نتایج جستجو برای: bip

تعداد نتایج: 2004  

Journal: :Biochemistry 2010
Craig A Belon Yoji D High Tse-I Lin Frederik Pauwels David N Frick

This study examines the effects of 1-N,4-N-bis[4-(1H-benzimidazol-2-yl)phenyl]benzene-1,4-dicarboxamide ((BIP)(2)B) on the NS3 helicase encoded by the hepatitis C virus (HCV). Molecular beacon-based helicase assays were used to show that (BIP)(2)B inhibits the ability of HCV helicase to separate a variety of RNA and DNA duplexes with half-maximal inhibitory concentrations ranging from 0.7 to 5 ...

Journal: :The Journal of biological chemistry 2001
A M Romeo L Christen E G Niles D J Kosman

The efficient replication of large DNA viruses requires dNTPs supplied by a viral ribonucleotide reductase. Viral ribonucleotide reductase is an early gene product of both vaccinia and herpes simplex virus. For productive infection, the apoprotein must scavenge iron from the endogenous, labile iron pool(s). The membrane-permeant, intracellular Fe(2+) chelator, 2,2'-bipyridine (bipyridyl, BIP), ...

Journal: :The Plant cell 1998
Crofts Leborgne-Castel Pesca Vitale Denecke

BiP is found in association with calreticulin, both in the presence and absence of endoplasmic reticulum stress. Although the BiP-calreticulin complex can be disrupted by ATP, several properties suggest that the calreticulin associated with BiP is neither unfolded nor partially or improperly folded. (1) The complex is stable in vivo and does not dissociate during 8 hr of chase. (2) When present...

Journal: :Nucleic acids research 2001
Y K Kim S H Back J Rho S H Lee S K Jang

Translational initiation of the human BiP mRNA is directed by an internal ribosomal entry site (IRES) located in the 5'-untranslated region (5'-UTR). In order to understand the mechanism of the IRES-dependent translation of BiP mRNA, cellular proteins interacting with the BiP IRES were investigated. La autoantigen, which augments the translation of polioviral mRNA and hepatitis C viral mRNA, bo...

Journal: :International Journal on Software Tools for Technology Transfer 2021

DR-BIP is an extension of the BIP component framework intended for programming reconfigurable systems encompassing various aspects dynamism. It relies on architectural motifs to structure architecture a system and coordinate its reconfiguration at runtime. An motif defines set interacting components that evolve according rules. With DR-BIP, dynamism can be captured as inter-play dynamic changes...

Journal: :The Journal of Cell Biology 1999
Rachel Hellman Marc Vanhove Annabelle Lejeune Fred J. Stevens Linda M. Hendershot

Immunoglobulin heavy chain-binding protein (BiP) is a member of the hsp70 family of chaperones and one of the most abundant proteins in the ER lumen. It is known to interact transiently with many nascent proteins as they enter the ER and more stably with protein subunits produced in stoichiometric excess or with mutant proteins. However, there also exists a large number of secretory pathway pro...

Journal: :Plant physiology 2011
Pedro A A Reis Gustavo L Rosado Lucas A C Silva Luciana C Oliveira Lucas B Oliveira Maximiller D L Costa Fátima C Alvim Elizabeth P B Fontes

The molecular chaperone binding protein (BiP) participates in the constitutive function of the endoplasmic reticulum (ER) and protects the cell against stresses. In this study, we investigated the underlying mechanism by which BiP protects plant cells from stress-induced cell death. We found that enhanced expression of BiP in soybean (Glycine max) attenuated ER stress- and osmotic stress-mediat...

Journal: :Plant physiology 2001
F C Alvim S M Carolino J C Cascardo C C Nunes C A Martinez W C Otoni E P Fontes

The binding protein (BiP) is an important component of endoplasmic reticulum stress response of cells. Despite extensive studies in cultured cells, a protective function of BiP against stress has not yet been demonstrated in whole multicellular organisms. Here, we have obtained transgenic tobacco (Nicotiana tabacum L. cv Havana) plants constitutively expressing elevated levels of BiP or its ant...

Journal: :The Journal of Cell Biology 1990
L M Hendershot

Immunoglobulin heavy chain binding protein (BiP, GRP78) associates stably with the free, nonsecreted Ig heavy chains synthesized by Abelson virus transformed pre-B cell lines. In cells synthesizing both Ig heavy and light chains, the Ig subunits assemble rapidly and are secreted. Only incompletely assembled Ig molecules can be found bound to BiP in these cells. In addition to Ig heavy chains, a...

2015
Steffen Preissler Cláudia Rato Ruming Chen Robin Antrobus Shujing Ding Ian M Fearnley David Ron

The endoplasmic reticulum (ER)-localized Hsp70 chaperone BiP affects protein folding homeostasis and the response to ER stress. Reversible inactivating covalent modification of BiP is believed to contribute to the balance between chaperones and unfolded ER proteins, but the nature of this modification has so far been hinted at indirectly. We report that deletion of FICD, a gene encoding an ER-l...

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