Titlebook: Stress-Inducible Cellular Responses; U. Feige,I. Yahara,B. S. Polla Book 1996 Birkhäuser Verlag 1996 Chaperone.Molekularbiologie.biology.c

corrode

书目名称Stress-Inducible Cellular Responses影响因子(影响力)




书目名称Stress-Inducible Cellular Responses影响因子(影响力)学科排名




书目名称Stress-Inducible Cellular Responses网络公开度




书目名称Stress-Inducible Cellular Responses网络公开度学科排名




书目名称Stress-Inducible Cellular Responses被引频次




书目名称Stress-Inducible Cellular Responses被引频次学科排名




书目名称Stress-Inducible Cellular Responses年度引用




书目名称Stress-Inducible Cellular Responses年度引用学科排名




书目名称Stress-Inducible Cellular Responses读者反馈




书目名称Stress-Inducible Cellular Responses读者反馈学科排名

fleeting

肉身

Anthropoid

Normal protein folding machineryria. Homologous components of this machinery have also been identified in other organelles such as the endoplasmic reticulum in which HSP70 and DnaJ-like homologs reside. The high degree of conservation presumably reflects the proficiency with which these molecules have evolved to mediate the folding of proteins to their native functional states.

Suppository

Experientia Supplementumhttp://image.papertrans.cn/s/image/879646.jpg

uveitis

原谅

Introductionaneous organella. Molecular chaperones assist their substrates in the complexes in folding, assembly and appropriate processing. In addition, dissociation of supramolecular complexes such as clathrin coats occurs only in the presence of molecular chaperones. Finally, degradation of proteins also has

旧式步枪

Protein folding and assembly in the endoplasmic reticulumists of enzymes that promote or stabilize protein folding. The second is composed of proteins termed “molecular chaperones” that bind transiently to nascent polypeptides and apparently prevent misfolding by masking those regions that could lead to incorrect interactions between protein domains or ag

Coordinate

Involvement of molecular chaperones in intracellular protein breakdownry proteins and in the breakdown of certain polyubiquitinated polypeptides by 26S proteasome. It is likley that the chaperones function in proteolysis either as elements that faciliate the recognition of unfolded proteins or that the chaperones partially unfold substrates to make them more susceptib

occult