نتایج جستجو برای: dimerization

تعداد نتایج: 10337  

2014
Jingjing Qi Na Li Kun Fan Peng Yin Chao Zhao Zengxia Li Yi Lin Liying Wang Xiliang Zha

Receptor-like protein tyrosine phosphatases (RPTPs) are type I transmembrane glycoproteins with N-glycans whose catalytic activities are regulated by dimerization. However, the intrinsic mechanism involved in dimerizing processes remains obscure. In this study, receptor protein tyrosine phosphatase rho (PTPRT) is identified as a novel substrate of N-Acetylglucosaminyltransferase V (GnT-V). We s...

2003
GRADY SMITHS

Lysine or Mg2+ alone at high concentrations brings about partial dimerization of the lysine-sensitive aspartokinase of Escherichia coli B. The native enzyme, which has a molecular weight of 75,300 and consists of 2 subunits, responds to a combination of lysine and Mg 2+ at much lower concentrations by dimerizing to a tetrameric molecule with a molecular weight approaching 150,000. This dimeriza...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1997
C A Blau K R Peterson J G Drachman D M Spencer

Receptor dimerization is the key signaling event for many cytokines, including erythropoietin. A system has been recently developed that permits intracellular protein dimerization to be reversibly activated in response to a lipid-soluble dimeric form of the drug FK506, called FK1012. FK1012 is used as a pharmacological mediator of dimerization to bring together FK506 binding domains, taken from...

Journal: :Cell 1998
Andrei V Khokhlatchev Bertram Canagarajah Julie Wilsbacher Megan Robinson Mark Atkinson Elizabeth Goldsmith Melanie H Cobb

The MAP kinase ERK2 is widely involved in eukaryotic signal transduction. Upon activation it translocates to the nucleus of the stimulated cell, where it phosphorylates nuclear targets. We find that nuclear accumulation of microinjected ERK2 depends on its phosphorylation state rather than on its activity or on upstream components of its signaling pathway. Phosphorylated ERK2 forms dimers with ...

Journal: :Molecular cell 2001
L Fairall L Chapman H Moss T de Lange D Rhodes

TRF1 and TRF2 are key components of vertebrate telomeres. They bind to double-stranded telomeric DNA as homodimers. Dimerization involves the TRF homology (TRFH) domain, which also mediates interactions with other telomeric proteins. The crystal structures of the dimerization domains from human TRF1 and TRF2 were determined at 2.9 and 2.2 A resolution, respectively. Despite a modest sequence id...

Journal: :Journal of computer-aided molecular design 2000
Amedeo Caflisch Hans J. Schramm Martin Karplus

Inhibition of dimerization to the active form of the HIV-1 aspartic proteinase (HIV-1 PR) may be a way to decrease the probability of escape mutations for this viral protein. The Multiple Copy Simultaneous Search (MCSS) methodology was used to generate functionality maps for the dimerization interface of HIV-1 PR. The positions of the MCSS minima of 19 organic fragments, once postprocessed to t...

Journal: :Physical review. B, Condensed matter 1994
Penc Mila

We propose a quantitative estimate of the charge gap that opens in the onedimensional dimerized Hubbard model at quarter-filling due to dimerization, which makes the system effectively half–filled, and to repulsion, which induces umklapp scattering processes. Our estimate is expected to be valid for any value of the repulsion and of the parameter describing the dimerization. It is based on anal...

2014
Natalia Tschowri Maria A. Schumacher Susan Schlimpert Naga babu Chinnam Kim C. Findlay Richard G. Brennan Mark J. Buttner

The cyclic dinucleotide c-di-GMP is a signaling molecule with diverse functions in cellular physiology. Here, we report that c-di-GMP can assemble into a tetramer that mediates the effective dimerization of a transcription factor, BldD, which controls the progression of multicellular differentiation in sporulating actinomycete bacteria. BldD represses expression of sporulation genes during vege...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1999
B S Wang C O Pabo

Peptides that mediate dimerization of attached zinc finger DNA-binding domains have been evolved in vitro starting from random sequences. We first used phage display to select dimerization elements from libraries of random 15-residue polypeptides that were fused to the N terminus of the zinc finger domains. We then reoptimized these peptides by sequentially randomizing five-residue blocks (proc...

Journal: :EMBO reports 2005
Qian Wang Greg Villeneuve Zhixiang Wang

Given that ligand binding is essential for the rapid internalization of epidermal growth factor receptor (EGFR), the events induced by ligand binding probably contribute to the regulation of EGFR internalization. These events include receptor dimerization, activation of intrinsic tyrosine kinase activity and autophosphorylation. Whereas the initial results are controversial regarding the role o...

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