Engagement of cellular prion protein with the co-chaperone Hsp70/90 organizing protein regulates the proliferation of glioblastoma stem-like cells
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
1757-6512
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
Engagement of cellular prion protein with the co-chaperone Hsp70/90 organizing protein regulates the proliferation of glioblastoma stem-like cells ; volume:8 ; number:1 ; day:17 ; month:4 ; year:2017 ; pages:1-14 ; date:12.2017
Stem cell research & therapy ; 8, Heft 1 (17.4.2017), 1-14, 12.2017
- Klassifikation
-
Biowissenschaften, Biologie
- Urheber
-
Iglesia, Rebeca Piatniczka
- Beteiligte Personen und Organisationen
-
Prado, Mariana Brandão
Cruz, Lilian
Martins, Vilma Regina
Santos, Tiago Góss
Lopes, Marilene Hohmuth
SpringerLink (Online service)
- DOI
-
10.1186/s13287-017-0518-1
- URN
-
urn:nbn:de:1111-20170501495
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2025, 07:32 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Iglesia, Rebeca Piatniczka
- Prado, Mariana Brandão
- Cruz, Lilian
- Martins, Vilma Regina
- Santos, Tiago Góss
- Lopes, Marilene Hohmuth
- SpringerLink (Online service)
Ähnliche Objekte (12)
Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation
Prion proteins
The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
Conformational dynamics of the Hsp70 chaperone
Protecting protein homeostasis in neurodegenerative disease models by modulating the HSP70/co-chaperone network
Dual roles of HSP70 chaperone HSPA1 in quality control of nascent and newly synthesized proteins
Die Prion-Protein-Isoformen
The Absence of Prion-Like Infectivity in Mice expressing Prion Protein-Like Protein
Polarisierter Transport des Prion-Proteins
Prion protein self-peptides modulate prion interactions and conversion
Luminescence resonance energy transfer between genetically encoded donor and acceptor for protein-protein interaction studies in the molecular chaperone HSP70/HSP90 complexes
The yeast Hsp70 homolog Ssb: a chaperone for general de novo protein folding and a nanny for specific intrinsically disordered protein domains
Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation
Prion proteins
The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
Conformational dynamics of the Hsp70 chaperone
Protecting protein homeostasis in neurodegenerative disease models by modulating the HSP70/co-chaperone network
Dual roles of HSP70 chaperone HSPA1 in quality control of nascent and newly synthesized proteins
Die Prion-Protein-Isoformen
The Absence of Prion-Like Infectivity in Mice expressing Prion Protein-Like Protein
Polarisierter Transport des Prion-Proteins
Prion protein self-peptides modulate prion interactions and conversion
Luminescence resonance energy transfer between genetically encoded donor and acceptor for protein-protein interaction studies in the molecular chaperone HSP70/HSP90 complexes
The yeast Hsp70 homolog Ssb: a chaperone for general de novo protein folding and a nanny for specific intrinsically disordered protein domains
Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation
Prion proteins
The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
Conformational dynamics of the Hsp70 chaperone
Protecting protein homeostasis in neurodegenerative disease models by modulating the HSP70/co-chaperone network
Dual roles of HSP70 chaperone HSPA1 in quality control of nascent and newly synthesized proteins
Die Prion-Protein-Isoformen
The Absence of Prion-Like Infectivity in Mice expressing Prion Protein-Like Protein
Polarisierter Transport des Prion-Proteins
Prion protein self-peptides modulate prion interactions and conversion
Luminescence resonance energy transfer between genetically encoded donor and acceptor for protein-protein interaction studies in the molecular chaperone HSP70/HSP90 complexes