-
Je něco špatně v tomto záznamu ?
The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases
V. Obsilova, T. Obsil
Jazyk angličtina Země Švýcarsko
Typ dokumentu časopisecké články, přehledy
Grantová podpora
20-00058S and 19-00121S
Grantová Agentura České Republiky
RVO:67985823 of the Institute of Physiology
Czech Academy of Sciences
NLK
Free Medical Journals
od 2000
Freely Accessible Science Journals
od 2000
PubMed Central
od 2007
Europe PubMed Central
od 2007
ProQuest Central
od 2000-03-01
Open Access Digital Library
od 2000-01-01
Open Access Digital Library
od 2007-01-01
Health & Medicine (ProQuest)
od 2000-03-01
ROAD: Directory of Open Access Scholarly Resources
od 2000
PubMed
33233473
DOI
10.3390/ijms21228824
Knihovny.cz E-zdroje
- MeSH
- alosterická regulace genetika MeSH
- apoptóza genetika MeSH
- fosforylace genetika MeSH
- lidé MeSH
- mitogenem aktivované proteinkinasy p38 genetika MeSH
- proteinkinasy genetika MeSH
- proteiny 14-3-3 genetika MeSH
- signální transdukce genetika MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- přehledy MeSH
Phosphorylation by kinases governs many key cellular and extracellular processes, such as transcription, cell cycle progression, differentiation, secretion and apoptosis. Unsurprisingly, tight and precise kinase regulation is a prerequisite for normal cell functioning, whereas kinase dysregulation often leads to disease. Moreover, the functions of many kinases are regulated through protein-protein interactions, which in turn are mediated by phosphorylated motifs and often involve associations with the scaffolding and chaperon protein 14-3-3. Therefore, the aim of this review article is to provide an overview of the state of the art on 14-3-3-mediated kinase regulation, focusing on the most recent mechanistic insights into these important protein-protein interactions and discussing in detail both their structural aspects and functional consequences.
Citace poskytuje Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc21011852
- 003
- CZ-PrNML
- 005
- 20210713154417.0
- 007
- ta
- 008
- 210420s2020 sz f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.3390/ijms21228824 $2 doi
- 035 __
- $a (PubMed)33233473
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a sz
- 100 1_
- $a Obsilova, Veronika $u Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences, 25250 Vestec, Czech Republic
- 245 14
- $a The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases / $c V. Obsilova, T. Obsil
- 520 9_
- $a Phosphorylation by kinases governs many key cellular and extracellular processes, such as transcription, cell cycle progression, differentiation, secretion and apoptosis. Unsurprisingly, tight and precise kinase regulation is a prerequisite for normal cell functioning, whereas kinase dysregulation often leads to disease. Moreover, the functions of many kinases are regulated through protein-protein interactions, which in turn are mediated by phosphorylated motifs and often involve associations with the scaffolding and chaperon protein 14-3-3. Therefore, the aim of this review article is to provide an overview of the state of the art on 14-3-3-mediated kinase regulation, focusing on the most recent mechanistic insights into these important protein-protein interactions and discussing in detail both their structural aspects and functional consequences.
- 650 _2
- $a proteiny 14-3-3 $x genetika $7 D048948
- 650 _2
- $a alosterická regulace $x genetika $7 D000494
- 650 _2
- $a apoptóza $x genetika $7 D017209
- 650 _2
- $a lidé $7 D006801
- 650 _2
- $a fosforylace $x genetika $7 D010766
- 650 _2
- $a proteinkinasy $x genetika $7 D011494
- 650 _2
- $a signální transdukce $x genetika $7 D015398
- 650 _2
- $a mitogenem aktivované proteinkinasy p38 $x genetika $7 D048051
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a přehledy $7 D016454
- 700 1_
- $a Obsil, Tomas $u Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences, 25250 Vestec, Czech Republic ; Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, 12843 Prague, Czech Republic
- 773 0_
- $w MED00176142 $t International journal of molecular sciences $x 1422-0067 $g Roč. 21, č. 22 (2020)
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/33233473 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y p $z 0
- 990 __
- $a 20210420 $b ABA008
- 991 __
- $a 20210713154414 $b ABA008
- 999 __
- $a ok $b bmc $g 1650276 $s 1132231
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2020 $b 21 $c 22 $e 20201121 $i 1422-0067 $m International journal of molecular sciences $n Int J Mol Sci $x MED00176142
- GRA __
- $a 20-00058S and 19-00121S $p Grantová Agentura České Republiky
- GRA __
- $a RVO:67985823 of the Institute of Physiology $p Czech Academy of Sciences
- LZP __
- $a Pubmed-20210420