Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution - Wikidata - awgldk - TriplyDB

Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution

Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution

http://www.wikidata.org/entity/Q27738995

about

Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1 NMR structures of membrane proteins in phospholipid bilayers NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles Structural studies of the HIV-1 accessory protein Vpu in langmuir monolayers: synchrotron X-ray reflectivity.Integrated analysis of residue coevolution and protein structures capture key protein sectors in HIV-1 proteins Creating a community resource for protein science.Molecular dynamics investigation of membrane-bound bundles of the channel-forming transmembrane domain of viral protein U from the human immunodeficiency virus HIV-1.Full length Vpu from HIV-1: combining molecular dynamics simulations with NMR spectroscopy.Peptide structural analysis by solid-state NMR spectroscopy.Comparative structural studies of Vpu peptides in phospholipid monolayers by x-ray scattering.Viroporins.Misdirection of membrane trafficking by HIV-1 Vpu and Nef: Keys to viral virulence and persistence.Vpu from HIV-1 on an atomic scale: experiments and computer simulations.Serine Phosphorylation of HIV-1 Vpu and Its Binding to Tetherin Regulates Interaction with Clathrin Adaptors.Relating structure and function of viral membrane-spanning miniproteins Correlation of the structural and functional domains in the membrane protein Vpu from HIV-1.Membrane protein assembly: two cytoplasmic phosphorylated serine sites of Vpu from HIV-1 affect oligomerization.Protein intrinsic disorder as a flexible armor and a weapon of HIV-1.Characterization of a novel simian immunodeficiency virus (SIVmonNG1) genome sequence from a mona monkey (Cercopithecus mona).Molecular dynamics simulations on the first two helices of Vpu from HIV-1.Patch formation of a viral channel forming protein within a lipid membrane--Vpu of HIV-1.Structural determination of virus protein U from HIV-1 by NMR in membrane environments.When a domain is not a domain, and why it is important to properly filter proteins in databases: conflicting definitions and fold classification systems for structural domains make filtering of such databases imperative Interaction of amiloride and one of its derivatives with Vpu from HIV-1: a molecular dynamics simulation.Assembling viral channel forming proteins: Vpu from HIV-1.Mapping the interaction between the cytoplasmic domains of HIV-1 viral protein U and human CD4 with NMR spectroscopy Modern High Resolution NMR for the Study of Structure, Dynamics and Interactions of Biological Macromolecules Evidences for Viral Strain Selection in Late Stages of HIV Infection: An Analysis of Vpu Alleles

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P2860

Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution

http://www.wikidata.org/entity/Q27738995

description

1997 nî lūn-bûn

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1997 թուականի Մայիսին հրատարակուած գիտական յօդուած

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1997 թվականի մայիսին հրատարակված գիտական հոդված

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1997年の論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年论文

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name

Secondary structure and tertia ...... cytoplasmic domain in solution

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Secondary structure and tertia ...... cytoplasmic domain in solution

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Secondary structure and tertia ...... cytoplasmic domain in solution

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Secondary structure and tertia ...... cytoplasmic domain in solution

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Secondary structure and tertia ...... cytoplasmic domain in solution

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Secondary structure and tertia ...... cytoplasmic domain in solution

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Secondary structure and tertia ...... cytoplasmic domain in solution

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Secondary structure and tertia ...... cytoplasmic domain in solution

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Secondary structure and tertia ...... cytoplasmic domain in solution

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J.1432-1033.1997.T01-1-00581.X

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Secondary structure and tertia ...... cytoplasmic domain in solution

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P2860

Structural studies of HIV-1 Tat protein

Structure of human parathyroid hormone 1-37 in solution

Prediction of protein secondary structure at better than 70% accuracy

Global fold determination from a small number of distance restraints.

The human immunodeficiency virus type 1 Vpu protein: a potential regulator of proteolysis and protein transport in the mammalian secretory pathway.

The human immunodeficiency virus type 1 encoded Vpu protein is phosphorylated by casein kinase-2 (CK-2) at positions Ser52 and Ser56 within a predicted alpha-helix-turn-alpha-helix-motif.

Characterization of a trifluoroethanol-induced partially folded state of alpha-lactalbumin.

Solution structure of the hydrophilic region of HIV-1 encoded virus protein U (Vpu) by CD and lH NMR spectroscopy

Interaction between the Cytoplasmic Domains of HIV-1 Vpu and CD4: Role of Vpu Residues Involved in CD4 Interaction andin VitroCD4 Degradation

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Dieter Willbold

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