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001-es BibID:BIBFORM054071
Első szerző:Lee, Robin van der
Cím:Classification of intrinsically disordered regions and proteins / Robin van der Lee, Marija Buljan, Benjamin Lang, Robert J. Weatheritt, Gary W. Daughdrill, A. Keith Dunker, Monika Fuxreiter, Julian Gough, Joerg Gsponer, David T. Jones, Philip M. Kim, Richard W. Kriwacki, Christopher J. Oldfield, Rohit V. Pappu, Peter Tompa, Vladimir N. Uversky, Peter E. Wright, M. Madan Babu
Dátum:2014
ISSN:0009-2665
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Chemical Reviews. - 114 : 13 (2014), p. 6589-6631. -
További szerzők:Buljan, Marija Lang, Benjamin Weatheritt, Robert J. Daughdrill, Gary W. Dunker, A. Keith Fuxreiter Mónika (1969-) (kutató vegyész) Gough, Julian Gsponer, Joerg Jones, David T. W. Kim, Philip M. Kriwacki, Richard W. Oldfield, Christopher J. Pappu, Rohit V. Tompa Péter Uversky, Vladimir N. Wright, Peter E. Babu, M. Madan
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2.

001-es BibID:BIBFORM031424
035-os BibID:WOS:000264694500008 PMID:19260013
Első szerző:Tompa Péter
Cím:Close encounters of the third kind: disordered domains and the interactions of proteins / Peter Tompa, Monika Fuxreiter, Christopher J. Oldfield, Istvan Simon, A. Keith Dunker, Vladimir N. Uversky
Dátum:2009
ISSN:0265-9247
Megjegyzések:Protein-protein interactions are thought to be mediated by domains, which areautonomous folding units of proteins. Recently, a second type of interaction hasbeen suggested, mediated by short segments termed linear motifs, which arerelated to recognition elements of intrinsically disordered regions. Here, wepropose a third kind of protein-protein recognition mechanism, mediated bydisordered regions longer than 20-30 residues. Bioinformatics predictions andwell-characterized examples, such as the kinase-inhibitory domain of Cdkinhibitors and the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 ofactin-binding proteins, show that these disordered regions conform to thedefinition of domains rather than motifs, i.e., they represent functional,evolutionary, and structural units. Their functions are distinct from those ofshort motifs and ordered domains, and establish a third kind of interactionprinciple. With these points, we argue that these long disordered regions shouldbe recognized as a distinct class of biologically functional protein domains.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Bioessays. - 31 : 3 (2009), p. 328-335. -
További szerzők:Fuxreiter Mónika (1969-) (kutató vegyész) Oldfield, Christopher J. Simon István Dunker, A. Keith Uversky, Vladimir N.
Pályázati támogatás:K60694
OTKA
NK71582
OTKA
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM031420
035-os BibID:WOS:000263923800012
Első szerző:Tóth-Petróczy Ágnes
Cím:Malleable machines in transcription regulation : the mediator complex / Ágnes Tóth-Petróczy, Christopher J. Oldfield, István Simon, Yuichiro Takagi, A. Keith Dunker, Vladimir N. Uversky, Mónika Fuxreiter
Dátum:2008
ISSN:1553-734X
Megjegyzések:The Mediator complex provides an interface between gene-specific regulatory proteins and the general transcription machinery including RNA polymerase II (RNAP II). The complex has a modular architecture (Head, Middle, and Tail) and cryoelectron microscopy analysis suggested that it undergoes dramatic conformational changes upon interactions with activators and RNAP II. These rearrangements have been proposed to play a role in the assembly of the preinitiation complex and also to contribute to the regulatory mechanism of Mediator. In analogy to many regulatory and transcriptional proteins, we reasoned that Mediator might also utilize intrinsically disordered regions (IDRs) to facilitate structural transitions and transmit transcriptional signals. Indeed, a high prevalence of IDRs was found in various subunits of Mediator from both Saccharomyces cerevisiae and Homo sapiens, especially in the Tail and the Middle modules. The level of disorder increases from yeast to man, although in both organisms it significantly exceeds that of multiprotein complexes of a similar size. IDRs can contribute to Mediator's function in three different ways: they can individually serve as target sites for multiple partners having distinctive structures; they can act as malleable linkers connecting globular domains that impart modular functionality on the complex; and they can also facilitate assembly and disassembly of complexes in response to regulatory signals. Short segments of IDRs, termed molecular recognition features (MoRFs) distinguished by a high protein-protein interaction propensity, were identified in 16 and 19 subunits of the yeast and human Mediator, respectively. In Saccharomyces cerevisiae, the functional roles of 11 MoRFs have been experimentally verified, and those in the Med8/Med18/Med20 and Med7/Med21 complexes were structurally confirmed. Although the Saccharomyces cerevisiae and Homo sapiens Mediator sequences are only weakly conserved, the arrangements of the disordered regions and their embedded interaction sites are quite similar in the two organisms. All of these data suggest an integral role for intrinsic disorder in Mediator's function.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:PLoS Computational Biology. - 4 : 12 (2008), p. e1000243. -
További szerzők:Oldfield, Christopher J. Simon István Takagi, Yuichiro Dunker, A. Keith Uversky, Vladimir N. Fuxreiter Mónika (1969-) (kutató vegyész)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM054889
Első szerző:Uversky, Vladimir N.
Cím:Intrinsically disordered proteins and their recognition functions / Vladimir N. Uversky, Monika Fuxreiter, Christopher J. Oldfield, A. Keith Dunker, Peter Tompa
Dátum:2009
ISBN:978-1-420-07005-7
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
Megjelenés:Computational protein-protein interaction / ed. by Ruth Nussinov, Gideon Scheiber. - p. 223-253. -
További szerzők:Fuxreiter Mónika (1969-) (kutató vegyész) Oldfield, Christopher J. Dunker, A. Keith Tompa Péter
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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