PXD021003 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Identification of human proteins interacting with locked G4 structures |
Description | G4 are noncanonical secondary structures consist in stacked tetrads of Hoogsteen hydrogen-bonded guanines bases. An essential feature of G-quadruplexes is their intrinsic polymorphic nature. Indeed, depending on the length and the composition of the sequence, as well as the environmental conditions (including the nature and concentration of metal cations, and local molecular crowding), a G-quadruplex-forming sequence can adopt different topologies in which the strands are in parallel or antiparallel conformations, with the co-existence of different types of loops (lateral, diagonal or propeller) with variable lengths. The impact of G4 on cellular metabolism is associated with protein or enzymatic factors that promote, inhibits or resolve these structures. Thus, the major impact of G4 on the human cell metabolism is associated with genetic defects affecting proteins that counteract their formation. Although a large number of proteins able to bind and/or "to resolve" G-quadruplex structures have been identified in vitro, less is known about their mode of interaction with G-quadruplex, their specificity versus the topology and finally their specificity for G4 structures relatively to G-rich single-stranded sequences. In this study we aimed to identify and characterize human proteins interacting with locked G4 structures. |
HostingRepository | PRIDE |
AnnounceDate | 2021-07-16 |
AnnouncementXML | Submission_2021-07-15_23:50:48.840.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Yohann Couté |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | LTQ Orbitrap Velos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2020-08-19 08:34:39 | ID requested | |
⏵ 1 | 2021-07-15 23:50:49 | announced | |
Publication List
Pipier A, Devaux A, Lavergne T, Adrait A, Cout, é Y, Britton S, Calsou P, Riou JF, Defrancq E, Gomez D, Constrained G4 structures unveil topology specificity of known and new G4 binding proteins. Sci Rep, 11(1):13469(2021) [pubmed] |
Keyword List
submitter keyword: G-quadruplex, Constrained G4 structures, Proteins, RNA Pol II pausing, nanoLC-MS/MS |
Contact List
Virginie Brun |
contact affiliation | EDyP |
contact email | virginie.brun@cea.fr |
lab head | |
Yohann Couté |
contact affiliation | EDyP |
contact email | yohann.coute@cea.fr |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
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[ - ]
- PRIDE
- PXD021003
- Label: PRIDE project
- Name: Identification of human proteins interacting with locked G4 structures