Structural insights into GrpEL1-mediated nucleotide and substrate release of human mitochondrial Hsp70
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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1 Online-Ressource.
- Language
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Englisch
- Bibliographic citation
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Structural insights into GrpEL1-mediated nucleotide and substrate release of human mitochondrial Hsp70 ; volume:15 ; number:1 ; day:30 ; month:12 ; year:2024 ; pages:1-17 ; date:12.2024
Nature Communications ; 15, Heft 1 (30.12.2024), 1-17, 12.2024
- Creator
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Morizono, Marc A.
McGuire, Kelly L.
Birouty, Natalie I.
Herzik, Mark A.
- Contributor
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SpringerLink (Online service)
- DOI
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10.1038/s41467-024-54499-1
- URN
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urn:nbn:de:101:1-2503072110543.246262170555
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:22 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Morizono, Marc A.
- McGuire, Kelly L.
- Birouty, Natalie I.
- Herzik, Mark A.
- SpringerLink (Online service)
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Multistep mechanism of substrate binding determines chaperone activity of Hsp70
A conserved R type Methionine Sulfoxide Reductase reverses oxidized GrpEL1/Mge1 to regulate Hsp70 chaperone cycle
Discovery and substrate specificity engineering of nucleotide halogenases
Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashion
Protein polarization driven by nucleoid exclusion of DnaK(HSP70)–substrate complexes
Unterlagen Grp. EWG III.- Unterlagen Grp. 4 GO 22
Absender, Grp - Gruz
Antibody–nucleotide conjugate as a substrate for DNA polymerases
Allosteric substrate release by a sialic acid TRAP transporter substrate binding protein
Varied DNA Polymerase : Substrate Interactions in the Nucleotide Binding Pocket
Chaperone network in the yeast cytosol : Hsp110 is revealed as an Hsp70 nucleotide exchange factor
Stud Grp MFüSys
Multistep mechanism of substrate binding determines chaperone activity of Hsp70
A conserved R type Methionine Sulfoxide Reductase reverses oxidized GrpEL1/Mge1 to regulate Hsp70 chaperone cycle
Discovery and substrate specificity engineering of nucleotide halogenases
Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashion
Protein polarization driven by nucleoid exclusion of DnaK(HSP70)–substrate complexes
Unterlagen Grp. EWG III.- Unterlagen Grp. 4 GO 22
Absender, Grp - Gruz
Antibody–nucleotide conjugate as a substrate for DNA polymerases
Allosteric substrate release by a sialic acid TRAP transporter substrate binding protein
Varied DNA Polymerase : Substrate Interactions in the Nucleotide Binding Pocket
Chaperone network in the yeast cytosol : Hsp110 is revealed as an Hsp70 nucleotide exchange factor