A critical evaluation of protein kinase regulation by activation loop autophosphorylation
R Reinhardt, TA Leonard - Elife, 2023 - elifesciences.org
Phosphorylation of proteins is a ubiquitous mechanism of regulating their function,
localization, or activity. Protein kinases, enzymes that use ATP to phosphorylate protein …
localization, or activity. Protein kinases, enzymes that use ATP to phosphorylate protein …
How do protein kinases take a selfie (autophosphorylate)?
J Beenstock, N Mooshayef, D Engelberg - Trends in biochemical sciences, 2016 - cell.com
Eukaryotic protein kinases (EPKs) control most biological processes and play central roles
in many human diseases. To become catalytically active, EPKs undergo conversion from an …
in many human diseases. To become catalytically active, EPKs undergo conversion from an …
A structurally-validated multiple sequence alignment of 497 human protein kinase domains
V Modi, RL Dunbrack Jr - Scientific reports, 2019 - nature.com
Studies on the structures and functions of individual kinases have been used to understand
the biological properties of other kinases that do not yet have experimental structures. The …
the biological properties of other kinases that do not yet have experimental structures. The …
The Src module: an ancient scaffold in the evolution of cytoplasmic tyrosine kinases
Tyrosine kinases were first discovered as the protein products of viral oncogenes. We now
know that this large family of metazoan enzymes includes nearly one hundred structurally …
know that this large family of metazoan enzymes includes nearly one hundred structurally …
Clinically precedented protein kinases: Rationale for their use in neurodegenerative disease
CL Benn, LA Dawson - Frontiers in Aging Neuroscience, 2020 - frontiersin.org
Kinases are an intensively studied drug target class in current pharmacological research as
evidenced by the large number of kinase inhibitors being assessed in clinical trials. Kinase …
evidenced by the large number of kinase inhibitors being assessed in clinical trials. Kinase …
An electrostatic selection mechanism controls sequential kinase signaling downstream of the T cell receptor
The sequence of events that initiates T cell signaling is dictated by the specificities and order
of activation of the tyrosine kinases that signal downstream of the T cell receptor. Using a …
of activation of the tyrosine kinases that signal downstream of the T cell receptor. Using a …
Ligand bias in receptor tyrosine kinase signaling
Ligand bias is the ability of ligands to differentially activate certain receptor signaling
responses compared with others. It reflects differences in the responses of a receptor to …
responses compared with others. It reflects differences in the responses of a receptor to …
[HTML][HTML] AlphaFold2 models of the active form of all 437 catalytically competent human protein kinase domains
B Faezov, RL Dunbrack Jr - bioRxiv, 2023 - ncbi.nlm.nih.gov
Humans have 437 catalytically competent protein kinase domains with the typical kinase
fold, similar to the structure of Protein Kinase A (PKA). Only 155 of these kinases are in the …
fold, similar to the structure of Protein Kinase A (PKA). Only 155 of these kinases are in the …
ProtCID: a data resource for structural information on protein interactions
Q Xu, RL Dunbrack Jr - Nature communications, 2020 - nature.com
Structural information on the interactions of proteins with other molecules is plentiful, and for
some proteins and protein families, there may be 100s of available structures. It can be very …
some proteins and protein families, there may be 100s of available structures. It can be very …
Sequence and structure-based analysis of specificity determinants in eukaryotic protein kinases
Protein kinases lie at the heart of cell-signaling processes and are often mutated in disease.
Kinase target recognition at the active site is in part determined by a few amino acids around …
Kinase target recognition at the active site is in part determined by a few amino acids around …