Results 61 to 70 of about 147,841 (291)
Applied Sciences, 2021 The chaperone (or chaperoning) system (CS) constitutes molecular chaperones, co-chaperones, and chaperone co-factors, interactors and receptors, and its canonical role is protein quality control.
Federica Scalia +5 more
doaj +1 more source
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
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
Российский офтальмологический журнал, 2018 The literary review focuses on the dysfunction of endoplasmic reticulum (EPR), the role of EPR stress and oxidative stress in the pathogenesis of optic nerve damage.
V. V. Neroev +2 more
doaj +1 more source
Methylglyoxal alters the function and stability of critical components of the protein quality control. [PDF]
PLoS ONE, 2010 BACKGROUND: Increased production and accumulation of methylglyoxal (MGO), as well as increased modification of proteins by glycoxidation, are hallmarks of aging and diabetes.
Carla Figueira Bento +3 more
doaj +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
FEBS Open Bio, EarlyView.Pharmacological inhibition of PERK in a DEN‐induced mouse model of liver cancer does not reduce tumor burden but alters cellular stress signaling. Despite blocking PERK activity, downstream stress responses, including CHOP expression, remain active, suggesting compensatory mechanisms within the unfolded protein response that may influence tumor ...
Ada Lerma‐Clavero +5 more
wiley +1 more source
Probing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics. [PDF]
PLoS ONE, 2012 Deciphering functional mechanisms of the Hsp90 chaperone machinery is an important objective in cancer biology aiming to facilitate discovery of targeted anti-cancer therapies.
Anshuman Dixit, Gennady M Verkhivker
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ATP‐driven molecular chaperone machines [PDF]
Biopolymers, 2013 ABSTRACTThis review is focused on the mechanisms by which ATP binding and hydrolysis drive chaperone machines assisting protein folding and unfolding. A survey of the key, general chaperone systems Hsp70 and Hsp90, and the unfoldase Hsp100 is followed by a focus on the Hsp60 chaperonin machine which is understood in most detail.
Clare, Daniel K, Saibil, Helen R
openaire +2 more sources
Mutant NPM1 in Acute Myeloid Leukemia Initiation and Maintenance
Aging and Cancer, EarlyView.NPM1 mutations drive acute myeloid leukemia by acting as neomorphic transcriptional regulators that cooperate with Menin–MLL and XPO1 to sustain HOX/MEIS1 expression and block differentiation. Targeting these mutant‐specific transcriptional dependencies provides a rational therapeutic strategy for NPM1‐mutated AML.
Yanan Jiang +3 more
wiley +1 more source