Asymmetric binding of transferrin receptor to parvovirus capsids - Test2 - elhamkhani - TriplyDB

Asymmetric binding of transferrin receptor to parvovirus capsids

Asymmetric binding of transferrin receptor to parvovirus capsids

http://www.wikidata.org/entity/Q24683829

about

Structural studies of the giant mimivirus Parvovirus glycan interactions Structural Comparison of Different Antibodies Interacting with Parvovirus Capsids Structure of a Packaging-Defective Mutant of Minute Virus of Mice Indicates that the Genome Is Packaged via a Pore at a 5-Fold Axis Structural and Functional Analysis of Coxsackievirus A9 Integrin v 6 Binding and Uncoating The Asymmetric Structure of an Icosahedral Virus Bound to Its Receptor Suggests a Mechanism for Genome Release A Strain-Specific Epitope of Enterovirus 71 Identified by Cryo-Electron Microscopy of the Complex with Fab from Neutralizing Antibody Structure of adeno-associated virus-2 in complex with neutralizing monoclonal antibody A20 Asymmetric genome organization in an RNA virus revealed via graph-theoretical analysis of tomographic data Host-specific parvovirus evolution in nature is recapitulated by in vitro adaptation to different carnivore species.Global displacement of canine parvovirus by a host-adapted variant: structural comparison between pandemic viruses with distinct host ranges.Single Mutations in the VP2 300 Loop Region of the Three-Fold Spike of the Carnivore Parvovirus Capsid Can Determine Host Range.Early steps in cell infection by parvoviruses: host-specific differences in cell receptor binding but similar endosomal trafficking.Limited transferrin receptor clustering allows rapid diffusion of canine parvovirus into clathrin endocytic structures Binding site on the transferrin receptor for the parvovirus capsid and effects of altered affinity on cell uptake and infection.Interaction of alphaVbeta3 and alphaVbeta6 integrins with human parechovirus 1.Evolutionary reconstructions of the transferrin receptor of Caniforms supports canine parvovirus being a re-emerged and not a novel pathogen in dogs Detecting small changes and additional peptides in the canine parvovirus capsid structure Maturation of flaviviruses starts from one or more icosahedrally independent nucleation centres The role of evolutionary intermediates in the host adaptation of canine parvovirus.Single-Particle Tracking Shows that a Point Mutation in the Carnivore Parvovirus Capsid Switches Binding between Host-Specific Transferrin Receptors.The Receptor-Binding Domain in the VP1u Region of Parvovirus B19.An icosahedral algal virus has a complex unique vertex decorated by a spike.Near-Atomic Resolution Structure of a Highly Neutralizing Fab Bound to Canine Parvovirus.Cells under siege: viral glycoprotein interactions at the cell surface.Structure of viruses: a short history.Molecular characterization of canine parvovirus in Vientiane, Laos.Parvovirus Capsid Structures Required for Infection: Mutations Controlling Receptor Recognition and Protease Cleavages.The novel asymmetric entry intermediate of a picornavirus captured with nanodiscs.Heparin binding induces conformational changes in Adeno-associated virus serotype 2.Interpretation of electron density with stereographic roadmap projections.Atomic Resolution Structure of the Oncolytic Parvovirus LuIII by Electron Microscopy and 3D Image Reconstruction.Protoparvovirus Cell Entry.Geometric Defects and Icosahedral Viruses.Atomic Resolution Structures of Human Bufaviruses Determined by Cryo-Electron Microscopy.Complex and dynamic interactions between parvovirus capsids, transferrin receptors and antibodies control cell infection and host range.All-atom molecular dynamics of the HBV capsid reveals insights into biological function and cryo-EM resolution limits.Parvoviruses: structure and infection

P2860

Q21145824-B54BC062-D4DC-4B75-9A5D-7C1E52C337C1 Q26858992-690B680F-F609-490C-85F2-D6B966BECA78 Q27654389-BCDB8F1C-147F-496F-AE7A-0A6C6F4D3FF6 Q27667143-0EADB49B-FB10-419B-B4E8-2C73844F11C6 Q27676071-463F836D-46C7-4106-B005-4FE107064B30 Q27678838-A01C090E-D205-48DA-BEA0-063C85F94C70 Q27679681-5123E94E-6930-464C-9315-E968B3B90A31 Q27681034-5CA5D1D9-8239-4A91-ABE1-B518F4BE93BD Q28544752-ED159431-7A60-48DD-B700-0AD77CF4481F Q30368432-4C004267-F59A-4BBF-A248-F1D34B8CF7DC Q30368796-E9EF5886-301E-459D-8F8C-DD622F657347 Q30380782-A053E171-F1D7-4A8A-8877-E08D85B40851 Q30490592-58228A61-6ACA-45E3-ABC7-BBFA838C97C3 Q30513989-E330EA7A-C1B8-47C3-BE6D-D6531A0FE2AF Q33826804-E6E8D4BF-1D61-487C-8293-B74DBA021500 Q34055408-67E490CE-9FBA-47BC-9123-3B265892DBF2 Q34263045-FA42E90D-897B-49C8-8920-05269B3D33D3 Q34808356-2078BBE6-34FF-43C1-8D46-BB7310602552 Q35082677-4B21C4AD-27C9-45F2-AAE0-E9CD42CB677B Q35689594-D905DF50-D9F2-4188-A09D-4148F32FA6BF Q35926928-C6FE2AE6-7700-4234-A438-AD10E1144B44 Q36735626-21A20DB8-D857-4AC3-9F95-E27DCD36B306 Q37256969-CB8C4658-9806-4770-B04E-6BDDF9392035 Q37347315-25380E4F-1306-4EBC-92A2-7B1EA7E20FB1 Q37858167-46E35922-06A9-4606-9E9B-C6732ED777E5 Q38124416-C4D13C6A-CB8B-41A8-8630-2D8B136242C2 Q40357699-2928D8DF-8905-444C-BE76-712E2BE5DDF0 Q40450578-DD21EDEE-64AB-4768-98C1-BB7F4816AAA8 Q40558572-E36959AE-3F10-497B-ACBD-D664D6871E25 Q41572340-AEA82E86-8434-4E78-836F-BDC571EE6204 Q41937157-341DD039-0033-435E-881F-0F9AAD9B07A4 Q46210737-DF5309DA-EA97-457A-B58B-105175343B62 Q46274294-AC258ED2-00D1-4A42-9843-1C37A768DB13 Q47233096-D887D5AF-9136-4360-8DF5-3ACE856143F5 Q47233169-AEF2ECE7-CDE6-4B4B-9733-B905011DADFC Q52309601-74A3B4BD-D52C-4858-BB43-3885F6869BAB Q53282380-2D72988F-B484-4381-BDA3-563F9DA7B43C Q56115905-E207702F-1CF6-4D62-A46B-E0BB3E555C49

P2860

Asymmetric binding of transferrin receptor to parvovirus capsids

http://www.wikidata.org/entity/Q24683829

description

2007 nî lūn-bûn

@nan

2007 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年学术文章

@wuu

2007年学术文章

@zh-cn

2007年学术文章

@zh-hans

2007年学术文章

@zh-my

2007年学术文章

@zh-sg

2007年學術文章

@yue

name

Asymmetric binding of transferrin receptor to parvovirus capsids

@ast

Asymmetric binding of transferrin receptor to parvovirus capsids

@en

Asymmetric binding of transferrin receptor to parvovirus capsids

@nl

type

label

Asymmetric binding of transferrin receptor to parvovirus capsids

@ast

Asymmetric binding of transferrin receptor to parvovirus capsids

@en

Asymmetric binding of transferrin receptor to parvovirus capsids

@nl

prefLabel

Asymmetric binding of transferrin receptor to parvovirus capsids

@ast

Asymmetric binding of transferrin receptor to parvovirus capsids

@en

Asymmetric binding of transferrin receptor to parvovirus capsids

@nl

P1433

Q24683829-0323B21B-D429-4128-A938-8D13ECC399D7

P1476

Q24683829-44EDD038-6F0D-4EEB-867E-CAB3F468D723

P2093

Q24683829-0CFA5D23-CA97-4F0F-BD8B-84B4799A85B7

Q24683829-2CD477B3-A994-4329-8A5E-36A3905E1259

Q24683829-307A928C-23BC-4ABA-8261-5093BE7F417E

Q24683829-78F8AD9B-4848-40CE-8027-F04165AC8AA0

Q24683829-87425B9A-4574-48F0-86E1-7FF331E27B79

Q24683829-967436E5-74F9-4C23-944A-4D7AF7B7ED3B

Q24683829-EAF53351-2308-400A-92E6-C86845981206

P2860

Q24683829-05223FEB-E037-4D7A-87F4-E9188D9D1595

Q24683829-11EC748B-8BB4-46E2-BA30-28B715F6281C

Q24683829-16C4C44B-B72D-48F1-88F6-A149A58C41D6

Q24683829-32C98DB0-7722-4092-AEF7-639CD9A576CB

Q24683829-3A58B2C8-F871-4FCF-A255-F12C757EC56E

Q24683829-42133EB0-5A05-4B9B-8EFA-4304349B1A9B

Q24683829-42568856-DAE4-4CDD-B6F6-FA5CFC434F33

Q24683829-4A06C79E-99BE-4600-8D32-13423210D0FA

Q24683829-4DEF4DFE-0FD9-47EC-986F-2DB5FBC3457F

Q24683829-51E21386-21FA-4F5A-AFD6-B2708C6446E2

P304

Q24683829-42512D36-E22C-4141-A99D-FED35EADE397

P31

Q24683829-CEB37585-5F07-487F-BB32-253577A7B520

P3181

Q24683829-9BB92B94-D25B-42EC-9E73-2FA623C841FE

P356

Q24683829-DED5ACE2-5F66-4FE6-8801-E8D81A9F1F31

P407

Q24683829-C6550A3D-864E-40A2-835E-3F2763EE4DBC

P433

Q24683829-503581F2-FA3A-42AE-9869-F6A372CF41C3

P478

Q24683829-B048920C-6D72-4596-A87C-29C235202C93

P50

Q24683829-0A3960E5-2004-40CE-A390-0ACDB3C0872A

Q24683829-9A55D513-0DA8-478E-8614-3DDCEFAF0D27

Q24683829-A076BD6F-7E19-4F8A-A960-33BACC7D7D19

Q24683829-B05D1CF8-A4D5-4995-87E6-D4A4E232AD58

P577

Q24683829-A4C4AE30-C141-4EC8-907A-AEF19B6A8D78

P5875

Q24683829-8B227F15-4C44-4390-B58F-26CFD56C1582

P698

Q24683829-868D5DFB-91F9-4164-8AC4-E52F37D7458D

P921

Q24683829-07EAFAA3-0433-401E-B2DC-28A109FB81EE

P932

Q24683829-44AC429B-D29E-493C-AB8F-8B569A3D8FEB

P3181

P356

PNAS.0701574104

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Asymmetric binding of transferrin receptor to parvovirus capsids

@en

P2093

Anthony J Battisti

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

Christian D S Nelson

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

Colin R Parrish

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

Laura M Palermo

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

Marc C Morais

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

Paul R Chipman

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

Valorie D Bowman

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

P2860

Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor

THE ORIGINS OF NEW PANDEMIC VIRUSES: The Acquisition of New Host Ranges by Canine Parvovirus and Influenza A Viruses

How Viruses Enter Animal Cells

Structural analysis of viral nucleocapsids by subtraction of partial projections

Crystal structure of the ectodomain of human transferrin receptor

The structure and evolution of the major capsid protein of a large, lipid-containing DNA virus.

Bacteriophage phi29 scaffolding protein gp7 before and after prohead assembly

Adding the Third Dimension to Virus Life Cycles: Three-Dimensional Reconstruction of Icosahedral Viruses from Cryo-Electron Micrographs

The canine parvovirus empty capsid structure

Structure determination of feline panleukopenia virus empty particles

P304

6585-9

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

P31

scholarly article

P3181

3909680

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

P356

10.1073/PNAS.0701574104

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

P407

P433

16

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

P478

104

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

P50

Michael Rossmann

Victor A Kostyuchenko

Susan Hafenstein

P577

2007-04-17T00:00:00Z

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

P5875

6403190

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

P698

17420467

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

P921

P932

1871829

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