FEBS Letters
Article . 2012 . Peer-reviewed
License: Wiley Online Library User Agreement
Data sources: Crossref
14‐3‐3 Interacts with LKB1 via recognizing phosphorylated threonine 336 residue and suppresses LKB1 kinase function
Authors: Bei Huang; Yu Bai; Haian Fu; Hanyan Sun; Tao Zhou;
pmid: 22575644
14‐3‐3 Interacts with LKB1 via recognizing phosphorylated threonine 336 residue and suppresses LKB1 kinase function
Abstract
LKB1 and 14‐3‐3 zeta colocalize by fluorescence microscopy (View interaction).
Related Organizations
- Emory University United States
- Anhui University China (People's Republic of)
Keywords
AMPK, Threonine, LKB1, AMP-Activated Protein Kinases, Protein Serine-Threonine Kinases, G1 Phase Cell Cycle Checkpoints, Kinase function, 14-3-3 Proteins, AMP-Activated Protein Kinase Kinases, Humans, Phosphorylation, 14-3-3, HeLa Cells
AMPK, Threonine, LKB1, AMP-Activated Protein Kinases, Protein Serine-Threonine Kinases, G1 Phase Cell Cycle Checkpoints, Kinase function, 14-3-3 Proteins, AMP-Activated Protein Kinase Kinases, Humans, Phosphorylation, 14-3-3, HeLa Cells
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citations
Citations provided by BIP!
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
popularity
Popularity provided by BIP!
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
15
Average
Average
Top 10%
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