Articles with "hsp104" as a keyword



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Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.

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Published in 2017 at "Biochemistry"

DOI: 10.1021/acs.biochem.7b00225

Abstract: Recent Hsp104 structural studies have reported both planar and helical models of the hexameric structure. The conformation of Hsp104 monomers within the hexamer is affected by nucleotide ligation. After nucleotide-driven hexamer formation, Hsp104-catalyzed disruption of… read more here.

Keywords: nucleotide bound; polypeptide binding; binding nucleotide; hsp104 ... See more keywords
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Probing the drivers of Staphylococcus aureus biofilm protein amyloidogenesis and disrupting biofilms with engineered protein disaggregases

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Published in 2023 at "mBio"

DOI: 10.1128/mbio.00587-23

Abstract: ABSTRACT Phenol-soluble modulins (PSMs) are the primary proteinaceous component of Staphylococcus aureus biofilms. Residence in the protective environment of biofilms allows bacteria to rapidly evolve and acquire antimicrobial resistance, which can lead to persistent infections… read more here.

Keywords: psm peptides; system; aureus biofilms; staphylococcus aureus ... See more keywords
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Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions

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Published in 2017 at "Frontiers in Molecular Biosciences"

DOI: 10.3389/fmolb.2017.00054

Abstract: Cellular proteostasis involves not only the expression of proteins in response to environmental needs, but also the timely repair or removal of damaged or unneeded proteins. AAA+ motor proteins are critically involved in these pathways.… read more here.

Keywords: function aaa; clpb hsp104; clpa clpb; hsp104 ... See more keywords
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The yeast molecular chaperone, Hsp104, influences transthyretin aggregate formation

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Published in 2022 at "Frontiers in Molecular Neuroscience"

DOI: 10.3389/fnmol.2022.1050472

Abstract: Patients with the fatal disorder Transthyretin Amyloidosis (ATTR) experience polyneuropathy through the progressive destruction of peripheral nervous tissue. In these patients, the transthyretin (TTR) protein dissociates from its functional tetrameric structure, misfolds, and aggregates into… read more here.

Keywords: yeast molecular; aggregate populations; chaperone; molecular chaperone ... See more keywords