Articles with "chaperone" as a keyword



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Cell‐Penetrating Chaperone Peptide Prevents Protein Aggregation and Protects against Cell Apoptosis

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Published in 2018 at "Advanced Biosystems"

DOI: 10.1002/adbi.201700095

Abstract: Many of the newly discovered therapeutic peptides and molecules are limited by their inability to cross the cell membrane. In the present study, a cell‐penetrating peptide (CPP), VPTLK, derived from Ku70 protein, is employed to… read more here.

Keywords: peptide; cell; cell penetrating; protein aggregation ... See more keywords
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Phenylalanine hydroxylase variants interact with the co‐chaperone DNAJC12

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Published in 2019 at "Human Mutation"

DOI: 10.1002/humu.23712

Abstract: DNAJC12, a type III member of the HSP40/DNAJ family, has been identified as the specific co‐chaperone of phenylalanine hydroxylase (PAH) and the other aromatic amino acid hydroxylases. DNAJ proteins work together with molecular chaperones of… read more here.

Keywords: pah; dnajc12; chaperone; phenylalanine hydroxylase ... See more keywords
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The co‐chaperone BAG3: Orchestrator of the cellular task force in response to stress

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Published in 2022 at "Journal of Cellular Biochemistry"

DOI: 10.1002/jcb.30212

Abstract: We and other research teams have been conducting studies on BAG3 protein for several years. BAG3 was first described as a co‐chaperone of HSP70 in 1999 (by Takayama et al. DOI: 10.1074/jbc.274.2.781) and its interactions… read more here.

Keywords: cancer; bag3; 1002 jcb; cell ... See more keywords
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Structural and biochemical insights into FKBP51 as a Hsp90 co-chaperone.

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Published in 2023 at "Journal of cellular biochemistry"

DOI: 10.1002/jcb.30384

Abstract: The FK506-binding protein 51 (FKBP51) is a high-molecular-weight immunophilin that emerged as an important drug target for stress-related disorders, chronic pain, and obesity. It has been implicated in a plethora of molecular pathways but remains… read more here.

Keywords: fkbp51 hsp90; insights fkbp51; biochemical insights; chaperone ... See more keywords
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Strong increase of leukocyte apha‐galactosidase A activity in two male patients with Fabry disease following oral chaperone therapy

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Published in 2019 at "Molecular Genetics & Genomic Medicine"

DOI: 10.1002/mgg3.894

Abstract: Fabry disease (OMIM 301500) is an X‐linked disorder caused by alpha‐galactosidase A (α‐Gal A) deficiency. The administration of a pharmacologic chaperone (migalastat) in Fabry patients with amenable mutations has been reported to improve or stabilize… read more here.

Keywords: fabry disease; increase; galactosidase; chaperone ... See more keywords
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Plasticity and transient binding are key ingredients of the periplasmic chaperone network

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Published in 2019 at "Protein Science"

DOI: 10.1002/pro.3641

Abstract: SurA, Skp, FkpA, and DegP constitute a chaperone network that ensures biogenesis of outer membrane proteins (OMPs) in Gram‐negative bacteria. Both Skp and FkpA are holdases that prevent the self‐aggregation of unfolded OMPs, whereas SurA… read more here.

Keywords: network; skp fkpa; chaperone network; plasticity transient ... See more keywords
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Structural and functional analysis of the Hsp70/Hsp40 chaperone system

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Published in 2019 at "Protein Science"

DOI: 10.1002/pro.3725

Abstract: As one of the most abundant and highly conserved molecular chaperones, the 70‐kDa heat shock proteins (Hsp70s) play a key role in maintaining cellular protein homeostasis (proteostasis), one of the most fundamental tasks for every… read more here.

Keywords: chaperone system; structural functional; chaperone; functional analysis ... See more keywords
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Calnexin/Calreticulin and Assays Related to N-Glycoprotein Folding In Vitro.

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Published in 2020 at "Methods in molecular biology"

DOI: 10.1007/978-1-0716-0430-4_29

Abstract: Calnexin (CNX) and calreticulin (CRT) are ER-resident lectin-like molecular chaperones involved in the quality control of secretory or membrane glycoproteins. They can exert molecular chaperone functions via specific binding to the early processing intermediates of… read more here.

Keywords: calnexin calreticulin; calnexin; calreticulin; cnx crt ... See more keywords
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Optimizing Chaperone Removal Strategy from Overexpressed Recombinant Proteins : GNE, a Case Study.

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Published in 2022 at "Methods in molecular biology"

DOI: 10.1007/978-1-0716-1859-2_20

Abstract: In the last two decades, numerous innovative advances, strategies and protocols have been developed and optimized to improve the quality and quantity of soluble recombinant protein production in E. coli. One of the major challenges… read more here.

Keywords: chaperone; removal; protein; chaperone removal ... See more keywords
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Measurement of Chaperone-Mediated Effects on Polyglutamine Protein Aggregation by the Filter Trap Assay.

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Published in 2018 at "Methods in molecular biology"

DOI: 10.1007/978-1-4939-7477-1_5

Abstract: The formation of aggregates by polyglutamine-containing (polyQ) proteins in neurons is a key to the pathogenesis of several progressive neurodegenerative diseases such as Huntington's disease (HD) spinocerebellar ataxias (SCAs), and spinal and bulbar muscular atrophy… read more here.

Keywords: trap assay; filter trap; chaperone; polyq ... See more keywords
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Co-Expression of a Thermally Stable and Methanol-Resistant Lipase and Its Chaperone from Burkholderia cepacia G63 in Escherichia coli

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Published in 2020 at "Applied Biochemistry and Biotechnology"

DOI: 10.1007/s12010-020-03453-0

Abstract: Biodiesel biosynthesis with enzymatic transesterification is considered green, sustainable, and environmentally friendly method. Lipase from Burkholderia cepacia G63 has excellent catalytic properties in biodiesel production. Lipase chaperones promote secretion and folding of enzymes, thereby enhancing… read more here.

Keywords: burkholderia cepacia; cepacia g63; escherichia coli; lipase ... See more keywords