubiquitin ligase activity and as a platform for several signaling adap...

2007
Bülent Sargin Chunaram Choudhary Nicola Crosetto Mirko H.H. Schmidt Marion Rensinghoff Christine Thiessen Lara Tickenbrock Joachim Schwäble Christian Brandts Benjamin August Steffen Koschmieder Srinivasa Rao Bandi Wolfgang E. Berdel Carsten Müller-Tidow Ivan Dikic Hubert Serve

*BS and CC contributed equally to the work presented hereAbstract In acute myeloid leukemia (AML), mutational activation of the receptor tyrosine kinase (RTK) Flt3 is frequently involved in leukemic transformation. However, little is known about a possible role of highly expressed wild-type Flt3 in AML. The proto-oncogene c-Cbl is an important regulator of RTK signaling, acting through its ubiq...

Journal: :The Journal of biological chemistry 2001
S A Ettenberg A Magnifico M Cuello M M Nau Y R Rubinstein Y Yarden A M Weissman S Lipkowitz

Cbl proteins function as ubiquitin protein ligases for the activated epidermal growth factor receptor and, thus, negatively regulate its activity. Here we show that Cbl-b is ubiquitinated and degraded upon activation of the receptor. Epidermal growth factor (EGF)-induced Cbl-b degradation requires intact RING finger and tyrosine kinase binding domains and requires binding of the Cbl-b protein t...

Journal: :Current Biology 1999
Zhihong Zhang Chris Elly Ling Qiu Amnon Altman Yun-Cai Liu

Engagement of the T-cell receptor (TCR)-CD3 complex induces a rapid increase in the activities of Src-family and Syk/Zap-70-family kinases [1] [2]. These activated kinases then induce the tyrosine phosphorylation of multiple intracellular proteins, eventually leading to T-cell activation. One of the prominent substrates for these kinases is the adaptor protein Cbl [3] and recent studies suggest...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1975
L E Rosenberg L Patel A C Lilljeqvist

Three distinct classes of human mutations (cbl A, cbl B, and cbl C) cause defective synthesis of cobalamin (Cbl; vitamin B(12)) coenzymes. Cultured fibroblasts from that unique class (cbl C) deficient in the synthesis of both Cbl coenzymes, 5'-deoxyadenosylcobalamin (AdoCbl) and methylcobalamin (MeCbl), were used to explore the underlying defect. We compared the uptake of transcobalamin II(TC I...

Journal: :Endocrinology 2004
Ana C P Thirone José B C Carvalheira Aparecida E Hirata Lício A Velloso Mario J A Saad

The phosphatidylinositol 3-kinase-independent pathway to induce glucose transport may involve the tyrosine phosphorylation of the protooncogene c-Cbl. In the present study, we examined whether acute exposure to insulin stimulates the tyrosine phosphorylation of Cbl and its association with Cbl-associated protein (CAP) in muscle and adipose tissue of rats in vivo. We report herein that insulin i...

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