Results 61 to 70 of about 3,365 (168)

N-Terminal Coiled-Coil Structure of ATPase Subunits of 26S Proteasome Is Crucial for Proteasome Function. [PDF]

open access: yesPLoS ONE, 2015
The proteasome is an essential proteolytic machine in eukaryotic cells, where it removes damaged proteins and regulates many cellular activities by degrading ubiquitinated proteins.
Tomonao Inobe, Reiko Genmei
doaj   +1 more source

Molecular Mechanisms Driving and Regulating the AAA+ ATPase VCP/p97, an Important Therapeutic Target for Treating Cancer, Neurological and Infectious Diseases

open access: yesBiomolecules, 2023
p97/VCP, a highly conserved type II ATPase associated with diverse cellular activities (AAA+ ATPase), is an important therapeutic target in the treatment of neurodegenerative diseases and cancer.
Sepideh Valimehr   +5 more
doaj   +1 more source

Pushing the limits of atomic force microscopy: Emerging methods for speed, resolution, and quantitative analysis

open access: yesJournal of Microscopy, EarlyView.
Abstract Since its introduction 40 years ago, atomic force microscopy (AFM) has transformed nanoscale imaging across the physical and life sciences. In biology, AFM has provided unprecedented insights into nanoscale biomolecular organisation under near‐physiological conditions, revealing structures and interactions inaccessible to many conventional ...
Yueqi Wang   +5 more
wiley   +1 more source

The N1 domain of the peroxisomal AAA-ATPase Pex6 is required for Pex15 binding and proper assembly with Pex1 [PDF]

open access: yes
The heterohexameric ATPases associated with diverse cellular activities (AAA)-ATPase Pex1/Pex6 is essential for the formation and maintenance of peroxisomes.
Judy, Ryan M   +9 more
core   +1 more source

Visualizing maturation factor extraction from the nascent ribosome by the AAA-ATPase Drg1. [PDF]

open access: yes, 2022
The AAA-ATPase Drg1 is a key factor in eukaryotic ribosome biogenesis that initiates cytoplasmic maturation of the large ribosomal subunit. Drg1 releases the shuttling maturation factor Rlp24 from pre-60S particles shortly after nuclear export, a strict ...
Loibl, Mathias   +13 more
core   +12 more sources

ATPase family AAA domain-containing 3A is a novel anti-apoptotic factor in lung adenocarcinoma cells

open access: yes, 2014
AAA domain-containing 3A (ATAD3A) is a member of the AAA-ATPase family. Three forms of ATAD3 have been identified: ATAD3A, ATAD3B and ATAD3C. In this study, we examined the type and expression of ATAD3 in lung adenocarcinoma (LADC).
Ko, W.J.   +17 more
core   +2 more sources

Viral hijacking of a replicative helicase loader and its implications for helicase loading control and phage replication

open access: yeseLife, 2016
Replisome assembly requires the loading of replicative hexameric helicases onto origins by AAA+ ATPases. How loader activity is appropriately controlled remains unclear.
Iris V Hood, James M Berger
doaj   +1 more source

Nucleotide-dependent conformational changes of the AAA+ ATPase p97 revisited [PDF]

open access: yes, 2016
The ubiquitous AAA-ATPase p97 segregates ubiquitylated proteins from their molecular environment. Previous studies of the nucleotide-dependent conformational changes of p97 were inconclusive.
Heck, Albert J R   +17 more
core   +1 more source

Developmental mechanisms contributing to non‐linear firing dynamics in spinal motoneurons of the postnatal mouse

open access: yesThe Journal of Physiology, EarlyView.
Abstract figure legend. In this study, we describe how persistent inward currents (PICs) and nonlinear firing dynamics mature in slow‐type (green) and fast‐type (purple) motoneurons (MNs) during the second and third postnatal weeks of development in mice.
Simon A. Sharples, Gareth B. Miles
wiley   +1 more source

AAA+ ATPases: structural insertions under the magnifying glass

open access: yesCurrent Opinion in Structural Biology, 2021
AAA+ ATPases are a diverse protein superfamily which power a vast number of cellular processes, from protein degradation to genome replication and ribosome biogenesis. The latest advances in cryo-EM have resulted in a spectacular increase in the number and quality of AAA+ ATPase structures.
Jessop, Matthew   +2 more
openaire   +4 more sources

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