Results 41 to 50 of about 234,152 (246)

Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor

Cell Reports, 2019
Summary: AAA+ proteins form asymmetric hexameric rings that hydrolyze ATP and thread substrate proteins through a central channel via mobile substrate-binding pore loops.
Célia Deville, Kamila Franke, Axel Mogk, Bernd Bukau, Helen R. Saibil   +4 more
doaj   +1 more source

The AAA + ATPase Thorase is neuroprotective against ischemic injury [PDF]

Journal of Cerebral Blood Flow & Metabolism, 2019
Neuronal preconditioning in vitro or in vivo with a stressful but non-lethal stimulus leads to new protein expression that mediates a profound neuroprotection against glutamate excitotoxicity and experimental stroke. The proteins that mediate neuroprotection are relatively unknown and under discovery.
Jianmin Zhang, Jia Yang, Huai-Shang Wang, O. Sherbini, Matthew J. Keuss, George K. Umanah, E. L. Pai, Zhikai Chi, Kaisa M. A. Paldanius, Wei He, Hong Wang, Shaida A. Andrabi, T. Dawson, V. Dawson   +13 more
semanticscholar   +3 more sources

The AAA+ ATPase RavA and its binding partner ViaA modulate E. coli aminoglycoside sensitivity through interaction with the inner membrane

Nature Communications, 2022
Membrane lipid composition is a key factor for bacterial stress adaptation. Here, authors show that ViaA and AAA+ ATPase RavA, alter lipid composition and modulate E. coli aminoglycoside sensitivity.
Jan Felix, Ladislav Bumba, Clarissa Liesche, Angélique Fraudeau, Fabrice Rébeillé, Jessica Y. El Khoury, Karine Huard, Benoit Gallet, Christine Moriscot, Jean-Philippe Kleman, Yoan Duhoo, Matthew Jessop, Eaazhisai Kandiah, Frédéric Barras, Juliette Jouhet, Irina Gutsche   +15 more
doaj   +1 more source

Microtubule-severing enzymes: From cellular functions to molecular mechanism. [PDF]

, 2018
Microtubule-severing enzymes generate internal breaks in microtubules. They are conserved in eukaryotes from ciliates to mammals, and their function is important in diverse cellular processes ranging from cilia biogenesis to cell division, phototropism ...
Ahmad, Akhmanova, Akhmanova, Allison, Antonina Roll-Mecak, Aubin-Tam, Banks, Barton, Benz, Bichet, Burk, Burk, Carlier, Carlier, Carlier, Charafeddine, Cheung, Chi, Connell, Denton, DeSantis, DesMarais, Dominguez, Dong, Doyle, Dymek, Dymek, Díaz-Valencia, Eckert, Evans, Francis J. McNally, Ganem, Gates, Grode, Guizetti, Han, Hara, Hartman, Hartman, Hawkins, Hazan, Hu, Hu, Iwaya, Jiang, Jiang, Jiang, Johjima, Joly, Kasher, Keating, Lacroix, Lata, Lee, Leo, Lindeboom, Liu, Loughlin, Lundin, Lučič, Maillard, Mains, Mao, Matsuo, McNally, McNally, McNally, McNally, McNally, McNally, Minoura, Mishra-Gorur, Mitchison, Monroe, Moretti, Mukherjee, Murata, Nakamura, Nicklas, Nithianantham, Olivares, Park, Peng, Portis, Puchades, Qiang, Rao, Reid, Rezabkova, Ribbeck, Rogers, Roll-Mecak, Roll-Mecak, Roll-Mecak, Roll-Mecak, Sharma, Sharp, Shaw, Sherwood, Sonbuchner, Srayko, Stamatakis, Stewart, Stone, Tao, Taylor, Ti, Tirnauer, Tran, Trotta, Vale, Valenstein, Vemu, Vemu, Vietri, Walker, Wang, Waterman-Storer, Wen, White, Whitehead, Wightman, Yang, Yang, Yang, Yu, Zehr, Zhang, Zhang, Zhang, Zhao   +130 more
core   +2 more sources

Bacterial Enhancer Binding Proteins—AAA⁺ Proteins in Transcription Activation

Biomolecules, 2020
Bacterial enhancer-binding proteins (bEBPs) are specialised transcriptional activators. bEBPs are hexameric AAA+ ATPases and use ATPase activities to remodel RNA polymerase (RNAP) complexes that contain the major variant sigma factor, σ54 to convert
Forson Gao, Amy E. Danson, Fuzhou Ye, Milija Jovanovic, Martin Buck, Xiaodong Zhang   +5 more
doaj   +1 more source

Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation. [PDF]

, 2019
The 26S proteasome is essential for proteostasis and the regulation of vital processes through ATP-dependent degradation of ubiquitinated substrates. To accomplish the multi-step degradation process, the proteasomes regulatory particle, consisting of lid
Aufderheide, Bard, Bard, Bard, Bashore, Beckwith, Dambacher, de la Peña, Ding, Dong, Eisele, Elsasser, Finley, Glickman, Glickman, Goldstein, Groll, Hershko, Kachroo, Lander, Lasker, Longtine, Matyskiela, Myers, Nemec, Peth, Prakash, Rubin, Smith, Sone, Tomko, Unverdorben, Verma, VerPlank, VerPlank, Wehmer, Wendler, Wenzel, Worden, Worden, Yao, Zhu, Śledź   +42 more
core   +1 more source

Cdc6 ATPase activity disengages Cdc6 from the pre-replicative complex to promote DNA replication [PDF]

, 2015
© 2015, Chang et al.To initiate DNA replication, cells first load an MCM helicase double hexamer at origins in a reaction requiring ORC, Cdc6, and Cdt1, also called pre-replicative complex (pre-RC) assembly.
Speck, C
core   +1 more source

Structure and function of the AAA+ ATPase p97/Cdc48p. [PDF]

Gene, 2016
p97 (also known as valosin-containing protein (VCP) in mammals or Cdc48p in Saccharomyces cerevisiae) is an evolutionarily conserved ATPase present in all eukaryotes and archaebacteria. In conjunction with a collection of cofactors and adaptors, p97/Cdc48p performs an array of biological functions mostly through modulating the stability of 'client ...
D. Xia, W. Tang, Y. Ye
semanticscholar   +3 more sources

AAA+ ATPases: structural insertions under the magnifying glass

Current 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, Felix, Jan, Gutsche, Irina   +2 more
openaire   +4 more sources

The AAA+ ATPase/ubiquitin ligase mysterin stabilizes cytoplasmic lipid droplets

Journal of Cell Biology, 2019
Mysterin, also known as RNF213, is an intracellular protein that forms large toroidal oligomers. Mysterin was originally identified in genetic studies of moyamoya disease (MMD), a rare cerebrovascular disorder of unknown etiology. While mysterin is known
Munechika Sugihara, Daisuke Morito, Shiori Ainuki, Y. Hirano, Kazutoyo Ogino, Akira Kitamura, Hiromi Hirata, K. Nagata   +7 more
semanticscholar   +1 more source