X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein.
about
A neuronal VLDLR variant lacking the third complement-type repeat exhibits high capacity binding of apoE containing lipoproteinsSpecificity of binding of the low density lipoprotein receptor-related protein to different conformational states of the clade E serpins plasminogen activator inhibitor-1 and proteinase nexin-1Structure of a receptor-binding fragment of reelin and mutational analysis reveal a recognition mechanism similar to endocytic receptorsAsymmetric binding of transferrin receptor to parvovirus capsidsViral entry pathways: the example of common cold virusesInsights into minor group rhinovirus uncoating: the X-ray structure of the HRV2 empty capsidStructure of Seneca Valley Virus-001: An Oncolytic Picornavirus Representing a New GenusMinor group human rhinovirus-receptor interactions: geometry of multimodular attachment and basis of recognitionStructure of the Minimal Interface Between ApoE and LRPInteraction of Decay-Accelerating Factor with Echovirus 7Gentamicin Binds to the Megalin Receptor as a Competitive Inhibitor Using the Common Ligand Binding Motif of Complement Type Repeats: INSIGHT FROM THE NMR STRUCTURE OF THE 10TH COMPLEMENT TYPE REPEAT DOMAIN ALONE AND IN COMPLEX WITH GENTAMICINA sialic acid binding site in a human picornavirusStructural basis of transcobalamin recognition by human CD320 receptorDecoding of lipoprotein-receptor interactions: properties of ligand binding modules governing interactions with apolipoprotein E.The single ligand-binding repeat of Tva, a low density lipoprotein receptor-related protein, contains two ligand-binding surfaces.Receptor-induced conformational changes in the SU subunit of the avian sarcoma/leukosis virus A envelope protein: implications for fusion activation.The minor receptor group of human rhinovirus (HRV) includes HRV23 and HRV25, but the presence of a lysine in the VP1 HI loop is not sufficient for receptor bindingHuman rhinovirus type 54 infection via heparan sulfate is less efficient and strictly dependent on low endosomal pH.The High Affinity Binding Site on Plasminogen Activator Inhibitor-1 (PAI-1) for the Low Density Lipoprotein Receptor-related Protein (LRP1) Is Composed of Four Basic Residues.Interaction of Fibrin with the Very Low Density Lipoprotein Receptor: Further Characterization and Localization of the Fibrin-Binding Site.Versatility in ligand recognition by LDL receptor family proteins: advances and frontiers.Mapping the binding region on the low density lipoprotein receptor for blood coagulation factor VIII.Low-density lipoprotein receptor-related protein-1: role in the regulation of vascular integrity.SorLA complement-type repeat domains protect the amyloid precursor protein against processing.High Affinity Binding of the Receptor-associated Protein D1D2 Domains with the Low Density Lipoprotein Receptor-related Protein (LRP1) Involves Bivalent Complex Formation: CRITICAL ROLES OF LYSINES 60 AND 191A mutation in the first ligand-binding repeat of the human very-low-density lipoprotein receptor results in high-affinity binding of the single V1 module to human rhinovirus 2.Discrimination among rhinovirus serotypes for a variant ICAM-1 receptor molecule.Nonneutralizing human rhinovirus serotype 2-specific monoclonal antibody 2G2 attaches to the region that undergoes the most dramatic changes upon release of the viral RNA.Identification of the human rhinovirus serotype 1A binding site on the murine low-density lipoprotein receptor by using human-mouse receptor chimerasReceptors for enterovirus 71.Human rhinovirus subviral a particle binds to lipid membranes over a twofold axis of icosahedral symmetry.Low pH-triggered beta-propeller switch of the low-density lipoprotein receptor assists rhinovirus infection.Molecular modeling, organ culture and reverse genetics for a newly identified human rhinovirus C.Structural basis for ligand capture and release by the endocytic receptor ApoER2.Human rhinovirus type 89 variants use heparan sulfate proteoglycan for cell attachment.Productive entry pathways of human rhinoviruses.New horizons for lipoprotein receptors: communication by β-propellers.Structural insights into recognition of beta2-glycoprotein I by the lipoprotein receptors.Predictive bioinformatic identification of minor receptor group human rhinoviruses.Rhinovirus-stabilizing activity of artificial VLDL-receptor variants defines a new mechanism for virus neutralization by soluble receptors.
P2860
Q24646231-9FA4E311-C885-41B3-AAD8-551A0E9212E4Q24650291-2B835CDE-5BB5-4C83-B47D-3687DBF19B6CQ24673808-47B78007-75C6-424E-A39B-0F0D1AF7C0B8Q24683829-42568856-DAE4-4CDD-B6F6-FA5CFC434F33Q26750146-036AE9E0-AF83-4DFC-8AD3-591F86E88F39Q27347786-F290DE43-745F-4146-936E-2317773B3CD8Q27652596-96E44DDD-D5F5-420B-BFA7-E48AB3753C24Q27653110-C5B50F41-6069-45B2-BECB-B30F2FF3CA7BQ27660292-3CA01802-BBED-40A2-9A9C-79FCB48AB72EQ27664791-C36E971B-3A7C-4D71-9053-5761C6F27AD8Q27675654-2D60305F-5A89-4345-BE4D-E666E9BC9EB0Q28543886-A077F757-FA7C-4E76-B482-B07BCE1932E2Q28854576-29710812-4C10-4645-943B-BC80B7597B2BQ30433192-C1668488-402B-4212-B29E-76B1FD198F69Q30440707-EF170C37-E9DB-442E-924D-FD8F00CD6AFDQ30448472-B5E2A1AB-B882-4734-9E5A-620878ED6400Q33842994-70B29C18-A6A4-478A-AEA0-D7B070330471Q35857392-BE11FB33-391E-4B92-9B2D-564BCB73EEDFQ36442395-A10E0B57-76AE-48E2-94F2-F13A00819A8FQ36758715-980DF214-C37E-4339-8F84-E15A71C2F0B5Q36942847-9792F2F1-FC05-464F-A248-7686E54DC765Q37048482-18367DC0-B779-41E3-BC48-2657CE4B5730Q38185972-08708A3F-043D-4AF5-85A0-3D2B4E9B0908Q38926992-E4E68C68-3A24-4965-A573-1F3D0C92AE5BQ39611483-F0D0C968-5355-4394-A9E9-5298DB9D1E0FQ39798492-29316F62-FDCA-435C-9291-47BB8F9FF7E5Q39960136-8FBBEC66-A78E-4B82-A62A-8796C37E4859Q40334830-5B85B850-249C-4328-B8C0-5B3B25D93157Q40546017-1A4346CD-560A-4094-92DE-C136CB919477Q41188412-27F66C89-3E81-4F67-A9A6-AAF9A0689682Q41610468-4819EF0C-BBAA-4EB5-9F5E-D083298C316BQ41863567-162DBDBF-32A0-4830-B8AB-F2598AB1CC2EQ41894556-E0CFFC72-A00F-46A2-843B-5183CF01BE4CQ41916799-EBDF18AE-8D80-436E-9770-4282944BDC05Q41927626-98943E98-CBCA-4031-8CE0-B624028E2973Q42090065-5E9B72B8-008B-4F9E-86DE-C2A262E9D5EDQ42105665-470E75A9-F6AE-4B3D-8757-6D37E3C49468Q42592414-55D34DFA-A2D1-4F26-B9EB-3F77FE56345BQ43541626-2C6D3894-0C42-48AC-93E8-2AA6DD594D40Q45423416-10070120-2ADF-416D-9B21-B4E88112484B
P2860
X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
X-ray structure of a minor gro ...... its cellular receptor protein.
@en
X-ray structure of a minor gro ...... its cellular receptor protein.
@nl
type
label
X-ray structure of a minor gro ...... its cellular receptor protein.
@en
X-ray structure of a minor gro ...... its cellular receptor protein.
@nl
prefLabel
X-ray structure of a minor gro ...... its cellular receptor protein.
@en
X-ray structure of a minor gro ...... its cellular receptor protein.
@nl
P2093
P2860
P356
P1476
X-ray structure of a minor gro ...... its cellular receptor protein.
@en
P2093
Dieter Blaas
Ignacio Fita
Manuela Reithmayer
Rosita Moser
P2860
P2888
P304
P356
10.1038/NSMB753
P577
2004-04-04T00:00:00Z
P5875
P6179
1042970371