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Chemical cross-linking coupled with mass spectrometry plays an important role in unravelling protein interactions, especially weak and transient interactions. Moreover, cross-linking complements several structure determination approaches such as cryo-EM. Although several computational approaches are...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080758 | MassIVE
We describe an efficient decision tree searching strategy (DTSS) to boost the identification of cross-linked peptides. The DTSS approach allows the identification of a wealth of complementary information to facilitate the construction of more protein-protein interaction networks for human cell lysat...
ORGANISM(S): Escherichia coli 
2020-11-23 | PXD018291 | Pride
Chemical cross-linking coupled with mass spectrometry plays an important role in unravelling protein interactions, especially weak and transient interactions. Moreover, cross-linking complements several structure determination approaches such as cryo-EM. Although several computational approaches are...
ORGANISM(S): Homo sapiens (Human) 
2016-09-27 | PXD003880 | Pride
Cross-linking mass spectrometry is an increasingly used, powerful technique to study protein-protein interactions or to provide structural information. Due to sub-stochiometric reaction efficiencies, cross-linked peptides are usually low abundant. This results in challenging data evaluation and the ...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2020-05-11 | PXD016963 | Pride
We compared the five different ways of fragmentation available on a tribrid mass spectrometer and optimized their collision energies with regard to optimal sequence coverage of cross-linked peptides. We created a library of bis(sulfosuccinimidyl)suberate (BS3/DSS) cross-linked precursors, derived fr...
ORGANISM(S): Homo sapiens (Human) 
2017-04-19 | PXD006131 | Pride
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
Cross-linking mass spectrometry (XLMS) is becoming increasingly popular, and current advances are widening the applicability of the technique so that it can be utilized by non-specialist laboratories. Specifically, the use of novel mass spectrometry-cleavable (MS-cleavable) reagents dramatically red...
ORGANISM(S): Bos taurus (Bovine) Cicer arietinum (Chickpea) (Garbanzo) Streptococcus pyogenes serotype M2 Candida albicans (Yeast) Homo sapiens (Human) Oryctolagus cuniculus (Rabbit) Escherichia coli Equus caballus (Horse) 
2019-02-01 | PXD011861 | Pride
Brain-derived amyloid-β (Aβ) dimers are associated with Alzheimer´s disease (AD). However, their covalent nature remains controversial. This feature is relevant, as a covalent cross-link would make brain-derived dimers (native dimers) more synaptotoxic than Aβ monomers and would make them suitable c...
ORGANISM(S): Homo sapiens (Human) 
2021-05-13 | PXD005657 | Pride
Dataset presented in Mango manuscript. Contains Ecoli cross-linked with BDP-NHP. Demonstration of whole proteome in-vivo cross-linking without an instrument capable of serial fragmentation.
ORGANISM(S): Escherichia coli 
2019-02-25 | PXD008975 | Pride
An X-ray crystallography structure of the trimeric nuclear export complex of CRM1, SNP1 and RanGTP is available on the PDB database with the ID 3GJX. To get an XL-MS dataset of a clean sample of a stable protein complex for benchmarking purposes, another sample from the protein expression, purificat...
ORGANISM(S): Escherichia coli 
2020-10-20 | PXD014359 | Pride
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