about
A second, non-canonical RNA-dependent RNA polymerase in SARS CoronavirusCrystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoproteinInteraction between the C-terminal domains of N and P proteins of measles virus investigated by NMRCrystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIIIThe Crystal Structure of the Human Co-Chaperone P58IPKStructural basis of fibrillar collagen trimerization and related genetic disorders.Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperoneHsp72 recognizes a P binding motif in the measles virus N protein C-terminusCytosolic 5'-triphosphate ended viral leader transcript of measles virus as activator of the RIG I-mediated interferon responseAssessing protein disorder and induced folding.Structural disorder within the replicative complex of measles virus: functional implications.The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded.Procollagen C-proteinase enhancer grasps the stalk of the C-propeptide trimer to boost collagen precursor maturation.Type I procollagen C-propeptide defects: study of genotype-phenotype correlation and predictive role of crystal structure.Procollagen C-proteinase enhancer stimulates procollagen processing by binding to the C-propeptide region only.Strong cooperativity and loose geometry between CUB domains are the basis for procollagen c-proteinase enhancer activity.High affinity binding between Hsp70 and the C-terminal domain of the measles virus nucleoprotein requires an Hsp40 co-chaperone.The interaction between the measles virus nucleoprotein and the Interferon Regulator Factor 3 relies on a specific cellular environment.Structural characterization of recombinant IAV polymerase reveals a stable complex between viral PA-PB1 heterodimer and host RanBP5.The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner.
P50
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P50
name
Jean-Marie Bourhis
@ast
Jean-Marie Bourhis
@en
Jean-Marie Bourhis
@es
Jean-Marie Bourhis
@nl
type
label
Jean-Marie Bourhis
@ast
Jean-Marie Bourhis
@en
Jean-Marie Bourhis
@es
Jean-Marie Bourhis
@nl
prefLabel
Jean-Marie Bourhis
@ast
Jean-Marie Bourhis
@en
Jean-Marie Bourhis
@es
Jean-Marie Bourhis
@nl