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ProteomicsDam1 complex-microtubule interaction
we used cross-linking mass spectrometry to determine the molecular architecture of the Dam1 complex alone and bound to microtubules. Our data provide a map of the subunit arrangement of the Dam1 complex. Analysis of the Dam1 complex assembled around microtubules reveals that the Spc34 and Ask1 sub...
ORGANISM(S): Candida albicans (Yeast) 
2016-03-01 | PXD003678 | Pride
Microtubule Mass spectrometry Cross-linking Dam1 complex 
ProteomicsStructural Basis for CAL1-Mediated Centromere Maintenance
Intermolecular interactions stabilising the CAL1–CENP-A/H4 complex were analysed using chemical Cross-Linking Mass Spectrometry (CLMS). Purified recombinant CAL11-160–CENP-A101-225–H4 complex was crosslinked using EDC and BS3. The crosslinked peptides were analysed by mass spectrometry to identify i...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2020-03-11 | PXD017238 | Pride
Cal1/cenp-a/cenp-c/centromeres/chromosome segregation 
ProteomicsAurora B kinase disrupts the extended conformation of lattice-bound Kinesin-13 MCAK
We reveal that MCAK has a compact conformation in solution using cross-linking and electron microscopy. When MCAK is bound to the microtubule ends, it adopts an extended conformation with the N terminus and neck region of MCAK interacting with the microtubule. Also Aurora Bphosphorylation does not a...
ORGANISM(S): Homo sapiens (Human) 
2019-01-07 | PXD008215 | Pride
Mcak Phosphorylation Microtubules Aurora b 
ProteomicsDirect Nucleosome Binding of Borealin Secures Chromosome Association of the Chromosomal Passenger Complex
CPC-NCP complexes were crosslinked using EDC and analysed by mass spectrometry. The results showed Borealin is critical for nucleosome binding made extensive contacts with NCPs, whereas Survivin interactions are mostly limited to the BIR domain and the H3 N-terminal tail as expected. Mapping the cro...
ORGANISM(S): Homo sapiens (Human) Xenopus laevis (African clawed frog) 
2019-09-30 | PXD012882 | Pride
Nucleosome core particles Chromosomal passenger complex Crosslinking 
ProteomicsIntegrative structural analysis of NF90-NF45 heterodimers reveals architectural rearrangements and oligomerisation on binding dsRNA
EDC Crosslinking Mass Spectrometry with quantitation of NF90-NF45 protein complex and NF45-NF90long-dsRNA complex
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD053010 | Pride
Crosslinking mass spectrometry Dsrnas Human nf45-nf90 complexes 
ProteomicsSka3-microtubule interactions - Ska3 Ensures Timely Mitotic Progression by Interacting Directly With Microtubules and Ska1 Microtubule Binding Domain
The Ndc 80 and Ska complex are the major microtubule-binding factors of the kinetochore responsible for maintaining chromosome-microtubule coupling during chromosome segregation. We previously showed that the Ska1 subunit of the Skacomlex binds dynamic microtubules. This project demonstrated that Sk...
ORGANISM(S): Homo sapiens (Human) 
2016-10-03 | PXD004952 | Pride
Microtubule Ska complex 
ProteomicsReconstitution of microtubule nucleation in vitro reveals novel roles for Mzt1
Protein-protein interaction within the MGM holocomplex has been investigated by chemical cross-linking mass spectrometry using EDC (1-ethyl-3-(3-dimethylaminopropyl)carbodiimide) cross-linker. Although this analysis was not exhaustive, we observed crosslinks between Alp4 and Alp6 along the length of...
ORGANISM(S): Schizosaccharomyces pombe 
2019-05-27 | PXD012624 | Pride
“mgm” (mto/gamma/mozart) holocomplex Cross-linking 
ProteomicsLamin A dimer and tetramer cross-links help explain disease mutations and polymer plasticity
Lamins are intermediate filament proteins responsible for nuclear mechanical integrity. Though linked to multiple heritable diseases, lamin structure and that of other intermediate filaments remains elusive. We employed cross-linking mass spectrometry to gain structural insights into lamin A dimer a...
ORGANISM(S): Homo sapiens (Human) Rattus norvegicus (Rat) 
2019-07-12 | PXD008337 | Pride
Silac Cross-link mass spectrometry Em Lamin a 
ProteomicsLamin A molecular compression and sliding as mechanisms behind nucleoskeleton elasticity (complementary data of PXD008337)
Lamin A is a nuclear intermediate filament protein critical for nuclear architecture and mechanics and mutated in a wide range of human diseases. Yet little is known about the molecular architecture of lamins and mechanisms of their assembly. Here we use cross-linking SILAC mass spectrometry to dete...
ORGANISM(S): Rattus norvegicus (Rat) 
2019-07-12 | PXD014009 | Pride
Lamin a Coiled coil Compression Disordered linker 
ProteomicsCross-linking mass spectrometric analysis of Ska-MT interactions
This project is about characterizing the interaction of the MT-binding domains (MTBD) of the human Ska complex with MTs by cross-linking mass spectrometry
ORGANISM(S): Homo sapiens (Human) 
2016-01-28 | PXD003502 | Pride
Cross-linking Microtubules Ska complex Lc-ms/ms 
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