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Mechanisms of the 14-3-3 protein function: regulation of protein function through conformational modulation
V. Obsilova, M. Kopecka, D. Kosek, M. Kacirova, S. Kylarova, L. Rezabkova, T. Obsil
Jazyk angličtina Země Česko
Typ dokumentu časopisecké články, práce podpořená grantem, přehledy
NLK
Directory of Open Access Journals
od 1991
Free Medical Journals
od 1998
ProQuest Central
od 2005-01-01
Medline Complete (EBSCOhost)
od 2006-01-01
Nursing & Allied Health Database (ProQuest)
od 2005-01-01
Health & Medicine (ProQuest)
od 2005-01-01
ROAD: Directory of Open Access Scholarly Resources
od 1998
- MeSH
- DNA-glykosylasy chemie ultrastruktura MeSH
- DNA-lyasa (apurinová nebo apyrimidinová) chemie ultrastruktura MeSH
- fosfoproteiny chemie ultrastruktura MeSH
- konformace proteinů MeSH
- lidé MeSH
- molekulární sekvence - údaje MeSH
- multienzymové komplexy chemie ultrastruktura MeSH
- oční proteiny chemie ultrastruktura MeSH
- proteiny 14-3-3 chemie ultrastruktura MeSH
- proteiny RGS chemie ultrastruktura MeSH
- proteiny vázající GTP - regulátory chemie ultrastruktura MeSH
- Schizosaccharomyces pombe - proteiny chemie ultrastruktura MeSH
- sekvence aminokyselin MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- vztahy mezi strukturou a aktivitou MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH
Many aspects of protein function regulation require specific protein-protein interactions to carry out the exact biochemical and cellular functions. The highly conserved members of the 14-3-3 protein family mediate such interactions and through binding to hundreds of other proteins provide multitude of regulatory functions, thus playing key roles in many cellular processes. The 14-3-3 protein binding can affect the function of the target protein in many ways including the modulation of its enzyme activity, its subcellular localization, its structure and stability, or its molecular interactions. In this minireview, we focus on mechanisms of the 14-3-3 protein-dependent regulation of three important 14-3-3 binding partners: yeast neutral trehalase Nth1, regulator of G-protein signaling 3 (RGS3), and phosducin.
Citace poskytuje Crossref.org
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