نتایج جستجو برای: ژن hsp70
تعداد نتایج: 22925 فیلتر نتایج به سال:
micrornaها یا mirna ها، rnaهایی کوچک به طول تقریبی 21-22 نوکلئوتید هستند که توسط ژنوم موجود کد شده، هیچ نوع پروتئینی را کد نمی کنند و به عنوان تنظیم کننده های مهم بیان ژن پس از رونویسی در گیاهان و جانوران شناخته شده اند. آن ها از طریق تنظیم منفی ژن های هدف خود، قابلیت تغییر الگوی بیان ژن را در بسیاری از شبکه های رشد، نمو و پاسخ به تنش در گیاهان دارند. آفتابگردان (helianthus annuus l.) گیاهی دیپ...
Heat shock protein 70 (Hsp70) is thought to play a critical role in the thermotolerance of mammalian cells, presumably due to its chaperone activity. We examined the chaperone activity and cellular heat resistance of a clonal cell line in which overexpression of Hsp70 was transiently induced by means of the tetracycline-regulated gene expression system. This single-cell-line approach circumvent...
Although heat-shock protein 70 (HSP70), an evolutionarily highly conserved molecular chaperone, is known to be post-translationally modified in various ways such as phosphorylation, ubiquitination and glycosylation, physiological significance of lysine methylation has never been elucidated. Here we identify dimethylation of HSP70 at Lys-561 by SETD1A. Enhanced HSP70 methylation was detected in ...
Heat shock protein 70 (Hsp70) is a family of proteins with key roles in regulating malignancy. Cancer cells rely on Hsp70 to inhibit apoptosis, regulate senescence and autophagy, and maintain the stability of numerous onco-proteins. Despite these important biological functions in cancer, robust chemical tools that enable the analysis of the Hsp70-regulated proteome in a tumor-by-tumor manner ar...
When purified from a tumor, certain heat shock protein 70 (HSP70)-peptide complexes (PCs) can function as effective vaccines against the tumor from which the complexes were isolated. The immunogenic mechanisms of HSP70 preparations imply that tumor-derived HSP70-PCs exhibit antigens associated with antigen-presenting cells such as dendritic cells ...
BACKGROUND There is increasing evidence that chaperones are also present outside the cell, exerting cytokine-like effects and influencing immune recognition. Hsp70 has been found to be present in human blood sera. Chaperonins Cpn10 and Cpn60 are present in pancreatic juice, but Hsp70 is not. These observations raise the possibility that molecular chaperones may be present in other secretory flu...
Heat shock-binding protein HspBP1 is a member of the Hsp70 co-chaperone family. The interaction between HspBP1 and the ATPase domain of the major heat shock protein Hsp70 up-regulates nucleotide exchange and reduces the affinity between Hsp70 and the peptide in its peptide-binding site. Previously we have shown that Tag7 (also known as peptidoglycan recognition protein PGRP-S), an innate immuni...
Distributions of heat shock protein (HSP)-70 mRNAs and heat shock cognate protein (HSC)-70 mRNAs after 10 min of transient global ischemia were investigated in gerbil forebrain by in situ hybridization using cloned cDNA probes selective for the mRNAs. Expression of HSP70 immunoreactivity was also examined in the same brains. In hippocampal CA1 neuronal cells, in which only a minimal induction o...
Heat shock proteins (HSPs) as stress proteins have vital roles in plant adaptation to biotic and abiotic stresses. These proteins expressed in almost all kinds of stresses and are well known to be contribute in protection of cells. Among them the HSP90, HSP70 and smHSPs have significant roles in cell. In this study, the gene fragments of smHSP, HSP70 and HSP90 from Capparis spinosa L. plant wer...
It has been reported that several proteins [heat shock protein 70 (Hsp70 and Hsc70), annexin II, and tropomyosin 5b] interact with the Ser(256) residue on the COOH terminus of aquaporin-2 (AQP2), where vasopressin-induced phosphorylation occurs for mediating AQP2 trafficking. However, it remains unknown whether these proteins, particularly Hsp70, play a role in AQP2 trafficking. Semiquantitativ...
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