Results 11 to 20 of about 287,054 (305)

Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone [PDF]

, 2012
Proteins are subject to continuous quality control for optimal proteostasis. The knowledge of peroxisome quality control systems is still in its infancy. Here we show that peroxisomes contain a member of the Lon family of proteases (Pln).
Aksam, Antonenkov, Arnold, Bartoszewska, Bender, Bota, Buchner, Dobson, Ellis, Fraaije, Franke, Goldberg, Guinier, Hanson, Hartl, Hillenga, Islinger, Iyer, Jaenicke, Jahn, Kiel, Kiel, Kikuchi, Kozin, Lee, Lingard, Liu, Meijer, Nettleship, Nijland, Okumoto, Omi, Opaliński, Paraszkiewicz, Petoukhov, Petoukhov, Petoukhov, Powers, Quiocho, Reeder, Rep, Roessle, Roudiak, Sambrook, Sauer, Stahlberg, Steinberg, Svergun, Tyedmers, van Dijken, van Roermund, Venkatesh, Volkov, von Janowsky, Wagner, Walton, Wanders, Waterham, West   +58 more
core   +4 more sources

Donor-strand exchange in chaperone-assisted pilus assembly revealed in atomic detail by molecular dynamics [PDF]

, 2008
Adhesive multi-subunit fibres are assembled on the surface of many pathogenic bacteria via the chaperone-usher pathway. In the periplasm, a chaperone donates a β-strand to a pilus subunit to complement its incomplete immunoglobulin-like fold.
Ashcroft, A.E., Paci, E., Radford, S.E., Rose, R.J., Waksman, G., Welsh, T.S.   +5 more
core   +1 more source

Chain-Selective Isotopic Labeling of the Heterodimeric Type III Secretion Chaperone, Scc4:Scc1, Reveals the Total Structural Rearrangement of the Chlamydia trachomatis Bi-Functional Protein, Scc4

Biomolecules, 2020
Scc4 is an unusual bi-functional protein from Chlamydia trachomatis (CT) that functions as a type III secretion system (T3SS) chaperone and an RNA polymerase (RNAP)-binding protein.
Thilini O. Ukwaththage, Samantha M. Keane, Li Shen, Megan A. Macnaughtan   +3 more
doaj   +1 more source

Small heat-shock proteins: important players in regulating cellular proteostasis [PDF]

, 2015
Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection.
Carver, John A., Ecroyd, Heath, Meehan, Sarah, Treweek, Teresa M.   +3 more
core   +1 more source

DnaK3 Is Involved in Biogenesis and/or Maintenance of Thylakoid Membrane Protein Complexes in the Cyanobacterium Synechocystis sp. PCC 6803

Life, 2020
DnaK3, a highly conserved cyanobacterial chaperone of the Hsp70 family, binds to cyanobacterial thylakoid membranes, and an involvement of DnaK3 in the biogenesis of thylakoid membranes has been suggested. As shown here, light triggers synthesis of DnaK3
Adrien Thurotte, Tobias Seidel, Ruven Jilly, Uwe Kahmann, Dirk Schneider   +4 more
doaj   +1 more source

Extragenic Suppression analysis of TS mutations using Sec61p [PDF]

, 2007
During synthesis, secretory and membrane proteins are cotranslationally translocated into the lumen of the endoplasmic reticulum through an aqueous gated channel.
Sterling Smith
core   +2 more sources

Mechanistic Insight Into the Interaction Between Helicobacter pylori Urease Subunit α and Its Molecular Chaperone Hsp60

Frontiers in Microbiology, 2019
Helicobacter pylori is the etiologic agent in a variety of gastroduodenal diseases. As its key pathogenic factors, both urease and Hsp60 play important roles in the pathogenesis of H. pylori.
Huilin Zhao, Yulong Wu, Zheng Xu, Ran Ma, Yunfei Ding, Xuelian Bai, Qianyu Rong, Ying Zhang, Boqing Li, Xiaofei Ji   +9 more
doaj   +1 more source

Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Ubiquitylation as a Novel Pharmaceutical Target for Cystic Fibrosis

Pharmaceuticals, 2020
Mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene decrease the structural stability and function of the CFTR protein, resulting in cystic fibrosis. Recently, the effect of CFTR-targeting combination therapy has dramatically
Ryosuke Fukuda, Tsukasa Okiyoneda
doaj   +1 more source

Dynamic Activity of Histone H3-Specific Chaperone Complexes in Oncogenesis

Frontiers in Oncology, 2022
Canonical histone H3.1 and variant H3.3 deposit at different sites of the chromatin via distinct histone chaperones. Histone H3.1 relies on chaperone CAF-1 to mediate replication-dependent nucleosome assembly during S-phase, while H3.3 variant is ...
Ting Wen, Qiao Yi Chen
doaj   +1 more source

The SseC translocon component in Salmonella enterica serovar Typhimurium is chaperoned by SscA [PDF]

, 2013
Background: Salmonella enterica is a causative agent of foodborne gastroenteritis and the systemic disease known as typhoid fever. This bacterium uses two type three secretion systems (T3SSs) to translocate protein effectors into host cells to manipulate
Allison, Sarah E, Coombes, Brian K, Cooper, Colin A, Mulder, David T, Pilar, Ana Victoria C   +4 more
core   +1 more source