On the public citation graph

Global analysis of specificity determinants in eukaryotic protein kinases

https://doi.org/10.1101/195115

0 signed · 67 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.

Claim with ORCID

Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.

See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/jcc.20289openalex-snapshot

Scalable molecular dynamics with NAMD

inferredcites →https://doi.org/10.1002/jcc.20945openalex-snapshot

CHARMM‐GUI: A web‐based graphical user interface for CHARMM

inferredcites →https://doi.org/10.1007/3-540-28397-8_36openalex-snapshot

klaR Analyzing German Business Cycles

inferredcites →https://doi.org/10.1007/978-1-60761-232-2_6openalex-snapshot

Human Protein Reference Database and Human Proteinpedia as Discovery Tools for Systems Biology

inferredcites →https://doi.org/10.1016/0076-6879(91)00127-iopenalex-snapshot

[3] Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations

inferredcites →https://doi.org/10.1016/j.cell.2015.08.056openalex-snapshot

Kinome-wide Decoding of Network-Attacking Mutations Rewiring Cancer Signaling

inferredcites →https://doi.org/10.1016/j.cell.2015.08.057openalex-snapshot

Unmasking Determinants of Specificity in the Human Kinome

inferredcites →https://doi.org/10.1016/j.celrep.2013.03.027openalex-snapshot

The Protein Interaction Landscape of the Human CMGC Kinase Group

inferredcites →https://doi.org/10.1016/j.gde.2010.10.012openalex-snapshot

Protein kinase signaling networks in cancer

inferredcites →https://doi.org/10.1016/j.sbi.2017.12.008openalex-snapshot

Evolution, dynamics and dysregulation of kinase signalling

inferredcites →https://doi.org/10.1016/j.tibs.2018.02.009openalex-snapshot

Homing in: Mechanisms of Substrate Targeting by Protein Kinases

inferredcites →https://doi.org/10.1016/s0167-4889(96)00083-3openalex-snapshot

How do protein kinases recognize their substrates?

inferredcites →https://doi.org/10.1016/s0960-9822(99)80205-xopenalex-snapshot

Protein modification: Docking sites for kinases

inferredcites →https://doi.org/10.1021/acschembio.7b00089openalex-snapshot

Rational Redesign of a Functional Protein Kinase-Substrate Interaction

inferredcites →https://doi.org/10.1021/bi00235a002openalex-snapshot

Role of acidic amino acids in peptide substrates of the .beta.-adrenergic receptor kinase and rhodopsin kinase

inferredcites →https://doi.org/10.1038/emboj.2008.8openalex-snapshot

Activation segment dimerization: a mechanism for kinase autophosphorylation of non‐consensus sites

inferredcites →https://doi.org/10.1038/nbt0307-285openalex-snapshot

A curated compendium of phosphorylation motifs

inferredcites →https://doi.org/10.1038/nmeth.3811openalex-snapshot

Plug-and-play analysis of the human phosphoproteome by targeted high-resolution mass spectrometry

inferredcites →https://doi.org/10.1038/nrg2707openalex-snapshot

Kinase mutations in human disease: interpreting genotype–phenotype relationships

inferredcites →https://doi.org/10.1038/nrm2203openalex-snapshot

Mechanisms of specificity in protein phosphorylation

inferredcites →https://doi.org/10.1042/bj20021641openalex-snapshot

Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions

inferredcites →https://doi.org/10.1073/pnas.0134224100openalex-snapshot

Structural basis and prediction of substrate specificity in protein serine/threonine kinases

inferredcites →https://doi.org/10.1073/pnas.0501980102openalex-snapshot

Prediction of water and metal binding sites and their affinities by using the Fold-X force field

inferredcites →https://doi.org/10.1073/pnas.0610251104openalex-snapshot

The hallmark of AGC kinase functional divergence is its C-terminal tail, a cis-acting regulatory module

inferredcites →https://doi.org/10.1073/pnas.0737647100openalex-snapshot

Amino acids determining enzyme-substrate specificity in prokaryotic and eukaryotic protein kinases

inferredcites →https://doi.org/10.1073/pnas.0802403105openalex-snapshot

Congenital disease SNPs target lineage specific structural elements in protein kinases

inferredcites →https://doi.org/10.1074/jbc.m413159200openalex-snapshot

Exceptional Disfavor for Proline at the P+1 Position among AGC and CAMK Kinases Establishes Reciprocal Specificity between Them and the Proline-directed Kinases

inferredcites →https://doi.org/10.1074/jbc.m601327200openalex-snapshot

The Structure of G Protein-coupled Receptor Kinase (GRK)-6 Defines a Second Lineage of GRKs

inferredcites →https://doi.org/10.1093/bib/bbt092openalex-snapshot

A survey on prediction of specificity-determining sites in proteins

inferredcites →https://doi.org/10.1093/bioinformatics/14.9.755openalex-snapshot

Profile hidden Markov models.

inferredcites →https://doi.org/10.1093/bioinformatics/btp348openalex-snapshot

trimAl: a tool for automated alignment trimming in large-scale phylogenetic analyses

inferredcites →https://doi.org/10.1093/bioinformatics/btr406openalex-snapshot

APCluster: an R package for affinity propagation clustering

inferredcites →https://doi.org/10.1093/bioinformatics/btt419openalex-snapshot

Kinannote, a computer program to identify and classify members of the eukaryotic protein kinase superfamily

inferredcites →https://doi.org/10.1093/bioinformatics/btu033openalex-snapshot

RAxML version 8: a tool for phylogenetic analysis and post-analysis of large phylogenies

inferredcites →https://doi.org/10.1093/database/bat026openalex-snapshot

The PhosphoGRID Saccharomyces cerevisiae protein phosphorylation site database: version 2.0 update

inferredcites →https://doi.org/10.1093/molbev/mst010openalex-snapshot

MAFFT Multiple Sequence Alignment Software Version 7: Improvements in Performance and Usability

inferredcites →https://doi.org/10.1093/molbev/msx116openalex-snapshot

TimeTree: A Resource for Timelines, Timetrees, and Divergence Times

inferredcites →https://doi.org/10.1093/nar/27.1.362openalex-snapshot

KinMutBase, a database of human disease-causing protein kinase mutations

inferredcites →https://doi.org/10.1093/nar/28.1.369openalex-snapshot

KinMutBase, a database of human disease-causing protein kinase mutations

inferredcites →https://doi.org/10.1093/nar/gki198openalex-snapshot

MAFFT version 5: improvement in accuracy of multiple sequence alignment

inferredcites →https://doi.org/10.1093/nar/gkq1104openalex-snapshot

Phospho.ELM: a database of phosphorylation sites--update 2011

inferredcites →https://doi.org/10.1093/nar/gks498openalex-snapshot

FastML: a web server for probabilistic reconstruction of ancestral sequences

inferredcites →https://doi.org/10.1093/nar/gku1267openalex-snapshot

PhosphoSitePlus, 2014: mutations, PTMs and recalibrations

inferredcites →https://doi.org/10.1093/nar/gkv1209openalex-snapshot

Ensembl Genomes 2016: more genomes, more complexity

inferredcites →https://doi.org/10.1110/ps.04637904openalex-snapshot

Evolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2α

inferredcites →https://doi.org/10.1126/science.1075762openalex-snapshot

The Protein Kinase Complement of the Human Genome

inferredcites →https://doi.org/10.1126/science.1136800openalex-snapshot

Clustering by Passing Messages Between Data Points

inferredcites →https://doi.org/10.1126/science.1862342openalex-snapshot

Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

inferredcites →https://doi.org/10.1126/science.271.5248.470openalex-snapshot

Determining Divergence Times of the Major Kingdoms of Living Organisms with a Protein Clock

inferredcites →https://doi.org/10.1126/science.aaf2144openalex-snapshot

Evolution of protein phosphorylation across 18 fungal species

inferredcites →https://doi.org/10.1126/scisignal.1159433openalex-snapshot

Linear Motif Atlas for Phosphorylation-Dependent Signaling

inferredcites →https://doi.org/10.1126/scisignal.2000482openalex-snapshot

Deciphering Protein Kinase Specificity Through Large-Scale Analysis of Yeast Phosphorylation Site Motifs

inferredcites →https://doi.org/10.1126/scisignal.aaa6711openalex-snapshot

Identifying three-dimensional structures of autophosphorylation complexes in crystals of protein kinases

inferredcites →https://doi.org/10.1186/1471-2105-10-207openalex-snapshot

Ensemble approach to predict specificity determinants: benchmarking and validation

inferredcites →https://doi.org/10.1186/1471-2105-9-245openalex-snapshot

Predikin and PredikinDB: a computational framework for the prediction of protein kinase peptide specificity and an associated database of phosphorylation sites

inferredcites →https://doi.org/10.1371/journal.pbio.1000134openalex-snapshot

Evolution of Phosphoregulation: Comparison of Phosphorylation Patterns across Yeast Species

inferredcites →https://doi.org/10.1371/journal.pgen.1004062openalex-snapshot

Functional Divergence and Evolutionary Turnover in Mammalian Phosphoproteomes

inferredcites →https://doi.org/10.1371/journal.pone.0007485openalex-snapshot

Sequence and Structure Signatures of Cancer Mutation Hotspots in Protein Kinases

inferredcites →https://doi.org/10.1371/journal.pone.0018910openalex-snapshot

Representative Proteomes: A Stable, Scalable and Unbiased Proteome Set for Sequence Analysis and Functional Annotation

inferredcites →https://doi.org/10.1371/journal.pone.0033806openalex-snapshot

The Origin and Evolution of G Protein-Coupled Receptor Kinases

inferredcites →https://doi.org/10.32614/cran.package.cvtoolsopenalex-snapshot

cvTools: Cross-Validation Tools for Regression Models

inferredcites →https://doi.org/10.3389/fcell.2015.00026openalex-snapshot

PRKACA: the catalytic subunit of protein kinase A and adrenocortical tumors

inferredcites →https://doi.org/10.7554/elife.04126openalex-snapshot

Ancestral resurrection reveals evolutionary mechanisms of kinase plasticity

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1002/med.21774openalex-snapshot

Drug design targeting active posttranslational modification protein isoforms

inferred← citeshttps://doi.org/10.1016/j.cels.2020.04.005openalex-snapshot

Prediction of Signed Protein Kinase Regulatory Circuits

inferred← citeshttps://doi.org/10.1016/j.tibs.2019.11.005openalex-snapshot

Strategies for Engineering and Rewiring Kinase Regulation

inferred← citeshttps://doi.org/10.1371/journal.pbio.3000341openalex-snapshot

Evolution of protein kinase substrate recognition at the active site

Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.