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Data from: A quantitative proteomic analysis of cofilin phosphorylation in myeloid cells and its modulation using the LIM kinase inhibitor Pyr1
负责人:
关键词:
Lim kinases;leukemia;Mus musculus;cofilin;proteomics;Homo Sapiens;phosphorylation
DOI:
doi:10.5061/dryad.4n5929c
摘要:
LIM kinases are located at a strategic crossroad, downstream of several signaling pathways and upstream of effectors such as microtubules
LIM Domain Kinase 1 (LIMK1), Human Kinase Domain; A Target Enabling Package
负责人:
Eidarus Salah;;Beltrami, Alessandra;;Apirat Chaikuad;;Hanke, Thomas;;Kashima, Risa;;Canning, Peter;;Knapp, Susanne Muller;;Knaus, Petra;;Hata, Aki
关键词:
Structural Genomics Drug Discovery Chemical Biology
DOI:
doi:10.5287/bodleian:zg5naqjyk
摘要:
ng via the kinase LIMK1. LIMK1 performs inhibitory phosphorylation on cofilin proteins blocking their actin-severing activity. Excessive BMPR2-LIM
Human Lim Domain Kinase 1 (Limk1), Kinase Domain; A Target Enabling Package
负责人:
关键词:
protein target enabling package disease structure cancer neuropsychiatry neuro neurological genetic disorders metabolic diseases oncology
DOI:
doi:10.5281/zenodo.1287260
摘要:
ng via the kinase LIMK1. LIMK1 performs inhibitory phosphorylation on cofilin proteins blocking their actin-severing activity. Excessive BMPR2-LIM
Human Lim Domain Kinase 1 (Limk1), Kinase Domain; A Target Enabling Package
负责人:
关键词:
protein target enabling package disease structure cancer neuropsychiatry neuro neurological genetic disorders metabolic diseases oncology
DOI:
doi:10.5281/zenodo.1241027
摘要:
ng via the kinase LIMK1. LIMK1 performs inhibitory phosphorylation on cofilin proteins blocking their actin-severing activity. Excessive BMPR2-LIM
Human LIM domain kinase 1 (LIMK1), kinase domain; A Target Enabling Package
负责人:
关键词:
protein target enabling package disease structure cancer neuropsychiatry neuro neurological genetic disorders metabolic diseases oncology
DOI:
doi:10.5281/zenodo.1219706
摘要:
ng via the kinase LIMK1. LIMK1 performs inhibitory phosphorylation on cofilin proteins blocking their actin-severing activity. Excessive BMPR2-LIM
Data from: Structure-based network analysis of activation mechanisms in the ErbB family of receptor tyrosine kinases: the regulatory spine residues
负责人:
关键词:
protein kinases;protein structure network analysis;structural stability;force constant analysis
DOI:
doi:10.5061/dryad.qj597
摘要:
s in the ErbB kinases. We have determined that residues that are indispensable for kinase regulation and catalysis often corresponded to the high centrality nodes
Data from: A highly sensitive LC-MS/MS method to determine novel Bruton's tyrosine kinase inhibitor spebrutinib: application to metabolic stability evaluation
负责人:
关键词:
LC-MS\/MS;Human liver microsomes;Metabolic stability assessment;Spebrutinib
DOI:
doi:10.5061/dryad.5m09t8k
摘要:
Spebrutinib (SBT) is a Bruton's tyrosine kinase inhibitor. SBT is currently in phase II and phase I clinical trials for the management
Data from: Ecological relevance of energy metabolism: transcriptional responses in energy sensing and expenditure to thermal and osmotic stresses
负责人:
关键词:
desiccation;Rain;Environmental stress;metabolic sensor;intertidal zone;glycolysis;temperature;energy metabolism;Cellana toreuma
DOI:
doi:10.5061/dryad.6824n
摘要:
high temperature, desiccation and rainfall. Expression levels of genes encoding metabolic regulators [two subunits of AMP-activated protein kinase, ampk?, ampk?; Fu
Data from: Dissecting nutrient-related co-expression networks in phosphate starved poplars
负责人:
关键词:
nutrition;ionome;phosphorus deficiciency;Not applicable;transcriptome;Populus × canescens
DOI:
doi:10.5061/dryad.3t5q5
摘要:
in the plant. In this module the GO term “response to P starvation” was enriched with phosphoenolpyruvate carboxylase kinases, phosphatases and pyrophosphatases
Data from: Dopamine promotes motor cortex plasticity and motor skill learning via PLC activation
负责人:
关键词:
phospholipase C;long term potentiation;motor cortex;learning;synaptic plasticity;dopamine
DOI:
doi:10.5061/dryad.mp5s3
摘要:
ferent G-proteins and bidirectionally modulate protein kinase A (PKA), leading to distinct physiological and behavioral effects. Here we show that D1

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