Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G - Test2 - elhamkhani - TriplyDB

Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G

Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G

http://www.wikidata.org/entity/Q27704710

about

Deconstructing the Antiviral Neutralizing-Antibody Response: Implications for Vaccine Development and Immunity Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site Griffithsin: An Antiviral Lectin with Outstanding Therapeutic Potential Survivors Remorse: antibody-mediated protection against HIV-1.Asymmetric recognition of HIV-1 Envelope trimer by V1V2 loop-targeting antibodies.Free Energy Perturbation Calculation of Relative Binding Free Energy between Broadly Neutralizing Antibodies and the gp120 Glycoprotein of HIV-1.Stabilized HIV-1 envelope glycoprotein trimers for vaccine use.Protein post-translational modifications: In silico prediction tools and molecular modeling.Antigenicity-defined conformations of an extremely neutralization-resistant HIV-1 envelope spike.Glycine Substitution at Helix-to-Coil Transitions Facilitates the Structural Determination of a Stabilized Subtype C HIV Envelope Glycoprotein Reducing V3 Antigenicity and Immunogenicity on Soluble, Native-Like HIV-1 Env SOSIP Trimers Glycosylation of the core of the HIV-1 envelope subunit protein gp120 is not required for native trimer formation or viral infectivity.Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein.Diversification in the HIV-1 Envelope Hyper-variable Domains V2, V4, and V5 and Higher Probability of Transmitted/Founder Envelope Glycosylation Favor the Development of Heterologous Neutralization Breadth Experimental Estimation of the Effects of All Amino-Acid Mutations to HIV's Envelope Protein on Viral Replication in Cell Culture Receptor Activation of HIV-1 Env Leads to Asymmetric Exposure of the gp41 Trimer.Structure and Recognition of a Novel HIV-1 gp120-gp41 Interface Antibody that Caused MPER Exposure through Viral Escape.Antibodyomics: bioinformatics technologies for understanding B-cell immunity to HIV-1.Delineating CD4 dependency of HIV-1: Adaptation to infect low level CD4 expressing target cells widens cellular tropism but severely impacts on envelope functionality.Effects of partially dismantling the CD4 binding site glycan fence of HIV-1 Envelope glycoprotein trimers on neutralizing antibody induction.Tyrosine-sulfated V2 peptides inhibit HIV-1 infection via coreceptor mimicry.Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding.Epitope-Independent Purification of Native-Like Envelope Trimers from Diverse HIV-1 Isolates.Structure of an N276-Dependent HIV-1 Neutralizing Antibody Targeting a Rare V5 Glycan Hole Adjacent to the CD4 Binding Site.Cryo-EM structure of a CD4-bound open HIV-1 envelope trimer reveals structural rearrangements of the gp120 V1V2 loop.Substrate recognition and catalysis by GH47 α-mannosidases involved in Asn-linked glycan maturation in the mammalian secretory pathway.Differences in Allelic Frequency and CDRH3 Region Limit the Engagement of HIV Env Immunogens by Putative VRC01 Neutralizing Antibody Precursors.Native-like Env trimers as a platform for HIV-1 vaccine design.Ontogeny-based immunogens for the induction of V2-directed HIV broadly neutralizing antibodies.Structural Analysis of the Glycosylated Intact HIV-1 gp120-b12 Antibody Complex Using Hydroxyl Radical Protein Footprinting.Improving the Expression and Purification of Soluble, Recombinant Native-Like HIV-1 Envelope Glycoprotein Trimers by Targeted Sequence Changes.Glycosylation Benchmark Profile for HIV-1 Envelope Glycoprotein Production Based on Eleven Env Trimers.Plasticity and Epitope Exposure of the HIV-1 Envelope Trimer.Changes in Structure and Antigenicity of HIV-1 Env Trimers Resulting from Removal of a Conserved CD4 Binding Site-Proximal Glycan.Recognition of HIV-inactivating peptide triazoles by the recombinant soluble Env trimer, BG505 SOSIP.664.Synthetic multivalent V3 glycopeptides display enhanced recognition by glycan-dependent HIV-1 broadly neutralizing antibodies.Antiviral lectins: Selective inhibitors of viral entry.Approaches to the induction of HIV broadly neutralizing antibodies.Genetic and structural analyses of affinity maturation in the humoral response to HIV-1.

P2860

Q27654848-467DDB95-B659-41A5-80D7-B979BCC1839D Q27728036-24D172B8-E057-4038-9F9E-98B4E7FBC5C4 Q27728037-0B953A4F-CC12-4237-B570-53CCB47F8995 Q27928014-8C938E1E-B642-48C3-9855-A8C01B0D2370 Q30238730-D9E7E06A-B159-48EE-B3C3-E47515B5B564 Q30352300-A199A1D6-05DF-4617-A0DC-0E30080347C3 Q30395868-C23D5CA2-AE9F-4B11-A562-79A2B736BAB2 Q30490942-8ED82AE2-6DA1-480B-8960-2B0B2777944D Q33580119-9EBC5D4F-074E-437C-869B-AD06121B37D9 Q33620194-214912FD-0AB0-43D3-95DF-8CCB284468DB Q33711154-6F87EF94-AF82-4FC3-A966-41B6F6D17AC0 Q33907694-C9F820E9-9A6E-445C-AABD-14B76A235307 Q34555891-2010FB89-46F0-4E48-9C29-2383E2F98B5F Q36157560-D6AAC9FE-7897-439F-8F17-52D0AEB27955 Q36194234-B3911821-FA43-4E95-9452-5858B3BD2051 Q36222292-95A926BC-DB33-48E8-B732-25AA5F748067 Q36228646-69161E23-ADE0-4D36-86C8-285090EB9509 Q36246403-6F4813BD-961D-4BFE-848B-5EAE2D58A364 Q36263513-42039A5D-E266-4CDC-81E3-C1875C0F185C Q36298503-89AB2730-7245-4AA2-9B5F-1AFF4311D98C Q36303368-FCC1AD17-0912-4215-9620-3FB19957DDE7 Q37221499-584D0851-77A5-4AFB-B807-420DAF61560A Q37240035-BA9519BB-9C8D-45C6-B2C6-96D0481DA3E4 Q37300461-8A2D8E20-4A46-4F48-BEB1-CF00DC8D34DF Q37409244-52C0C044-3978-42DF-8A16-9E9C9D1204B9 Q37469648-3A14AED7-B650-4D01-A46C-13EC9EC7E943 Q37493274-BF1CB616-F1E6-4C27-BF82-6D6225AD6DAF Q37551245-399A70C7-C828-446C-9DDB-B62DA1E13C1A Q37633417-463E1557-E664-4EE3-829D-A3B75ED2F54A Q37634061-94AC3BF3-C7C6-41AE-971B-85A65BABCDC1 Q37656791-FF97C057-E469-4D0D-B430-EF4051DA9931 Q38708708-970EAE63-1965-48A3-82E5-5D1C5A363CC6 Q38716288-50070693-46C0-4BEA-B755-5CD36924A35E Q38725480-188AFDDC-E7E8-4A00-8F69-ED40627E8A55 Q38753943-97887844-CDD5-4CA1-9C3B-DF323BF53FDC Q38774504-58DBB925-E002-4361-95ED-419096FA46CE Q38807382-8DC2AA65-3999-4E5A-B83B-35177E2B5215 Q38891044-EB6C34A6-F0A2-4C17-948E-2AC5184EFA9D Q38936867-B375202E-829C-4FD1-BC32-53F0D44DF919 Q38992744-1313E446-096B-468D-815B-856039FC8961

P2860

Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G

http://www.wikidata.org/entity/Q27704710

description

2016 nî lūn-bûn

@nan

2016 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2016 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

name

Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G

@ast

Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G

@en

Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G

@nl

type

label

Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G

@ast

Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G

@en

Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G

@nl

prefLabel

Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G

@ast

Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G

@en

Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G

@nl

P1433

Q27704710-3345D920-C06D-4F7B-9D94-7E798CBCBB5C

P1476

Q27704710-729D2D06-C8FC-499E-BDD2-9CD950DA8404

P2093

Q27704710-15E1030E-377E-4745-B770-4F8757947D9C

Q27704710-175CE2F7-DA71-437B-B308-D513A3277BF1

Q27704710-17D27E8D-C35F-4E62-8E94-CD041303091B

Q27704710-1A4D26F1-C77B-4B44-9946-273423AFCA46

Q27704710-1F95C688-4798-4E43-939C-E7DD96284A2D

Q27704710-3C4F0922-FF79-4509-ACD4-17E4F31F3D79

Q27704710-45F47B42-932D-48E5-B39C-B316EDEF61F1

Q27704710-49CD89A0-FE64-409F-8C75-2EF84EEAA8E9

Q27704710-57F24311-3128-4B4C-B51A-3E1C85EF61AE

Q27704710-65B74561-CFC7-4D82-A990-27D1486D27BB

P2860

Q27704710-0F3B50FF-1616-4515-91DE-45DCC4FC0945

Q27704710-12E73583-5360-4FE9-9812-1245649C5865

Q27704710-17896725-F984-49AA-8AF2-3E233230B111

Q27704710-1B82BC8D-F291-45FD-B3EE-C489BA93D7DA

Q27704710-1F42802D-B7A9-4468-BBE4-D751B8DCD986

Q27704710-2ECE991B-2DEC-421C-B7FC-B49DF05C2ED1

Q27704710-31B45878-2E94-4403-96A3-99271AED07EA

Q27704710-36EE8AD7-9EBB-4272-A39A-CC58588A5ECC

Q27704710-3A127042-F857-4B23-881B-B3613BB3E8BB

Q27704710-3A950D13-B193-4DF2-A6F3-D8C4A69EDC20

P304

Q27704710-5AB2C5CC-0D49-4436-B3C4-2F4029157806

P31

Q27704710-45DA7BCD-6FC7-4120-A392-BFCDE699CB67

P3181

Q27704710-00F6A9E6-BDB7-42EC-8124-BC0B1AF6743D

P356

Q27704710-A783FF86-4FB8-43A5-BB62-CE572EF59591

P407

Q27704710-F9DB1B41-D0BA-4AEA-BAB0-44B17BA15FE7

P433

Q27704710-4FAFE098-93EE-4F2F-BEA8-40CD972444ED

P478

Q27704710-433B7F86-12F4-444F-B9A9-C3C2D2A38161

P50

Q27704710-032320E8-06FC-4577-95D6-3A852ABD4A99

Q27704710-552B4BC1-3D61-4A83-B990-88011AE75B7E

Q27704710-699E7EC7-5FFF-475D-AC55-83DF43F48111

Q27704710-95E5729C-969C-43FF-9597-A6C660E6B3AC

Q27704710-A794F1C4-E441-45BC-B09A-2AF543A10DEF

Q27704710-C473F134-8FD3-42B4-9D48-E7F5A5F9FD71

Q27704710-E5CCB8A2-09B3-4F32-840B-70B571E4A31C

P577

Q27704710-EAE9332B-80C4-4C25-AB73-4236C39E8088

P5875

Q27704710-B2922151-6C6D-4E5D-B7A9-898701D94680

P698

Q27704710-186929B1-0796-4C64-A56F-C970692D5B11

P932

Q27704710-A7985189-9780-4BD7-B615-4452176B076F

P3181

P356

J.CELL.2016.04.010

P1433

P1476

Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G

@en

P2093

Aliaksandr Druz

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

Anna-Janina Behrens

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

Baoshan Zhang

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

Chang W Choi

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

Chang-Chun D Lee

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

Chi-Huey Wong

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

Chung-Yi Wu

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

Dennis R Burton

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

Guillaume B E Stewart-Jones

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

Gwo-Yu Chuang

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

P2860

Structural mechanism of trimeric HIV-1 envelope glycoprotein activation

The HIV-1 Envelope Glycoproteins: Fusogens, Antigens, and Immunogens

Rates of molecular evolution in RNA viruses: a quantitative phylogenetic analysis

The hepatitis C virus glycan shield and evasion of the humoral immune response

Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site

Structural Repertoire of HIV-1-Neutralizing Antibodies Targeting the CD4 Supersite in 14 Donors

Crystal structure, conformational fixation and entry-related interactions of mature ligand-free HIV-1 Env

Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9

Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies

Structures of HIV-1 Env V1V2 with broadly neutralizing antibodies reveal commonalities that enable vaccine design

P304

813-826

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

P31

scholarly article

P3181

2829174

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

P356

10.1016/J.CELL.2016.04.010

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

P407

P433

4

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

P478

165

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

P50

Carole A. Bewley

P577

2016-04-21T00:00:00Z

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

P5875

301552437

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

P698

27114034

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

P932

5543418

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