Results 201 to 210 of about 63,350 (232)

Lon/Pim1-mediated degradation of presequence translocase-associated motor components Pam16 and Pam18 in Saccharomyces cerevisiae. [PDF]

Biochem J
Boggula Y, Chatterjee A, Simaiya G, Pal A, Srinivasan A, Sepuri NBV.   +5 more
europepmc   +1 more source

Cryo-EM structures of human ClpXP reveal mechanisms of assembly and proteolytic activation. [PDF]

Nat Commun
Chen W, Lander GC, Yang J.
europepmc   +1 more source

[Regulation of salmonella systemic infection by AAA+ proteases].

Nihon saikingaku zasshi. Japanese journal of bacteriology, 2006
openaire   +1 more source

Some of the next articles are maybe not open access.

Related searches:

Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease

Nature, 1999
The AAA domain, a conserved Walker-type ATPase module, is a feature of members of the AAA family of proteins, which are involved in many cellular processes, including vesicular transport, organelle biogenesis, microtubule rearrangement and protein degradation. The function of the AAA domain, however, has not been explained.
Thomas Langer
exaly   +4 more sources

Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases

Nature Reviews Microbiology, 2009
Members of the AAA+ protein superfamily contribute to many diverse aspects of protein homeostasis in prokaryotic cells. As a fundamental component of numerous proteolytic machines in bacteria, AAA+ proteins play a crucial part not only in general protein quality control but also in the regulation of developmental programmes, through the controlled ...
Janine Kirstein, Kürşad Turgay, David A Dougan   +2 more
exaly   +3 more sources

Mitochondrial AAA+ proteases

2023
Mitochondria are multifunctional organelles that play a central role in a wide range of life-sustaining tasks in eukaryotic cells, including adenosine triphosphate (ATP) production, calcium storage and coenzyme generation pathways such as iron-sulfur cluster biosynthesis.
openaire   +2 more sources

AAA+ Proteases: ATP-Fueled Machines of Protein Destruction

Annual Review of Biochemistry, 2011
AAA+ family proteolytic machines (ClpXP, ClpAP, ClpCP, HslUV, Lon, FtsH, PAN/20S, and the 26S proteasome) perform protein quality control and are used in regulatory circuits in all cells. These machines contain a compartmental protease, with active sites sequestered in an interior chamber, and a hexameric ring of AAA+ ATPases.
Robert T, Sauer, Tania A, Baker
openaire   +2 more sources

Discovery of AAA+ Protease Substrates through Trapping Approaches

Trends in Biochemical Sciences, 2019
Proteases play essential roles in cellular proteostasis. Mechanisms through which proteases recognize their substrates are often hard to predict and therefore require experimentation. In vivo trapping allows systematic identification of potential substrates of proteases, their adaptors, and chaperones.
Jui-Yun Rei Liao, Klaas J. van Wijk
openaire   +2 more sources

Principles of AAA+ Proteases

2022
ATPases associated with diverse cellular activities (AAA+) proteases in bacteria help maintain protein homeostasis by degrading misfolded and regulatory proteins. While a handful of protein targets for these proteases have been identified in Caulobacter crescentus and other organisms, more research is needed to elucidate mechanisms that govern ...
openaire   +1 more source

Nucleotide-dependent substrate recognition by the AAA+ HslUV protease

Nature Structural & Molecular Biology, 2005
ATP-dependent protein degradation is controlled principally by substrate recognition. The AAA+ HslU ATPase is thought to bind protein substrates, denature them, and translocate the unfolded polypeptide into the HslV peptidase. The lack of well-behaved high-affinity substrates for HslUV (ClpYQ) has hampered understanding of the rules and mechanism of ...
Randall E, Burton, Tania A, Baker, Robert T, Sauer   +2 more
openaire   +2 more sources