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MetabolomicsTowards engineering ectomycorrhization into switchgrass bioenergy crops via a lectin receptor-like kinase
Soil-borne microbes can establish compatible relationships with host plants, providing a large variety of nutritive and protective compounds in exchange for photosynthesized sugars. However, the molecular mechanisms mediating the establishment of these beneficial relationships remain unclear. Our pr...
2021-08-11 | MTBLS2597 | MetaboLights
ProteomicsDynamics of S752D MuSK kinase domain
The dynamics of purified MuSK S752D kinase domain was probed by HDX-MS.
ORGANISM(S): Homo sapiens (Human) 
2026-08-17 | PXD072130 | Pride
Kinase domain Hdx-ms Musk 
ProteomicsDynamics of wild-type MuSK kinase domain
The dynamics of purified wild-type kinase domain was probed by HDX-MS.
ORGANISM(S): Homo sapiens (Human) 
2026-08-17 | PXD071785 | Pride
Kinase domain Hdx-ms Musk 
GenomicsMutation Detection in p210 kinase domain
Mutation Detection in p210 kinase domain
PRJNA1303185 | ENA
ProteomicsAnalysis of PKD1 autophosphorylation in vitro and confirmation of stoichiometric S742 phosphorylation of a recombinant PRKD1 kinase domain
Protein kinase D1 (PRKD1, also referred to as PKD1), has been proposed to undergo autophosphorylation on serine 742 and potentially also on serine 738 in the activation loop of its kinase domain. We used recombinant PKD1 kinase domain to test whether PKD1 is indeed able to undergo autophosphorylatio...
ORGANISM(S): Homo sapiens (Human) 
2019-08-19 | PXD013216 | Pride
Pkd1 Protein kinase d 
TranscriptomicsGene Expression Profiling of the MLL-AF4 and Flt3 tyrosine kinase domain (TKD) genes in 32Dc cell
The tumorigenesis capacity of MLL-AF4 alone is insufficient for causing leukemia. Based on the finding that an Flt3 gene mutation in the tyrosine kinase domain (TKD) was observed in approximately 15% of MLL leukemia, we investigated synergistic leukemogenesis effects of the two genes in vitro. In a ...
ORGANISM(S): Mus musculus 
2009-03-31 | E-GEOD-14236 | biostudies-arrayexpress
MetabolomicsSCP4-STK35/PDIK1L complex is a dual phospho-catalytic signaling dependency in acute myeloid leukemia
Acute myeloid leukemia (AML) cells rely on phospho-signaling pathways to gain unlimited proliferation potential. Here, we used domain-focused CRISPR screening to identify the nuclear phosphatase SCP4 as a dependency in AML, yet this enzyme is dispensable in normal hematopoietic progenitor cells. Usi...
2025-05-29 | MTBLS3707 | MetaboLights
ProteomicsInvestigating the monomer-dimer transition of PKD1 kinase domain with EDC crosslinking
The project aim was to generate experimental constraints for the in silico modeling of the dimeric structure of the PKD kinase domain. And identify conformational changes upon dimerization. For this we used the heterobifunctional zero length crosslinker EDC to identify salt bridges within the protei...
ORGANISM(S): Homo sapiens (Human) 
2023-03-11 | PXD031997 | Pride
Protein kinase d Kinase domain dimer Activation loop ordering 
ProteomicsPost-translational modification mapping - CRK10 WT and crk10-A397T kinase domain
We have analysed the recombinant kinase domain of AtCRK10 (At4g23180) purified as an N-terminal His-tag from Escherichia coli cells by LC-MS/MS. Both the WT and the crk10-A39T7 mutant allele of the CRK10 kinase domain were analysed. Post-translational modifications were identified, and a MASCOT sear...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2023-07-20 | PXD023831 | Pride
Arabidopsis Cysteine-rich receptor-like kinase Kinase domain Crk10 
ProteomicsPKC isoforms activate LRRK1 kinase by phosphorylating conserved residues (Ser1064, Ser1074 and Thr1075) within the CORB GTPase domain
Leucine-rich-repeat-kinase 1 (LRRK1) and its homologue LRRK2 are multidomain kinases possessing an atypical ROC-CORA-CORB containing GTPase domain and phosphorylate distinct Rab proteins. LRRK1 loss of function mutations cause the bone disorder osteosclerotic metaphyseal dysplasia, whereas LRRK2 mis...
ORGANISM(S): Homo sapiens (Human) 
2022-09-02 | PXD034420 | Pride
Rab7a Lrrk1 Pkc Phosphorylation 
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