Results 11 to 20 of about 110,947 (209)
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
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Hsp70 and Hsp110 Chaperones Promote Early Steps of Proteasome Assembly [PDF]
Biomolecules, 2022 Whereas assembly of the 20S proteasome core particle (CP) in prokaryotes apparently occurs spontaneously, the efficiency of this process in eukaryotes relies on the dedicated assembly chaperones Ump1, Pba1-Pba2, and Pba3-Pba4.
Ana C. Matias +3 more
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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
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Molecular chaperones and selection against mutations [PDF]
Biology Direct, 2008 Background Molecular chaperones help to restore the native states of proteins after their destabilization by external stress. It has been proposed that another function of chaperones is to maintain the activity of proteins destabilized by mutation ...
Korona Ryszard, Tomala Katarzyna
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QRB Discovery, 2021 Abstract Chaperones protect other proteins against misfolding and aggregation, a key requirement for maintaining biological function. Experimental observations of changes in solubility of amyloid proteins in the presence of certain chaperones are discussed here in terms of thermodynamic driving forces.
Sara Linse +2 more
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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.
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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 ...
El-Mkami, H. +31 more
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Differential regulation of circulating levels of molecular chaperones in patients undergoing treatment for periodontal disease. [PDF]
, 2007 Evidence is emerging that molecular chaperones, in addition to their intracellular protein folding actions, can act as intercellular signaling proteins with an ability to modulate leukocyte function. Recent evidence has also shown that these proteins can
Alireza Shamaei-Tousi +24 more
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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
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The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation [PDF]
, 2011 Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant ...
Bowman, Andrew +16 more
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