Compaction and binding properties of the intrinsically disordered C-terminal domain of Henipavirus nucleoprotein as unveiled by deletion studies.

Compaction and binding properties of the intrinsically disordered C-terminal domain of Henipavirus nucleoprotein as unveiled by deletion studies.

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http://www.wikidata.org/entity/Q54348285
Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virusStructural disorder within paramyxoviral nucleoproteinsIntrinsic disorder mediates hepatitis C virus core-host cell protein interactions.Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus.Structural Disorder within Paramyxoviral Nucleoproteins and Phosphoproteins in Their Free and Bound Forms: From Predictions to Experimental Assessment.Modulation of Re-initiation of Measles Virus Transcription at Intergenic Regions by PXD to NTAIL Binding Strength.The structurally disordered paramyxovirus nucleocapsid protein tail domain is a regulator of the mRNA transcription gradient.How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication.How disordered is my protein and what is its disorder for? A guide through the "dark side" of the protein universe.Charge neutralization as the major factor for the assembly of nucleocapsid-like particles from C-terminal truncated hepatitis C virus core protein.Interaction between the C-terminal domains of measles virus nucleoprotein and phosphoprotein: a tight complex implying one binding site.The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1.Dynamics of the intrinsically disordered C-terminal domain of the nipah virus nucleoprotein and interaction with the x domain of the phosphoprotein as unveiled by NMR spectroscopy.Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site-directed spin labeling EPR spectroscopy.Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins.Fuzzy regions in an intrinsically disordered protein impair protein-protein interactions.
P2860

Compaction and binding properties of the intrinsically disordered C-terminal domain of Henipavirus nucleoprotein as unveiled by deletion studies.

Item
http://www.wikidata.org/entity/Q54348285
description
2011 nî lūn-bûn
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2011年の論文
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2011年学术文章
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2011年学术文章
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2011年学术文章
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2011年学术文章
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2011年学术文章
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2011年學術文章
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2011年學術文章
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2011年學術文章
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Compaction and binding propert ...... unveiled by deletion studies.
@en
Compaction and binding propert ...... unveiled by deletion studies.
@nl
type
label
Compaction and binding propert ...... unveiled by deletion studies.
@en
Compaction and binding propert ...... unveiled by deletion studies.
@nl
prefLabel
Compaction and binding propert ...... unveiled by deletion studies.
@en
Compaction and binding propert ...... unveiled by deletion studies.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P356
P1433
P1476
Compaction and binding propert ...... unveiled by deletion studies.
@en
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698