Fusing structure and function: a structural view of the herpesvirus entry machinery. - Wikidata - awgldk - TriplyDB

Fusing structure and function: a structural view of the herpesvirus entry machinery.

Fusing structure and function: a structural view of the herpesvirus entry machinery.

http://www.wikidata.org/entity/Q35622700

about

New viruses for cancer therapy: meeting clinical needs Analysis of a neutralizing antibody for human herpesvirus 6B reveals a role for glycoprotein Q1 in viral entry Human complement receptor type 1/CD35 is an Epstein-Barr Virus receptor Zika Fetal Neuropathogenesis: Etiology of a Viral Syndrome Virion Glycoprotein-Mediated Immune Evasion by Human Cytomegalovirus: a Sticky Virus Makes a Slick Getaway Structural and Mechanistic Insights into the Tropism of Epstein-Barr Virus Retargeting Strategies for Oncolytic Herpes Simplex Viruses Nanostructures for the Inhibition of Viral Infections Human immunodeficiency virus and heparan sulfate: from attachment to entry inhibition Current and potential treatments for ubiquitous but neglected herpesvirus infections Revisit the Correlation between the Elastic Mechanics and Fusion of Lipid Membranes Structure of Herpes Simplex Virus Glycoprotein D Bound to the Human Receptor Nectin-1 Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion Structural basis for the antibody neutralization ofHerpes simplex virus Mechanism for neutralizing activity by the anti-CMV gH/gL monoclonal antibody MSL-109 Interaction domain of glycoproteins gB and gH of Marek's disease virus and identification of an antiviral peptide with dual functions The lantibiotic peptide labyrinthopeptin A1 demonstrates broad anti-HIV and anti-HSV activity with potential for microbicidal applications Comparative proteomics reveals novel components at the plasma membrane of differentiated HepaRG cells and different distribution in hepatocyte- and biliary-like cells Assembly and architecture of the EBV B cell entry triggering complex Antigenic Characterization of the HCMV gH/gL/gO and Pentamer Cell Entry Complexes Reveals Binding Sites for Potently Neutralizing Human Antibodies Characterization of Vesicular Stomatitis Virus Pseudotypes Bearing Essential Entry Glycoproteins gB, gD, gH, and gL of Herpes Simplex Virus 1.Anti-Viral Properties of Amyloid-β Peptides.Herpesviral capture of immunomodulatory host genes.Herpes simplex virus internalization into epithelial cells requires Na+/H+ exchangers and p21-activated kinases but neither clathrin- nor caveolin-mediated endocytosis.Importance of Highly Conserved Peptide Sites of Human Cytomegalovirus gO for Formation of the gH/gL/gO Complex.Dysregulated Glycoprotein B-Mediated Cell-Cell Fusion Disrupts Varicella-Zoster Virus and Host Gene Transcription during Infection.A derivative of platelet-derived growth factor receptor alpha binds to the trimer of human cytomegalovirus and inhibits entry into fibroblasts and endothelial cells Insertion of a ligand to HER2 in gB retargets HSV tropism and obviates the need for activation of the other entry glycoproteins.Herpesvirus Entry into Host Cells Mediated by Endosomal Low pH.Dendritic cells during Epstein Barr virus infection.Global sensing of the antigenic structure of herpes simplex virus gD using high-throughput array-based SPR imaging.Genome-wide analysis of wild-type Epstein-Barr virus genomes derived from healthy individuals of the 1,000 Genomes Project.Newcastle disease virus (NDV) recombinants expressing infectious laryngotracheitis virus (ILTV) glycoproteins gB and gD protect chickens against ILTV and NDV challenges.A receptor-based switch that regulates anthrax toxin pore formation.Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.Antibody-induced conformational changes in herpes simplex virus glycoprotein gD reveal new targets for virus neutralization.The Epstein-Barr virus (EBV) glycoprotein B cytoplasmic C-terminal tail domain regulates the energy requirement for EBV-induced membrane fusion.Herpes simplex virus glycoproteins gH/gL and gB bind Toll-like receptor 2, and soluble gH/gL is sufficient to activate NF-κB Amino acid differences in glycoproteins B (gB), C (gC), H (gH) and L (gL) are associated with enhanced herpes simplex virus type-1 (McKrae) entry via the paired immunoglobulin-like type-2 receptor α.Herpes virus fusion and entry: a story with many characters.

P2860

Q24567699-8759654E-AB47-42BA-870A-87AEE744B8A4 Q24631036-B0B21CD8-469F-4FA2-99FA-C1CD38BD31B4 Q24632150-6582B26D-FA41-487D-B911-BC6EB8FCD613 Q26700454-4350C4D0-B96B-470F-AF1D-7EE70DB29CFE Q26745798-BC15C99B-E260-45DE-B1AF-468C033D01A1 Q26752331-B5E13AF7-BB2F-4747-BEA5-6650705FA6C6 Q26765439-2A35C3C9-1541-4DD8-8028-2E092520FF0D Q26801513-BB7515DE-A7EA-478A-9444-EF3EB2DD2E8D Q27004059-A1E8498C-B1B2-4E19-997C-7A8412B8326E Q27023452-EA3BE039-CFFE-469A-9A62-29E41066D342 Q27317843-084A18AC-0ACF-4F28-8A34-DEFFF9482192 Q27674775-3AFD8932-5AC8-4482-A7F4-61E63B8E97F3 Q27676007-970C43A0-3993-4618-B97C-5D9BED95C21D Q27680164-0D00F339-20BB-4B0D-B56E-F6FC2E34ABF0 Q27683850-0C3A7E7E-517F-4B9A-A93E-B5482ECA7A10 Q28486009-3504FA8F-3611-4476-9B7F-03D37E67061B Q28533345-FE85CD6F-0DB7-4DDB-8CB5-7C92443C0570 Q28535470-9F54AF89-70FD-463C-9760-A7D7944E800C Q28542501-D997F432-3C26-4A44-8B8E-241E009E7DF3 Q28550400-96EEC4DF-73DC-4A93-9D40-F5C64F99AFC4 Q30353044-406A21AA-D672-4E38-A9A2-34A73B69B3C1 Q30390299-8109846E-F2A6-4277-9236-7C554C25709F Q30401468-547B3AC1-69EA-4999-AA6E-3D2433310403 Q30405542-562D6FB2-460D-478F-9416-281E7D3C4773 Q30832341-7C1CB89D-0BBB-41D6-89DB-1AA6BCDDA73F Q30832346-52C93236-13A3-4085-BFEC-1FCCED51A068 Q33558900-1346A4DF-44D7-422E-9549-EDD9E0E8DE88 Q33621028-2C01530B-724D-4C64-AA12-DDC92911D325 Q33727577-6F0FF9BE-119E-4F7F-8E02-775B7B3BF769 Q33782152-368728CB-C6A5-4DEB-A8D2-AE5B36829B85 Q33834821-AE8EBB3F-BB47-4273-B43A-F624403455DB Q33925373-458337A9-A1C4-47A0-BDF4-D12DF8EBE4F3 Q34057946-F6A78D37-D30B-4E6F-ACB5-E6069E0D73B0 Q34102678-DF6FC750-BB17-4566-AFF4-CC946947E46F Q34182329-D69DDA26-27FF-4294-A86B-087AF01AB46A Q34237174-BE97A6DC-7F16-4DE9-9639-E90962CBFC00 Q34261421-90418302-83F6-4DDD-9F41-6EC826D5EDDE Q34267595-1FB10755-183F-4A3B-B21E-B9D108F542CD Q34281238-76AF0361-1707-4415-A2C2-57A511B857B0 Q34285628-35C52B70-33C2-42BB-BF06-EA55CB1FA109

P2860

Fusing structure and function: a structural view of the herpesvirus entry machinery.

http://www.wikidata.org/entity/Q35622700

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

2011年论文

@zh

2011年论文

@zh-cn

name

Fusing structure and function: a structural view of the herpesvirus entry machinery.

@ast

Fusing structure and function: a structural view of the herpesvirus entry machinery.

@en

type

label

Fusing structure and function: a structural view of the herpesvirus entry machinery.

@ast

Fusing structure and function: a structural view of the herpesvirus entry machinery.

@en

prefLabel

Fusing structure and function: a structural view of the herpesvirus entry machinery.

@ast

Fusing structure and function: a structural view of the herpesvirus entry machinery.

@en

P1433

Q35622700-8F2BE36A-4F57-4696-943E-252A8677F4A0

P1476

Q35622700-20C2DECA-30E7-4075-8995-47A73A181FDC

P2093

Q35622700-025D3251-D1DA-4F6D-B5E8-5249F78EDB81

Q35622700-044132B1-6F7F-4D70-80EE-8B2DB49469F6

Q35622700-2C50B3D4-B93E-4D48-9916-EFDFAA19225B

Q35622700-B890C4EF-EC34-4F40-B410-8880A05004DC

P2860

Q35622700-058128D4-4A8C-43F1-B745-2421DEA70BD5

Q35622700-064CB2CA-291F-4467-8EA1-498B5519216B

Q35622700-065E3A14-818A-4B30-8E72-30674D0ADD95

Q35622700-07F33958-B684-4C61-91DE-6B904A0ED6DB

Q35622700-0A183296-2DFB-4550-B8F2-BD1F9DC5F566

Q35622700-0BED8C57-5B8D-42FB-B5C0-1B2C60CACB37

Q35622700-0C0F7893-8BF3-4632-AA0A-923CA5D1C929

Q35622700-0E313408-9DC0-4827-AB07-DCD2DDD94812

Q35622700-0EBC17A7-C9B1-4E9D-B1E7-35F46DC2EFAF

Q35622700-0ED65080-A73D-4AAC-A910-AA9A86338A6A

P2888

Q35622700-3E4AA52D-337F-4858-B0DE-5709315B0DBA

P304

Q35622700-BB41DE76-F22A-488D-8DCD-9A9D32A38C4E

P31

Q35622700-24FE392B-E451-4177-9B86-FBFEB1C7BE4B

P356

Q35622700-ABD5F1E1-FC0D-4F87-B4F2-304C0C3F78EF

P407

Q35622700-E5322CE0-681F-4250-A75A-4A930CAE6C05

P433

Q35622700-2924F9F0-4576-4523-A36E-C2AC3D82AA8F

P478

Q35622700-923FBD05-4AF2-4364-9720-7DE472DD25BB

P577

Q35622700-3B517885-6900-482A-8A1E-31F6A2C4EDF1

P5875

Q35622700-B2EC6CFB-A617-48F5-BC1C-7431B6006A73

P698

Q35622700-A55CE7BB-3F0A-4BEB-8F27-F36165F6D2C5

P932

Q35622700-E2A3EE20-8E83-4DF8-A644-39FFA9059AC3

P356

P1433

Nature Reviews Microbiology

P1476

Fusing structure and function: a structural view of the herpesvirus entry machinery.

@en

P2093

Julia O Jackson

http://www.w3.org/2001/XMLSchema#string

Richard Longnecker

http://www.w3.org/2001/XMLSchema#string

Sarah A Connolly

http://www.w3.org/2001/XMLSchema#string

Theodore S Jardetzky

http://www.w3.org/2001/XMLSchema#string

P2860

Epstein-Barr virus infection of polarized tongue and nasopharyngeal epithelial cells

PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein B

Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor

Structure-based analysis of the herpes simplex virus glycoprotein D binding site present on herpesvirus entry mediator HveA (HVEM).

Bimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion

Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1

Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops

HIV-1 entry inhibitors: an overview

Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B

Antigenic and mutational analyses of herpes simplex virus glycoprotein B reveal four functional regions

P2888

P304

369-381

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1038/NRMICRO2548

http://www.w3.org/2001/XMLSchema#string

P407

P433

5

http://www.w3.org/2001/XMLSchema#string

P478

9

http://www.w3.org/2001/XMLSchema#string

P577

2011-04-11T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

51037849

http://www.w3.org/2001/XMLSchema#string

P698

21478902

http://www.w3.org/2001/XMLSchema#string

P932

3242325

http://www.w3.org/2001/XMLSchema#string