Results 11 to 20 of about 184,458 (283)
Cellular and Molecular Life Sciences, 2011 This review describes the properties of some rare eukaryotic chaperones that each assist in the folding of only one target protein. In particular, we describe (1) the tubulin cofactors, (2) p47, which assists in the folding of collagen, (3) α-hemoglobin stabilizing protein (AHSP), (4) the adenovirus L4-100 K protein, which is a chaperone of the major ...
Szolajska, Ewa, Chroboczek, Jadwiga
openaire +2 more sources
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 +3 more
doaj +1 more source
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 +7 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 +32 more
core +1 more source
Current Opinion in Structural Biology, 2014 The folding and assembly of myosin motor proteins is essential for most movement processes at the cellular, but also at the organism level. Importantly, myosins, which represent a very diverse family of proteins, require the activity of general and specialized folding factors to develop their full motor function.
Hellerschmied, Doris, Clausen, Tim
openaire +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 +2 more
doaj +1 more source
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 +3 more
doaj +1 more source
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 +2 more
doaj +1 more source
The Chlamydia trachomatis Type III Secretion Chaperone Slc1 Engages Multiple Early Effectors, Including TepP, a Tyrosine-phosphorylated Protein Required for the Recruitment of CrkI-II to Nascent Inclusions and Innate Immune Signaling [PDF]
, 2014 Chlamydia trachomatis, the causative agent of trachoma and sexually transmitted infections, employs a type III secretion (T3S) system to deliver effector proteins into host epithelial cells to establish a replicative vacuole.
Bastidas, Robert J. +6 more
core +3 more sources
G3: Genes, Genomes, Genetics, 2017 Accumulation of toxic proteins in neurons has been linked with the onset of neurodegenerative diseases, which in many cases are characterized by altered neuronal function and synapse loss.
Sandeep Raut +5 more
doaj +1 more source