Sort   by:  
 Page size 
ProteomicsMitochondrial dysfunction underlies cell cycle arrest and tubular hypoplasia in ClC-Kb-deficient Bartter syndrome mice
The pathogenesis of Bartter syndrome (BS) has long been attributed to decreased NaCl reabsorption in the thick ascending limb of Henle’s loop (TAL). By studying Clc-k2 (mouse ortholog of ClC-Kb)-knockout (Clc-k2-/-) mice, we recently uncovered an additional mechanism in which loss of transport funct...
ORGANISM(S): Mus musculus (Mouse) 
2026-07-09 | PXD069389 | Pride
Metabolism Clc-k2 Mitochondria Cell cycle Bartter syndrome type 3 
TranscriptomicsAtbZIP16 integrates light and hormone signaling pathways to regulate Arabidopsis early seedling development
In response to environmental light signals, transcriptomic adjustment plays an important role in Arabidopsis seed germination and seedling development. G-box cis-element is commonly present in promoters of genes positively or negatively responding to the light signal. For the pursuit of additional t...
ORGANISM(S): Arabidopsis thaliana 
2013-07-22 | E-GEOD-30910 | biostudies-arrayexpress
ProteomicsAAV Orbitrap CD-MS for AAV2, AAV6, and AAV8
CD-MS analysis collected on an Orbitrap UHMR. Note, this data was collected on a beta version of the DMT software and thus contains STORI files stored in separate zip files. The DMT files are also included as supplemental files, along with the UniDecCD processing parameters.
ORGANISM(S): Adeno-associated Dependoparvovirus A (ncbitaxon:1511891) 
2023-04-05 | MSV000091650 | MassIVE
UnknownOxidation of protein-bound methionine in Photofrin-photodynamic therapy-treated human tumor cells explored by methionine-containing peptide enrichment and quantitative proteomics approach.
Not available
S-EPMC5431048 | biostudies-literature
ProteomicsIdentifying the phosphorylation sites on PNET1 protein in Arabidopsis.
The nuclear pore complex (NPC) is a cornerstone of eukaryotic cell functionality, orchestrating the essential transport of molecules between the nucleus and cytoplasm. Emerging evidence suggests its potential involvement in cell cycle regulation, but the specific roles and mechanisms of nucleoporins...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-08-04 | PXD054530 | Pride
Phosphorylation Nuclear pore complex Immunoprecipitation Cell cycle Callus Lc-ms/ms 
ProteomicsQuantitative proteomics and bioinformatics analyses reveal the mechanism of pan-aurora kinase inhibitor tozasertib in neuroblastoma
Neuroblastoma is the third most common pediatric cancer and is responsible for approximately 15% of all childhood cancer deaths (Maris & Matthay, 1999). In our analysis, we found that poor patient survival with increasing mRNA expression level of AURKA and AURKB in Mycn-amplified neuroblastoma. In t...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2019-09-30 | PXD007640 | Pride
Neuroblastoma/ tozasertib/ itraq/ metabolite/ aurora kinase inhibitor. 
ProteomicsComprehensive understanding the molecular components of LTBR signalling complex in cancers
Lymphotoxin beta receptor (LTBR), a member of TNFRSF, was identified as a key regulator in the development, organization, and homeostasis of lymphoid tissues (Wolf, Seleznik, Zeller, & Heikenwalder, 2010). Recently, LTBR has been shown to play a role in tumor biology, both in solid tumors and in hem...
ORGANISM(S): Homo sapiens (Human) 
2025-04-01 | PXD034142 | Pride
Human Ap-ms Lc-ms Lfq 
ProteomicsMass spectrometry data of the ERα-NTD samples exposed to 0-50ms x-ray beam
Here we present MS data of ERα-NTD protein samples exposed to 0-50 ms of X-ray beam at the Advanced Light Source (Berkeley, CA). Irradiated protein samples were digested with two sets of proteases, Asp-N and Lys-C, and pepsin. LC-MS/MS data was utilized to identify 16 sites of modification listed in...
ORGANISM(S): Homo sapiens (Human) 
2020-05-26 | PXD011361 | Pride
Erα-ntd Lc-ms Fp 
UnknownPrediction for Intravenous Immunoglobulin Resistance by Using Weighted Genetic Risk Score Identified From Genome-Wide Association Study in Kawasaki Disease.
Not available
S-EPMC5647111 | biostudies-literature
ProteomicsPhosphorylation sites of PTPN22 treated by Calyculin A in 293T cells
Phosphorylation sites of PTPN22 induced by Calyculin A treatment were identified by LC-MS
ORGANISM(S): Homo sapiens (Human) 
2021-09-08 | PXD016103 | Pride
Ptpn22 phosphorylation 
Sort   by:  
 Page size