Results 51 to 60 of about 80,587 (292)

20S Proteasome Assembly: Alternative Pathways and Complexes

open access: yes, 2017
The ubiquitin-proteasome system is responsible for the targeted degradation of proteins within the cell. The 26S proteasome, which is the protease of this system, is a high molecular weight complex consisting of 33 subunits that arrange to form two ...
Hammack, Lindsay J, Hammack, Lindsay J.
core   +2 more sources

Dissecting the assembly pathway of the 20S proteasome

open access: yesFEBS Letters, 1997
Proteasomes reach their mature active state via a complex cascade of folding, assembly and processing events. The Rhodococcus proteasome offers a means to dissect the assembly pathway and to characterize intermediates; its four subunits (α1, α2, β1, β2) assemble efficiently in vitro with any combination of α and β. Assembly studies with wild‐type and N‐
Zühl, F.   +3 more
openaire   +3 more sources

Redox Control of 20S Proteasome Gating [PDF]

open access: yesAntioxidants & Redox Signaling, 2012
The proteasome is the primary contributor in intracellular proteolysis. Oxidized or unstructured proteins can be degraded via a ubiquitin- and ATP-independent process by the free 20S proteasome (20SPT). The mechanism by which these proteins enter the catalytic chamber is not understood thus far, although the 20SPT gating conformation is considered to ...
Gustavo M, Silva   +10 more
openaire   +2 more sources

Microbiome−host proteostasis crosstalk—An emerging perspective on mechanisms and interventions toward healthy longevity

open access: yesFEBS Letters, EarlyView.
Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley   +1 more source

Sex-specific adaptive homeostasis in D. melanogaster depends on increased proteolysis by the 20S Proteasome: Data-in-Brief

open access: yesData in Brief, 2018
Adaptive homeostasis enables rapid cellular signaling, leading to transcriptional and translational modifications (Davies, 2016) [1]. The Proteasome is one of the main cellular proteolytic enzymes that plays an essential role in the rapid clearance of ...
Laura C.D. Pomatto   +3 more
doaj   +1 more source

Nutrient/TOR signaling controls adipose mitochondrial transcription factor A (TFAM) to regulate organismal growth in Drosophila

open access: yesFEBS Letters, EarlyView.
Animals must match their growth rate to available nutrients. We show that in Drosophila larvae, the nutrient‐sensing TOR kinase controls growth by regulating levels of TFAM, a key regulator of mitochondrial function, in the adipose tissue. When nutrients are abundant, high TOR activity suppresses TFAM, lowering mitochondrial bioenergetic activity and ...
Shrivani Sriskanthadevan‐Pirahas   +4 more
wiley   +1 more source

The microbiome in human skin aging

open access: yesFEBS Letters, EarlyView.
Age‐related skin changes encompass the well‐known visible phenotypic alterations, together with microbiome dysbiosis and a series of molecular aging hallmarks. These hallmarks characterize not only a fully stablished aged phenotype but also the skin aging process itself.
Manuel Huerta Arana   +3 more
wiley   +1 more source

The ubiquitin system in normal and infected germinal center B cells

open access: yesFEBS Letters, EarlyView.
The ubiquitin system plays a central role in germinal center (GC) B cells, influencing differentiation to long‐lived memory B cells. Oncogenic gammaherpesviruses gain access to memory B cells by establishing latency in GC B cells. Mapping ubiquitin mechanisms in normal and infected GC B cells will define specific molecular circuits in B cells germane ...
Destiny Davis   +2 more
wiley   +1 more source

The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag

open access: yesNature Communications, 2021
The 20S particle is part of the 26S proteasome, but also exists as a free complex. Here, the authors outline signature activities of the 20S and combine chemical, structural, functional and proteomic assays to show that the 20S can degrade ubiquitin tags
Indrajit Sahu   +14 more
doaj   +1 more source

Silybins are stereospecific regulators of the 20S proteasome

open access: yesBioorganic & Medicinal Chemistry, 2022
A reduced proteasome activity tiles excessive amyloid growth during the progress of protein conformational diseases (PCDs). Hence, the development of safe and effective proteasome enhancers represents an attractive target for the therapeutic treatment of these chronic disorders.
Persico, Marco   +11 more
openaire   +7 more sources

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