Results 61 to 70 of about 94,343 (283)

Mixed‐class J‐domain protein scaffolds promote expanded aggregate handling and multivalent Hsp70 engagement during functional disaggregase assembly

open access: yesFEBS Letters, EarlyView.
Protein aggregates threaten proteostasis and cell health. In human cells, Hsp70–J‐domain protein‐based disaggregases remove aggregates, but how they assemble remains unclear. Our biochemical findings show that DNAJA2‐ and DNAJB1‐containing disaggregase scaffolds enhance luciferase aggregate targeting, and that Hsp70 recruitment by both J‐domain ...
Anna Szlachcic, Nadinath B. Nillegoda
wiley   +1 more source

Interaction of human heat shock protein 70 with tumor-associated peptides [PDF]

open access: yes, 2009
Molecular chaperones of the heat shock protein 70 (Hsp70) family play a crucial role in the presentation of exogenous antigenic peptides by antigen-presenting cells (APCs).
Manzenrieder, Florian   +20 more
core   +1 more source

YlmG1 is localized exclusively to the chloroplast envelope membrane and is involved in preprotein translocation in Arabidopsis thaliana

open access: yesFEBS 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

The Neurochaperonopathies: Anomalies of the Chaperone System with Pathogenic Effects in Neurodegenerative and Neuromuscular Disorders

open access: yesApplied 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

Molecular chaperones: Pathways and networks [PDF]

open access: yes, 1999
Some proteins synthesized by growing eukaryotic cells are transferred along unidirectional pathways of molecular chaperones until the risk of aggregation has decreased and they can be released safely.
John Ellis, R., R. John Ellis
core   +1 more source

Chemical Chaperones Modulate the Formation of Metabolite Assemblies [PDF]

open access: yes, 2021
The formation of amyloid-like structures by metabolites is associated with several inborn errors of metabolism (IEMs). These structures display most of the biological, chemical and physical properties of protein amyloids.
Shai Karidi-Heller   +10 more
core   +1 more source

Evolutionarily divergent DUF4465 domains have a common vitamin B12‐binding function

open access: yesFEBS 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

Pharmacological therapies for monogenic obesity caused by MC4R dysfunction [PDF]

open access: yes, 2010
PhDMutations in the melanocortin-4 receptor (MC4R) are the most common cause of monogenic obesity. The majority of MC4R mutations are predicted to cause the receptor to aberrantly fold.
Gooljar, Sakina B
core  

Large‐scale bidirectional arrayed genetic screens identify OXR1 and EMC4 as modifiers of αSynuclein aggregation

open access: yesFEBS 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

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