Intrinsic disorder in measles virus nucleocapsids.

scientific article

Intrinsic disorder in measles virus nucleocapsids. is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode2011PNAS..108.9839J
P356DOI10.1073/PNAS.1103270108
P932PMC publication ID3116414
P698PubMed publication ID21613569
P5875ResearchGate publication ID51166207

P50authorMartin BlackledgeQ21994149
Malene Ringkjøbing JensenQ24185684
Sonia LonghiQ42173216
Frank GabelQ51016637
Ambroise DesfossesQ56810338
Loic SalmonQ58189963
P2093author name stringGuillaume Communie
Marc Jamin
Rob W H Ruigrok
Luca Mollica
Nicolas Martinez
Euripedes Almeida Ribeiro
P2860cites workIntrinsically unstructured proteins and their functionsQ22061731
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The molecular length of measles virus RNA and the structural organization of measles nucleocapsidsQ36612474
The hypervariable C-terminal tail of the Sendai paramyxovirus nucleocapsid protein is required for template function but not for RNA encapsidationQ36650413
Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplingsQ37596029
Mechanism of coupled folding and binding of an intrinsically disordered proteinQ40210194
Significant differences in nucleocapsid morphology within the ParamyxoviridaeQ40717498
Characterization of nucleocapsid binding by the measles virus and mumps virus phosphoproteinsQ41275462
Capping and alpha-helix stabilityQ41330687
Measles virus nucleocapsid protein expressed in insect cells assembles into nucleocapsid-like structuresQ41544678
Solution NMR studies of the maturation intermediates of a 13 MDa viral capsidQ41624507
Conformational flexibility in recombinant measles virus nucleocapsids visualised by cryo-negative stain electron microscopy and real-space helical reconstructionQ41628305
Nucleoprotein-RNA orientation in the measles virus nucleocapsid by three-dimensional electron microscopyQ41848162
Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings.Q43243601
The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partnerQ44746385
Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoproteinQ45394782
The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoproteinQ45728875
NMR: prediction of molecular alignment from structure using the PALES software.Q48590571
Combining prediction, computation and experiment for the characterization of protein disorder.Q51635477
On the origin of NMR dipolar waves in transient helical elements of partially folded proteins.Q51872107
A set of BEST triple-resonance experiments for time-optimized protein resonance assignment.Q51916074
Highly populated turn conformations in natively unfolded tau protein identified from residual dipolar couplings and molecular simulation.Q53285737
Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing 2D NMR with reduced radiofrequency loadQ57896529
Conformational analysis of a set of peptides corresponding to the entire primary sequence of the N-terminal domain of the ribosomal protein L9: evidence for stable native-like secondary structure in the unfolded state 1 1Edited by P. E. WrightQ59600485
Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfacesQ67559626
Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoproteinQ94952407
P433issue24
P407language of work or nameEnglishQ1860
P921main subjectmeaslesQ79793
viral nucleocapsidQ4384107
P304page(s)9839-9844
P577publication date2011-05-25
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleIntrinsic disorder in measles virus nucleocapsids
P478volume108

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