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ProteomicsReverse-phase liquid chromatography (RPLC) in Combination with Tip-Based Strong Cation Exchange (SCX-Tip) Fractionation, ReST, an Alternative Approach for Cross-linked Peptides analysis
Chemical cross-linking in combination with mass spectrometry (XL-MS) has emerged as a useful method for structural elucidation of proteins and protein complexes. Efficient enrichment procedures are necessary to analyze cross-linked products due to their relatively low abundance. Currently, strong ca...
ORGANISM(S): Homo sapiens (Human) 
2022-06-16 | PXD023817 | Pride
Scx-tip Mass spectrometry Fractionation Chemical cross-linking 
ProteomicsEfficient micro-scale basic reverse phase peptide fractionation for global and targeted proteomics
This work describes a micro-scale basic reverse phase liquid chromatographic (bRPLC) fractionation method that offers high reproducibility and efficiency for peptide mixtures from small (5-20 g) samples. Shotgun and targeted proteomic analysis were performed to detect differentially expressed prote...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2016-02-09 | MSV000079500 | MassIVE
ProteomicsA proteomic map of human choroid tissue
The choroid is the vascular layer situated between the outer sclera and the inner retina. Together with the ciliary body and the iris it forms the uvea. Because of its rich blood supply it is also called the nutritive layer and it supplies oxygen and nutrition to the retinal pigment epithelium and t...
ORGANISM(S): Homo sapiens (Human) 
2018-04-25 | PXD002273 | Pride
Human Brplc Choroid Eye Lc-ms/ms 
UnknownEfficient Microscale Basic Reverse Phase Peptide Fractionation for Global and Targeted Proteomics.
Not available
S-EPMC5785084 | biostudies-literature
ProteomicsProteome and glycoproteome analysis of fibroblasts from patients with congenital disorders of glycosylation
In the biological systems, several genes are involved in protein glycosylation pathway. Congenital Disorders of Glycosylation (CDG) is known to be a multisystem disorder. Pathogenic variants in the glycosylation genes lead to abnormal N- or O-linked glycosylation that causes cellular stress. We used...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD044327 | Pride
Glycosylation Proteomics Glycoproteomics Cdg Fibroblasts 
ProteomicsN-glycoproteomics and proteomics in NGLY1 deficient patient-derived dermal fibroblasts
In the biological systems, several genes are involved in protein glycosylation and deglycosylation pathways. Congenital disorders of deglycosylation (CDDG) are a set of disorders which occur due to the defect in genes involved in deglycosylation pathways. The only known CDDG so far is the defect in ...
ORGANISM(S): Homo sapiens (Human) 
2023-05-10 | PXD034364 | Pride
Proteomics Fibroblasts Human Glycoproteomics Mass spectrometry Ngly1 Congenital disorder of glycosylation Congenital disorder of deglycosylation 
ProteomicsMapping proteome of seminal plasma and spermatozoa of Indian Indigenous Malnad Gidda (Bos indicus) cattle
Malnad Gidda is one among the 43 registered cattle breeds of India with unique traits and spread over Western Ghats and coastal regions of Karnataka state in India. Selection of highly elite fertile bulls for the breeding purpose is a critical control point in animal breeding programmes. Therefore, ...
ORGANISM(S): Bos indicus 
2020-06-12 | PXD014172 | Pride
Spermatozoa Protein profiling Scx Malnad gidda Seminal plasma Brplc 
ProteomicsFurther delineation of defects in MRPS2 causing human OXPHOS deficiency and early developmental abnormalities in zebrafish
Background: Mitochondrial ribosomal protein-small 2 (MRPS2) encodes a vital structural protein essential for assembling mitochondrial ribosomal small subunit and thus mitochondrial translation. We describe individuals with phenotypes of acute onset severe metabolic decompensation and symptomatic hyp...
ORGANISM(S): Homo sapiens (Human) 
2025-11-10 | PXD062317 | Pride
Mitochondrial disorder Rare disease Genetic disorder 
UnknownData of phosphoproteomic analysis of non-functioning pituitary adenoma.
Not available
S-EPMC5996405 | biostudies-literature
ProteomicsProteomic analysis of Pichia pastoris GS115
Pichia pastoris GS115 was cultured in YPD medium and protein were extracted and separated on SDS-PAGE followed by in-gel trypsin digestion. Protein were also digested in-solution using trypsin and fractionated using SCX and bRPLC. A total of 101 peptide fractions were analyzed on LTQ-Orbitrap Velos ...
ORGANISM(S): Komagataella pastoris (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris) 
2014-11-18 | PXD000627 | Pride
Pichia Lc-ms/ms 
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