Results 11 to 20 of about 183,487 (307)

The YdiU Domain Modulates Bacterial Stress Signaling through Mn2+-Dependent UMPylation

Cell Reports, 2020
Summary: Sensing stressful conditions and adjusting the cellular metabolism to adapt to the environment are essential activities for bacteria to survive in variable situations. Here, we describe a stress-related protein, YdiU, and characterize YdiU as an
Yinlong Yang, Yingying Yue, Nannan Song, Cuiling Li, Zenglin Yuan, Yan Wang, Yue Ma, Hui Li, Fengyu Zhang, Weiwei Wang, Haihong Jia, Peng Li, Xiaobing Li, Qi Wang, Zhe Ding, Hongjie Dong, Lichuan Gu, Bingqing Li   +17 more
doaj   +1 more source

Chaperone discovery [PDF]

BioEssays, 2012
AbstractMolecular chaperones assist de novo protein folding and facilitate the refolding of stress‐denatured proteins. The molecular chaperone concept was coined nearly 35 years ago, and since then, tremendous strides have been made in understanding how these factors support protein folding.
Quan, Shu, Bardwell, James C. A.
openaire   +3 more sources

Identification and in silico expression pattern analysis of Eucalyptus expressed sequencing tags (ESTs) encoding molecular chaperones

Genetics and Molecular Biology, 2005
Expressed Sequence Tags (ESTs) sequencing provides reliable and useful information concerning gene expression patterns in the genomic context. Our group used bioinformatics to identify and annotate 5'EST-contigs belonging to the molecular chaperones ...
Thiago C. Cagliari, Ana O. Tiroli, Júlio C. Borges, Carlos H.I. Ramos   +3 more
doaj   +1 more source

Stoichiometric Analysis of Shifting in Subcellular Compartmentalization of HSP70 within Ischemic Penumbra

Molecules, 2021
The heat shock protein (HSP) 70 is considered the main hallmark in preclinical studies to stain the peri-infarct region defined area penumbra in preclinical models of brain ischemia.
Federica Mastroiacovo, Francesca Biagioni, Paola Lenzi, Larisa Ryskalin, Stefano Puglisi-Allegra, Ferdinando Nicoletti, Alessandro Frati, Francesco Fornai   +7 more
doaj   +1 more source

The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution [PDF]

, 2013
NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a ...
Andrew Bowman, Andrew Stirling, Andrews, Berndsen, Bonangelino, Bowman, Colin M. Hammond, Das, David A. Robinson, David G. Norman, Del Rosario, Dmitri I. Svergun, Driscoll, D’Arcy, D’Arcy, Fillingham, Fleissner, Hagelueken, Hansen, Hassane El-Mkami, Ishimi, Jeschke, Kolonko, Konarev, Krogan, Kuryan, Laskey, McBryant, McBryant, Milov, Newman, Noda, Ohkuni, Park, Park, Petoukhov, Pramila, Ransom, Richard Ward, Roessle, Schwieters, Selth, Selth, Su, Svergun, Svergun, Tang, Tang, Tom Owen-Hughes, Toth, Tsubota, Ward, Weifeng Shang, Xue   +53 more
core   +8 more sources

The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins

Biomolecules, 2021
Protein homeostasis is an essential component of proper cellular function; however, sustaining protein health is a challenging task, especially during the aerobic lifestyle.
Meytal Radzinski, Tal Oppenheim, Norman Metanis, Dana Reichmann   +3 more
doaj   +1 more source

Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor. [PDF]

, 2019
Molecular chaperones such as Hsp40 and Hsp70 hold the androgen receptor (AR) in an inactive conformation. They are released in the presence of androgens, enabling transactivation and causing the receptor to become aggregation-prone.
Banduseela, Varuna C, Brun-Heath, Isabelle, Chiesa, Giulio, Di Sanza, Claudio, Eftekharzadeh, Bahareh, Felli, Isabella C, García, Jesús, Gestwicki, Jason E, Giorgetti, Elisa, Lieberman, Andrew P, Marin-Argany, Marta, Martínez-Cristóbal, Paula, Nath, Samir R, Nebreda, Ángel R, Pierattelli, Roberta, Rauch, Jennifer N, Salvatella, Xavier, Schwarz, Daniel MC, Shao, Hao, Yu, Zhigang   +19 more
core   +2 more sources

Molecular chaperone genes in the sugarcane expressed sequence database (SUCEST)

Genetics and Molecular Biology, 2001
Some newly synthesized proteins require the assistance of molecular chaperones for their correct folding. Chaperones are also involved in the dissolution of protein aggregates making their study significant for both biotechnology and medicine and the ...
Júlio C. Borges, Maria C. Peroto, Carlos H.I. Ramos   +2 more
doaj   +1 more source

Mitochondrial molecular chaperones [PDF]

, 1994
After synthesis in the cytosol, most mitochondrial proteins must traverse mitochondrial membranes to reach their functional location. During this process, proteins become unfolded and then refold to attain their native conformation after crossing the ...
Atencio, Caplan, Caplan, Cheng, Craig, Cyr, Deshales, Eilers, Gambill, Glick, Glick, Hartl, Hartl, Hwang, Johnson, Kang, Kiebler, Langer, Liberek, Manning-Krieg, Neupert, Ostermann, Palleros, Rassow, Rospert, Sanders, Scherer, Schleyer, Schröder, Simon, Vestweber, Voos, Xia   +32 more
core   +1 more source

HSP70 and their co-chaperones in the human malaria parasite P. falciparum and their potential as drug targets

Frontiers in Molecular Biosciences, 2022
As part of their life-cycle, malaria parasites undergo rapid cell multiplication and division, with one parasite giving rise to over 20 new parasites within the course of 48 h.
Julian Barth, Tim Schach, Jude M. Przyborski   +2 more
doaj   +1 more source