Skip to search formSkip to main contentSkip to account menu

phosphoserine binding

Interacting selectively and non-covalently with a phosphorylated serine residue within a protein. [GOC:ai]
National Institutes of Health

Related topics

Related topics

1 relation

Broader (1)

phosphoserine/phosphothreonine binding

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2019
2019
Characterization of SMG7 14-3-3-like domain reveals phosphoserine binding-independent regulation of p53 and UPF1
The 14-3-3-related protein SMG7 plays critical roles in regulation of DNA damage response and nonsense-mediated mRNA decay (NMD… 
Highly Cited
2014
Highly Cited
2014
Phospho-dependent and phospho-independent interactions of the helicase UPF1 with the NMD factors SMG5–SMG7 and SMG6
Nonsense-mediated mRNA decay (NMD) is a eukaryotic surveillance pathway that recognizes mRNAs with premature stop codons and… 
2013
2013
Akt Switches TopBP1 Function from Checkpoint Activation to Transcriptional Regulation through Phosphoserine Binding-Mediated Oligomerization
ABSTRACT Our previous study showed that Akt phosphorylates TopBP1 at the Ser-1159 residue and induces its oligomerization… 
2005
2005
The shear stress of keeping arteries clear
  • D. Harrison
  • Nature Network Boston
  • 2005
  • Corpus ID: 10228592
The force exerted by blood as it flows through the vessels influences the development of atherosclerosis. An understanding of how… 
Highly Cited
2002
Highly Cited
2002
Critical Role of WW Domain Phosphorylation in Regulating Phosphoserine Binding Activity and Pin1 Function*
Phosphoserine-binding modules help determine the specificity of signal transduction events. One such module, the group IV WW… 
Highly Cited
2002
Highly Cited
2002
Drosophila 14-3-3/PAR-5 is an essential mediator of PAR-1 function in axis formation.
Highly Cited
2002
Highly Cited
2002
Identification of 14-3-3ζ as a Protein Kinase B/Akt Substrate*
Protein kinase B/Akt (PKB/Akt) is a member of the ACG kinase family, which also includes protein kinase C, that phosphorylates a… 
Highly Cited
2001
Highly Cited
2001
Structural basis of Smad1 activation by receptor kinase phosphorylation.
Highly Cited
2001
Highly Cited
2001
14-3-3 inhibits Bad-induced cell death through interaction with serine-136.
14-3-3 proteins are a family of multifunctional phosphoserine binding molecules that can serve as effectors of survival signaling… 
Highly Cited
1996
Highly Cited
1996
Phosphorylation of CREB at Ser-133 induces complex formation with CREB-binding protein via a direct mechanism
We have characterized a phosphoserine binding domain in the coactivator CREB-binding protein (CBP) which interacts with the… 
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy (opens in a new tab), Terms of Service (opens in a new tab), and Dataset License (opens in a new tab)