Sort   by:  
 Page size 
TranscriptomicsRNA-Seq Profiling of a Defective Seed Coat Mutation in Glycine max Reveals Differential Expression of Proline Rich and Other Cell Wall Protein Transcripts
The plant cell wall performs a number of essential functions including providing shape to many different cell types and serving as a defense against potential pathogens. The net pattern mutation creates breaks in the seed coat of soybean (Glycine max) because of ruptured cell walls. Using RNA-Seq, w...
ORGANISM(S): Glycine max 
2014-05-16 | E-GEOD-54903 | biostudies-arrayexpress
TranscriptomicsThe Estrogen Receptor Co-Regulator Protein, Proline Glutamic Acid and Leucine Rich Protein 1 (PELP1) Mediates Estrogen Rapid Signaling and Neuroprotection in the Brain
We examined the role of PELP1 in E2-ER-mediated transcription in the hippocampus under conditions of GCI by perfroming global transcriptome analysis. E2-treated FLOX and PELP1 FBKO mice were subjected to GCI followed by 24 h reperfusion and the isolated RNA was utilized for RNA-seq analysis. Our res...
ORGANISM(S): Mus musculus 
2015-12-07 | E-GEOD-72136 | biostudies-arrayexpress
ProteomicsHuman salivary basic proline-rich proteins
Human basic proline-rich proteins and basic glycosylated proline-rich proteins are the most complex family of human adult salivary proteins, secreted only by the parotid gland, expressed by the polymorphic PRB1-4 genes. This study reports the results obtained for their characterization in our labora...
ORGANISM(S): Homo sapiens (Human) 
2018-08-08 | PXD009813 | Pride
Human High-resolution esi−ms/ms experiments Saliva 
ProteomicsMapping of transglutaminase 2 active sites of human salivary small basic proline-rich
Due to the distinctive features of oral mucosa, determination of the proteins involved in the formation of “oral protein pellicle” is demanding. The present study investigated the susceptibility of several human basic proline-rich peptides (bPRPs) named P-H, P-D, P-F, P-J, and II-2 as substrates of ...
ORGANISM(S): Homo sapiens (Human) 
2019-10-25 | PXD014658 | Pride
Bprps Saliva Transglutaminase 2 Human 
ProteomicsCharacterization of the interactome of receptor tyrosine kinase proline rich motifs
Here we explore the interactome of the proline-rich motif regions of non-activated receptor tyrosine kinases by affinity purification mass spectrometry.
ORGANISM(S): Homo sapiens (Human) 
2024-10-01 | PXD041383 | Pride
Human Cancer Receptor tyrosine kinase 
ProteomicsPepSAVI-MS reveals proline-rich antimicrobial peptide in Amaranthus tricolor
PepSAVI-MS, a mass spectrometry-based peptidomics pipeline, was implemented for antimicrobial peptide (AMP) discovery in the medicinal plant Amaranthus tricolor. This investigation revealed a novel 1.7 kDa AMP, deemed Atr-AMP1. Initial efforts to determine the sequence of Atr-AMP1 utilized chemical ...
ORGANISM(S): Amaranthus tricolor 
2020-05-26 | PXD014547 | Pride
Peptidomics E. coli Mass spectrometry Amaranthus tricolor Antimicrobial peptides Pepsavi-ms Hydroxyproline 
ProteomicsProteinase K digestion of Annexin A11 fibrils
Human Annexin A11 (Uniprot accession no. P50995) head domain (residues 2-196) was recombinantly expressed, purified, fibrilized, and digested by proteinase K. Products were analyzed by LC/MS/MS.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-01-20 | MSV000091107 | MassIVE
GenomicsRole of the proline-rich disordered domain of DROSHA in intronic microRNA processing
Role of the proline-rich disordered domain of DROSHA in intronic microRNA processing
PRJNA961731 | ENA
ProteomicsA novel RNA binding protein YebC enhances translation of proline-rich amino acid stretches in bacteria
The ribosome employs a set of highly conserved translation factors to efficiently synthesise proteins. Some translation factors interact with the ribosome in a transient manner and are thus challenging to identify. However, proteins involved in translation could be specifically identified by their i...
ORGANISM(S): Streptococcus pyogenes M1 GAS 
2025-07-14 | PXD054642 | Pride
Streptococcus pyogenes Rna binding protein Rna Rna-protein xl 
ProteomicsPRR of Tau Crosslinking with Tubulin
We used cross-linking mass spectrometry with the cleavable cross-linker, disuccinimidyl dibutyric urea (DSBU) to map sites of interaction between the proline rich domain (PRR, tau amino acids 149-244) and tubulin. For comparison, we also conducted these experiments with PRR constructs containing mul...
ORGANISM(S): Bos taurus (Bovine) Escherichia coli 
2026-03-09 | PXD049384 | Pride
Tubulin Tau Phosphorylation Proline rich region 
Sort   by:  
 Page size