Results 61 to 70 of about 227,395 (295)
F1000Research, 2018 Background: Mycobacterial α-crystallin (Acr) is a chaperone that prevents misfolding of proteins when Mycobacterium tuberculosis is found in a latent form in the host tissue. Methods: Using insulin as a model substrate and utilizing polynomial graphs, we
Gautam Krishnan, Utpal Roy
doaj +1 more source
A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity. [PDF]
, 2014 Hsp90 is a conserved chaperone that facilitates protein homeostasis. Our crystal structure of the mitochondrial Hsp90, TRAP1, revealed an extension of the N-terminal β-strand previously shown to cross between protomers in the closed state. In this study,
Agard, David A +5 more
core +2 more sources
FEBS Open Bio, EarlyView.Cytosolically synthesized chloroplast preproteins are translocated across the outer and inner envelope membranes through translocons called TOC and TIC, respectively. In green algae and plants, the TIC core is composed of essential membrane proteins, Tic12, Tic20, and Tic214.
Mengyi Li, Xueyang Zhao, Masato Nakai
wiley +1 more source
Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
Journal of Hematology & Oncology, 2018 Heat shock protein 90 (Hsp90) is a critical molecular chaperone protein that regulates the folding, maturation, and stability of a wide variety of proteins.
Ting Li +3 more
doaj +1 more source
Structural characterization of PaFkbA: A periplasmic chaperone from Pseudomonas aeruginosa
Computational and Structural Biotechnology Journal, 2021 Bacterial Mip-like FK506-binding proteins (FKBPs) mostly exhibit peptidyl–prolyl-cis/trans-isomerase (PPIase) and chaperone activities. These activities are associated with various intracellular functions with diverse molecular mechanisms.
Qin Huang +14 more
doaj +1 more source
Evolutionarily divergent DUF4465 domains have a common vitamin B12‐binding function
FEBS Open Bio, EarlyView.We show that DUF4465 family proteins, widespread across bacteria from gut microbiomes, hydrothermal vents, and soil, share a common vitamin B12‐binding function. These augmented β‐jellyroll proteins bind vitamin B12 via extended loops. Our findings establish sequence‐diverse DUF4465 proteins as a widespread class of B12‐binding proteins, highlighting ...
Charlea Clarke +4 more
wiley +1 more source
Chemical chaperone treatment reduces intracellular accumulation of mutant collagen IV and ameliorates the cellular phenotype of a COL4A2 mutation that causes haemorrhagic stroke [PDF]
, 2013 Haemorrhagic stroke accounts for approximately 20% of stroke cases and porencephaly is a clinical consequence of perinatal cerebral haemorrhaging. Here we report the identification of a novel dominant G702D mutation in the collagen domain of COL4A2 ...
Aislynn Taggart +35 more
core +1 more source
FEBS Open Bio, EarlyView.Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane +11 more
wiley +1 more source
The proteostasis network and its decline in ageing
, 2019 Ageing is a major risk factor for the development of many diseases, prominently including neurodegenerative disorders such as Alzheimer disease and Parkinson disease.
Hartl, F., Hipp, M., Kasturi, P.
core +1 more source
Altered Function of the DnaJ Family Cochaperone DNJ-17 Modulates Locomotor Circuit Activity in a Caenorhabditis elegans Seizure Model. [PDF]
, 2016 The highly conserved cochaperone DnaJ/Hsp40 family proteins are known to interact with molecular chaperone Hsp70, and can regulate many cellular processes including protein folding, translocation, and degradation.
Jin, Yishi, Takayanagi-Kiya, Seika
core +2 more sources