Articles with "chaperonin" as a keyword



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An inventory of interactors of the human HSP60/HSP10 chaperonin in the mitochondrial matrix space

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Published in 2020 at "Cell Stress and Chaperones"

DOI: 10.1007/s12192-020-01080-6

Abstract: The HSP60/HSP10 chaperonin assists folding of proteins in the mitochondrial matrix space by enclosing them in its central cavity. The chaperonin forms part of the mitochondrial protein quality control system. It is essential for cellular… read more here.

Keywords: hsp10 chaperonin; hsp60 hsp10; chaperonin; mitochondrial matrix ... See more keywords
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Cryo-EM Structure of the Novel Viral Chaperonin, Encoded by Gene 228 of Bacteriophage AR9 Bacillus subtilis

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Published in 2020 at "Microscopy and Microanalysis"

DOI: 10.1017/s1431927620017584

Abstract: Chaperonins are some of the most studied families of chaperones. They are multimeric complexes that ensure the proper folding of newly synthesized polypeptide chains and prevent the aggregation of denatured stressed proteins in an ATP-dependent… read more here.

Keywords: structure novel; novel viral; cryo structure; bacteriophage ... See more keywords
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The chaperonin CCT8 controls proteostasis essential for T cell maturation, selection, and function

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Published in 2021 at "Communications Biology"

DOI: 10.1038/s42003-021-02203-0

Abstract: T cells rely for their development and function on the correct folding and turnover of proteins generated in response to a broad range of molecular cues. In the absence of the eukaryotic type II chaperonin… read more here.

Keywords: cct8; biology; chaperonin; maturation selection ... See more keywords
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The substrate specificity of eukaryotic cytosolic chaperonin CCT

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Published in 2018 at "Philosophical Transactions of the Royal Society B: Biological Sciences"

DOI: 10.1098/rstb.2017.0192

Abstract: The cytosolic chaperonin CCT (chaperonin containing TCP-1) is an ATP-dependent double-ring protein machine mediating the folding of members of the eukaryotic cytoskeletal protein families. The actins and tubulins are obligate substrates of CCT because they… read more here.

Keywords: specificity eukaryotic; cytosolic chaperonin; chaperonin; cct ... See more keywords
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Human Papillomavirus Infection Requires the CCT Chaperonin Complex

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Published in 2021 at "Journal of Virology"

DOI: 10.1128/jvi.01943-20

Abstract: Several of the mechanisms that function during the infection of target cells by HPV particles have been previously described. However, many aspects of this process remain unknown. ABSTRACT Human papillomavirus (HPV) infection is a multistep… read more here.

Keywords: infection; human papillomavirus; hpv; cct chaperonin ... See more keywords

Crystal structures of dimeric and heptameric mtHsp60 reveal the mechanism of chaperonin inactivation

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Published in 2023 at "Life Science Alliance"

DOI: 10.26508/lsa.202201753

Abstract: The crystal structure of the dimeric mtHsp60 from grouper fish has been determined, revealing a symmetrical subunit interaction with an exchanged α-helix connecting the two subunits. This structure provides new insights into the conformational changes… read more here.

Keywords: mthsp60; structure; chaperonin; crystal structures ... See more keywords
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Structural and Dynamic Disturbances Revealed by Molecular Dynamics Simulations Predict the Impact on Function of CCT5 Chaperonin Mutations Associated with Rare Severe Distal Neuropathies

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Published in 2023 at "International Journal of Molecular Sciences"

DOI: 10.3390/ijms24032018

Abstract: Mutations in genes encoding molecular chaperones, for instance the genes encoding the subunits of the chaperonin CCT (chaperonin containing TCP-1, also known as TRiC), are associated with rare neurodegenerative disorders. Using a classical molecular dynamics… read more here.

Keywords: chaperonin; associated rare; molecular dynamics; cct5 ... See more keywords

In Vivo Incorporation of Photoproteins into GroEL Chaperonin Retaining Major Structural and Functional Properties

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Published in 2023 at "Molecules"

DOI: 10.3390/molecules28041901

Abstract: The incorporation of photoproteins into proteins of interest allows the study of either their localization or intermolecular interactions in the cell. Here we demonstrate the possibility of in vivo incorporating the photoprotein Aequorea victoria enhanced… read more here.

Keywords: photoproteins groel; chaperonin; incorporation photoproteins; vivo incorporation ... See more keywords