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Dynamic proteins and multi-protein complexes govern most biological processes. Cross-linking/mass spectrometry (CLMS) is increasingly successful in providing residue- resolution data on static proteinaceous structures. Here we investigate the technical feasibility of recording dynamic processes usin...
ORGANISM(S): Homo sapiens (Human) 
2015-06-08 | PXD002142 | Pride
The analysis of proteins and protein complexes by cross-linking mass spectrometry (XL-MS) has expanded in the last dec-ade. However, mostly used approaches suffer important limitations in term of efficiency and sensitivity. We describe here a new workflow based on the advanced use of the trifunction...
ORGANISM(S): Oryctolagus cuniculus (Rabbit) 
2021-08-11 | PXD010422 | Pride
The nucleocapsid N is one of four structural proteins of the coronaviruses. Its essential role in genome encapsidation makes it a critical therapeutic target for COVID-19 and related diseases. However, the inherent disorder of full-length N has hampered its structural analysis. Here, we describe a s...
ORGANISM(S): Severe acute respiratory syndrome coronavirus 2 
2025-07-21 | PXD052584 | Pride
In higher plants, a P-type proton pumping ATPase generates the proton-motive force essential for the function of all other transporters and for proper growth and development. X-ray crystallographic studies of the plant plasma membrane proton pump have provided information on amino acids involved in...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2018-09-24 | PXD010892 | Pride
We have developed a new and robust in vivo cross-linking mass spectrometry (XL-MS) that utilizes a multifunctional MS-cleavable cross-linker to enable the efficient capture, enrichment, and identification of in vivo cross-linked peptides at the whole proteome scale.
ORGANISM(S): Homo sapiens (Human) 
2021-07-30 | PXD012788 | Pride
Cross-linking mass spectrometry performed on intact nuclei purified from HEK293T for structural interactome profiling of the nuclear pore complex
ORGANISM(S): Homo sapiens (Human) 
2026-09-21 | PXD080872 | Pride
The tetrameric tumor suppressor p53 represents a great challenge for 3D structural analysis due to its high degree of intrinsic disorder (ca. 40%). We developed and applied an integrative structural biology approach combining complementary techniques of structural mass spectrometry (MS), namely cros...
ORGANISM(S): Escherichia coli 
2023-06-26 | PXD037030 | Pride
We investigated points in the typical sample workflow that could contribute to the perceived low cross-linking yields. We demonstrate, through a 2-step cross-linking strategy called Click-Linking, that the chemical reaction is not the main contributor to the low number of identified cross-links. We ...
ORGANISM(S): Homo sapiens (Human) 
2025-11-18 | PXD069512 | Pride
An experimental and computational approach for identification of protein-protein interactions by in-vivo chemical crosslinking and mass spectrometry (CLMS) has been developed that takes advantage of the specific characteristics of cyanurbiotindipropionylsuccinimide (CBDPS), an affinity-tagged isotop...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-03-17 | PXD014055 | Pride
An experimental and computational approach for identification of protein-protein interactions by in-vivo chemical crosslinking and mass spectrometry (CLMS) has been developed that takes advantage of the specific characteristics of cyanurbiotindipropionylsuccinimide (CBDPS), an affinity-tagged isotop...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-03-17 | PXD017066 | Pride
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