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Protein Kinase−Inhibitor Database: Structural Variability of and Inhibitor Interactions with the Protein Kinase P-Loop
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/bip.20656openalex-snapshot
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inferredcites →https://doi.org/10.1002/cmdc.200700075openalex-snapshot
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inferredcites →https://doi.org/10.1002/cmdc.200700255openalex-snapshot
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inferredcites →https://doi.org/10.1002/j.1460-2075.1992.tb05493.xopenalex-snapshot
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inferredcites →https://doi.org/10.1002/pro.355openalex-snapshot
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inferredcites →https://doi.org/10.1002/prot.20026openalex-snapshot
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inferredcites →https://doi.org/10.1002/prot.340230412openalex-snapshot
Knowledge‐based protein secondary structure assignment
inferredcites →https://doi.org/10.1007/978-90-481-2339-1_4openalex-snapshot
Structural Biology Contributions to the Discovery of Drugs to Treat Chronic Myelogenous Leukemia
inferredcites →https://doi.org/10.1007/s00726-007-0015-4openalex-snapshot
Strong and weak hydrogen bonds in protein-ligand complexes of kinases: a comparative study
inferredcites →https://doi.org/10.1016/j.bbapap.2007.11.002openalex-snapshot
Conserved spatial patterns across the protein kinase family
inferredcites →https://doi.org/10.1016/j.bbapap.2009.10.013openalex-snapshot
Insights into protein kinase regulation and inhibition by large scale structural comparison
inferredcites →https://doi.org/10.1016/j.bmcl.2008.02.011openalex-snapshot
Benzothiazole based inhibitors of p38α MAP kinase
inferredcites →https://doi.org/10.1016/j.jmb.2007.01.004openalex-snapshot
A Structural Comparison of Inhibitor Binding to PKB, PKA and PKA-PKB Chimera
inferredcites →https://doi.org/10.1016/j.jmb.2009.01.033openalex-snapshot
First Inactive Conformation of CK2α, the Catalytic Subunit of Protein Kinase CK2
inferredcites →https://doi.org/10.1016/j.sbi.2006.10.006openalex-snapshot
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inferredcites →https://doi.org/10.1016/j.str.2005.11.024openalex-snapshot
Molecular Mechanism for the Regulation of Rho-Kinase by Dimerization and Its Inhibition by Fasudil
inferredcites →https://doi.org/10.1016/s0092-8674(02)00741-9openalex-snapshot
The Conformational Plasticity of Protein Kinases
inferredcites →https://doi.org/10.1016/s0896-6273(00)81200-3openalex-snapshot
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inferredcites →https://doi.org/10.1021/ci050528topenalex-snapshot
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inferredcites →https://doi.org/10.1021/ci800289yopenalex-snapshot
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Profile hidden Markov models.
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Imprint of evolutionary conservation and protein structure variation on the binding function of protein tyrosine kinases
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The Universal Protein Resource (UniProt)
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The Universal Protein Resource (UniProt) 2009
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WebLogo: A Sequence Logo Generator: Figure 1
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Structural biology contributions to the discovery of drugs to treat chronic myelogenous leukaemia
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Crystal Structure of the T315I Mutant of Abl Kinase
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The Protein Kinase Complement of the Human Genome
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Structures of the Tyrosine Kinase Domain of Fibroblast Growth Factor Receptor in Complex with Inhibitors
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Comparative Genomics of the Eukaryotes
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Structural Mechanism for STI-571 Inhibition of Abelson Tyrosine Kinase
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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inferred← citeshttps://doi.org/10.1002/anie.2953141openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s10822-016-9941-0openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s12272-014-0495-1openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bmc.2013.07.021openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bpj.2014.01.031openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ccr.2014.07.007openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.compbiolchem.2015.01.001openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.drudis.2022.04.002openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ejmech.2014.12.038openalex-snapshot
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