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Protein folding assisted by chaperones
(Bentham Science Publ LtdSharjahEmirados Árabes Unidos, 2005)
The biology of molecular chaperones: very complex activities for quite simple proteins
(Bentham Science Publishers, 2014-04-30)
From a social perspective, the term chaperone refers to a person, usually a matron, who used to accompany young ladies in public and supervise young people at a social gathering to ensure proper behavior. By analogy, ...
ER chaperones in neurodegenerative disease: Folding and beyond
(Elsevier, 2016)
Proteins along the secretory pathway are co-translationally translocated into the lumen of the endoplasmic reticulum (ER) as unfolded polypeptide chains. Afterwards, they are usually modified with N-linked glycans, correctly ...
Heat causes oligomeric disassembly and increases the chaperone activity of small heat shock proteins from sugarcane
(Elsevier France-editions Scientifiques Medicales ElsevierParisFrança, 2010)
Chaperones and their role in telomerase ribonucleoprotein biogenesis and telomere maintenance
(2019-01-01)
Telomere length maintenance is important for genome stability and cell division. In most eukaryotes, telomeres are maintained by the telomerase ribonucleoprotein (RNP) complex, minimally composed of the Telomerase Reverse ...
Biochemical and biophysical characterization of small heat shock proteins from sugarcane Involvement of a specific region located at the N-terminus with substrate specificity
(Pergamon-elsevier Science LtdOxfordInglaterra, 2007)
Characterization of the accessory protein ClpT1 from Arabidopsis thaliana: oligomerization status and interaction with Hsp100 chaperones
(Biomed Central, 2014-08)
El presente articulo se encuentra aceptado con modificaciones. Background: The caseinolytic protease (Clp) is crucial for chloroplast biogenesis and proteostasis. The Arabidopsis Clp consists of two heptameric rings (P ...
The Interplay between Calcium and the in Vitro Lectin and Chaperone Activities of Calreticulin
(American Chemical Society, 2007-03)
The ER resident protein calreticulin fulfills at least two important roles. It works as a chaperone preventing Golgi exit of non-native protein species and enhancing protein folding efficiency in either N-glycan-dependent, ...