Nipah virus attachment glycoprotein stalk C-terminal region links receptor binding to fusion triggering

scientific article

Nipah virus attachment glycoprotein stalk C-terminal region links receptor binding to fusion triggering is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1128/JVI.02277-14
P932PMC publication ID4300768
P698PubMed publication ID25428863

P50authorAbrrey I MonrealQ54560622
Hector C AguilarQ97566627
Anthony V NicolaQ100513241
P2093author name stringQian Liu
Birgit Bradel-Tretheway
Jonel P Saludes
Xiaonan Lu
P2860cites workAmino acid substitutions in the F-specific domain in the stalk of the newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F proteinQ37596488
Fusion activation through attachment protein stalk domains indicates a conserved core mechanism of paramyxovirus entry into cellsQ37713834
Henipavirus membrane fusion and viral entryQ37994632
Clinical and pathological manifestations of human henipavirus infectionQ37994637
Henipavirus receptor usage and tropismQ38018531
Epidemiology of henipavirus disease in humansQ38023240
A stabilized headless measles virus attachment protein stalk efficiently triggers membrane fusionQ39106872
A quantitative and kinetic fusion protein-triggering assay can discern distinct steps in the nipah virus membrane fusion cascadeQ39697289
Glycoprotein interactions in paramyxovirus fusionQ39900113
N-glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and viral entryQ40287207
Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signalingQ42049782
Domain architecture and oligomerization properties of the paramyxovirus PIV 5 hemagglutinin-neuraminidase (HN) proteinQ43227660
Two key residues in ephrinB3 are critical for its use as an alternative receptor for Nipah virusQ25257200
Nipah Virus InfectionQ27478245
Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeQ27487974
Host cell recognition by the henipaviruses: Crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3Q27651214
Crystal Structure and Carbohydrate Analysis of Nipah Virus Attachment Glycoprotein: a Template for Antiviral and Vaccine DesignQ27652284
Structure of the measles virus hemagglutinin bound to the CD46 receptorQ27658662
Structure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalkQ27672276
Structure of the cleavage-activated prefusion form of the parainfluenza virus 5 fusion proteinQ27673665
Structure and Mutagenesis of the Parainfluenza Virus 5 Hemagglutinin-Neuraminidase Stalk Domain Reveals a Four-Helix Bundle and the Role of the Stalk in Fusion PromotionQ27674994
Mechanisms and functions of Eph and ephrin signallingQ28208291
Mutational analysis of heptad repeats in the membrane-proximal region of Newcastle disease virus HN protein.Q33646121
Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusionQ34301817
Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactoseQ34418848
EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirusQ34432746
Unraveling a three-step spatiotemporal mechanism of triggering of receptor-induced Nipah virus fusion and cell entry.Q35053036
Emerging paramyxoviruses: molecular mechanisms and antiviral strategiesQ35658152
Site occupancy and glycan compositional analysis of two soluble recombinant forms of the attachment glycoprotein of Hendra virus.Q35779475
Structural rearrangements of the central region of the morbillivirus attachment protein stalk domain trigger F protein refolding for membrane fusionQ35956606
Cysteines in the stalk of the nipah virus G glycoprotein are located in a distinct subdomain critical for fusion activationQ36086698
Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggeringQ36300779
N-Glycans on the Nipah virus attachment glycoprotein modulate fusion and viral entry as they protect against antibody neutralizationQ36363882
New insights into the Hendra virus attachment and entry process from structures of the virus G glycoprotein and its complex with Ephrin-B2Q36373573
Interacting Domains of the HN and F Proteins of Newcastle Disease VirusQ36474158
Mechanism for active membrane fusion triggering by morbillivirus attachment proteinQ36506813
Detection of receptor-induced glycoprotein conformational changes on enveloped virions by using confocal micro-Raman spectroscopy.Q36668002
Individual N-glycans added at intervals along the stalk of the Nipah virus G protein prevent fusion but do not block the interaction with the homologous F proteinQ36668013
Residues in the stalk domain of the hendra virus g glycoprotein modulate conformational changes associated with receptor bindingQ36949836
Envelope protein dynamics in paramyxovirus entryQ36994390
A novel receptor-induced activation site in the Nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F)Q37041588
P433issue3
P407language of work or nameEnglishQ1860
P921main subjectNipah virusQ15928531
P304page(s)1838-1850
P577publication date2014-11-26
P1433published inJournal of VirologyQ1251128
P1476titleNipah virus attachment glycoprotein stalk C-terminal region links receptor binding to fusion triggering
P478volume89

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cites work (P2860)
Q38829623A Structurally Unresolved Head Segment of Defined Length Favors Proper Measles Virus Hemagglutinin Tetramerization and Efficient Membrane Fusion Triggering
Q56551553A stochastic assembly model for Nipah virus revealed by super-resolution microscopy
Q89529516Differential Features of Fusion Activation within the Paramyxoviridae
Q94596521Epitope-Based Peptide Vaccine against Glycoprotein G of Nipah Henipavirus Using Immunoinformatics Approaches
Q53690283Formation of high-order oligomers is required for functional bioactivity of an African bat henipavirus surface glycoprotein.
Q93017158Fusogenicity of the Ghana Virus (Henipavirus: Ghanaian bat henipavirus) Fusion Protein is Controlled by the Cytoplasmic Domain of the Attachment Glycoprotein
Q41925118Monomeric ephrinB2 binding induces allosteric changes in Nipah virus G that precede its full activation
Q40949336Morbillivirus and henipavirus attachment protein cytoplasmic domains differently affect protein expression, fusion support and particle assembly
Q35921009Multiple Novel Functions of Henipavirus O-glycans: The First O-glycan Functions Identified in the Paramyxovirus Family
Q38744525Multiple Strategies Reveal a Bidentate Interaction between the Nipah Virus Attachment and Fusion Glycoproteins
Q93010935Nipah and Hendra Virus Glycoproteins Induce Comparable Homologous but Distinct Heterologous Fusion Phenotypes
Q90046587Nipah virus: epidemiology, pathology, immunobiology and advances in diagnosis, vaccine designing and control strategies - a comprehensive review
Q38878292Novel Functions of Hendra Virus G N-Glycans and Comparisons to Nipah Virus
Q64114537Rabies-based vaccine induces potent immune responses against Nipah virus
Q92710888Receptor-mediated cell entry of paramyxoviruses: Mechanisms, and consequences for tropism and pathogenesis
Q39364461Structure and organization of paramyxovirus particles
Q36551612Structure and stabilization of the Hendra virus F glycoprotein in its prefusion form
Q98205399Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation
Q35582400Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry

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