The Membrane Fusion Activity of the Influenza Virus Haemagglutinin Glycoprotein View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1985

AUTHORS

Don C. Wiley , John J. Skehel

ABSTRACT

The haemagglutinin (HA) glycoprotein of influenza virus is active in promoting the fusion of the virus membrane with that of the cell to effect infectious entry into the cell. The HA protein undergoes a conformational change triggered by the low pH found in intracellular vesicles, which produces a fusion active conformation. Biochemical and spectroscopic studies of this transition indicate that a hydrophobic peptide is uncovered. The analysis of mutants with altered pH optimal for fusion illuminate elements of the conformational change. More... »

PAGES

231-239

Book

TITLE

Modern Trends of Colloid Science in Chemistry and Biology

ISBN

978-3-7643-1711-9
978-3-0348-6513-5

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-3-0348-6513-5_11

DOI

http://dx.doi.org/10.1007/978-3-0348-6513-5_11

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1036302116


Indexing Status Check whether this publication has been indexed by Scopus and Web Of Science using the SN Indexing Status Tool
Incoming Citations Browse incoming citations for this publication using opencitations.net

JSON-LD is the canonical representation for SciGraph data.

TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT

[
  {
    "@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json", 
    "about": [
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0601", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Biochemistry and Cell Biology", 
        "type": "DefinedTerm"
      }, 
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/06", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Biological Sciences", 
        "type": "DefinedTerm"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "Harvard University", 
          "id": "https://www.grid.ac/institutes/grid.38142.3c", 
          "name": [
            "Department of Biochemistry & Molecular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA\u00a002138, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Wiley", 
        "givenName": "Don C.", 
        "id": "sg:person.01104357451.72", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01104357451.72"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Harvard University", 
          "id": "https://www.grid.ac/institutes/grid.38142.3c", 
          "name": [
            "Department of Biochemistry & Molecular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA\u00a002138, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Skehel", 
        "givenName": "John J.", 
        "id": "sg:person.0744102055.80", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0744102055.80"
        ], 
        "type": "Person"
      }
    ], 
    "citation": [
      {
        "id": "https://doi.org/10.1016/0042-6822(74)90187-1", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1006631901"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/304076a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1011610967", 
          "https://doi.org/10.1038/304076a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/289366a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1016242659", 
          "https://doi.org/10.1038/289366a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/300658a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1016471617", 
          "https://doi.org/10.1038/300658a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/0042-6822(77)90371-3", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1038868106"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/0042-6822(75)90284-6", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1046990731"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1073/pnas.79.4.968", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1049278670"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1073/pnas.75.6.2737", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1049947717"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1017/s0033583500005072", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1054003074"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1017/s0033583500005072", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1054003074"
        ], 
        "type": "CreativeWork"
      }
    ], 
    "datePublished": "1985", 
    "datePublishedReg": "1985-01-01", 
    "description": "The haemagglutinin (HA) glycoprotein of influenza virus is active in promoting the fusion of the virus membrane with that of the cell to effect infectious entry into the cell. The HA protein undergoes a conformational change triggered by the low pH found in intracellular vesicles, which produces a fusion active conformation. Biochemical and spectroscopic studies of this transition indicate that a hydrophobic peptide is uncovered. The analysis of mutants with altered pH optimal for fusion illuminate elements of the conformational change.", 
    "editor": [
      {
        "familyName": "Eicke", 
        "givenName": "Hans-Friedrich", 
        "type": "Person"
      }
    ], 
    "genre": "chapter", 
    "id": "sg:pub.10.1007/978-3-0348-6513-5_11", 
    "inLanguage": [
      "en"
    ], 
    "isAccessibleForFree": false, 
    "isPartOf": {
      "isbn": [
        "978-3-7643-1711-9", 
        "978-3-0348-6513-5"
      ], 
      "name": "Modern Trends of Colloid Science in Chemistry and Biology", 
      "type": "Book"
    }, 
    "name": "The Membrane Fusion Activity of the Influenza Virus Haemagglutinin Glycoprotein", 
    "pagination": "231-239", 
    "productId": [
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1007/978-3-0348-6513-5_11"
        ]
      }, 
      {
        "name": "readcube_id", 
        "type": "PropertyValue", 
        "value": [
          "acedb8465c882559cc81159bb7fb629607bb0b3b32b50a23846dd9d8dd9d586b"
        ]
      }, 
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1036302116"
        ]
      }
    ], 
    "publisher": {
      "location": "Basel", 
      "name": "Birkh\u00e4user Basel", 
      "type": "Organisation"
    }, 
    "sameAs": [
      "https://doi.org/10.1007/978-3-0348-6513-5_11", 
      "https://app.dimensions.ai/details/publication/pub.1036302116"
    ], 
    "sdDataset": "chapters", 
    "sdDatePublished": "2019-04-16T00:50", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-uberresearch-data-dimensions-target-20181106-alternative/cleanup/v134/2549eaecd7973599484d7c17b260dba0a4ecb94b/merge/v9/a6c9fde33151104705d4d7ff012ea9563521a3ce/jats-lookup/v90/0000000001_0000000264/records_8700_00000265.jsonl", 
    "type": "Chapter", 
    "url": "http://link.springer.com/10.1007/978-3-0348-6513-5_11"
  }
]
 

Download the RDF metadata as:  json-ld nt turtle xml License info

HOW TO GET THIS DATA PROGRAMMATICALLY:

JSON-LD is a popular format for linked data which is fully compatible with JSON.

curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1007/978-3-0348-6513-5_11'

N-Triples is a line-based linked data format ideal for batch operations.

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1007/978-3-0348-6513-5_11'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1007/978-3-0348-6513-5_11'

RDF/XML is a standard XML format for linked data.

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1007/978-3-0348-6513-5_11'


 

This table displays all metadata directly associated to this object as RDF triples.

102 TRIPLES      23 PREDICATES      36 URIs      20 LITERALS      8 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1007/978-3-0348-6513-5_11 schema:about anzsrc-for:06
2 anzsrc-for:0601
3 schema:author N5049efd104da461e80115d4a52f6e9a6
4 schema:citation sg:pub.10.1038/289366a0
5 sg:pub.10.1038/300658a0
6 sg:pub.10.1038/304076a0
7 https://doi.org/10.1016/0042-6822(74)90187-1
8 https://doi.org/10.1016/0042-6822(75)90284-6
9 https://doi.org/10.1016/0042-6822(77)90371-3
10 https://doi.org/10.1017/s0033583500005072
11 https://doi.org/10.1073/pnas.75.6.2737
12 https://doi.org/10.1073/pnas.79.4.968
13 schema:datePublished 1985
14 schema:datePublishedReg 1985-01-01
15 schema:description The haemagglutinin (HA) glycoprotein of influenza virus is active in promoting the fusion of the virus membrane with that of the cell to effect infectious entry into the cell. The HA protein undergoes a conformational change triggered by the low pH found in intracellular vesicles, which produces a fusion active conformation. Biochemical and spectroscopic studies of this transition indicate that a hydrophobic peptide is uncovered. The analysis of mutants with altered pH optimal for fusion illuminate elements of the conformational change.
16 schema:editor Ncfbf4c80e6fa4f6b926b1bba6a8620f9
17 schema:genre chapter
18 schema:inLanguage en
19 schema:isAccessibleForFree false
20 schema:isPartOf Nfc7d832db776414b805b31fc81d6c16b
21 schema:name The Membrane Fusion Activity of the Influenza Virus Haemagglutinin Glycoprotein
22 schema:pagination 231-239
23 schema:productId N1e4ade17d1bc44988d2dbb812d9b91c2
24 N235f07a624d745dc866cbffc70814555
25 Nd96dae3f2cf048a88667c4ef2707ef11
26 schema:publisher N464ef35c982c4ae09df307ab4656f8da
27 schema:sameAs https://app.dimensions.ai/details/publication/pub.1036302116
28 https://doi.org/10.1007/978-3-0348-6513-5_11
29 schema:sdDatePublished 2019-04-16T00:50
30 schema:sdLicense https://scigraph.springernature.com/explorer/license/
31 schema:sdPublisher N5546af5a1d6640feaf4684ace3dfac1a
32 schema:url http://link.springer.com/10.1007/978-3-0348-6513-5_11
33 sgo:license sg:explorer/license/
34 sgo:sdDataset chapters
35 rdf:type schema:Chapter
36 N1e4ade17d1bc44988d2dbb812d9b91c2 schema:name readcube_id
37 schema:value acedb8465c882559cc81159bb7fb629607bb0b3b32b50a23846dd9d8dd9d586b
38 rdf:type schema:PropertyValue
39 N235f07a624d745dc866cbffc70814555 schema:name dimensions_id
40 schema:value pub.1036302116
41 rdf:type schema:PropertyValue
42 N464ef35c982c4ae09df307ab4656f8da schema:location Basel
43 schema:name Birkhäuser Basel
44 rdf:type schema:Organisation
45 N5049efd104da461e80115d4a52f6e9a6 rdf:first sg:person.01104357451.72
46 rdf:rest N82f5327aa1054b0cb0d8f37d319201ae
47 N5546af5a1d6640feaf4684ace3dfac1a schema:name Springer Nature - SN SciGraph project
48 rdf:type schema:Organization
49 N82f5327aa1054b0cb0d8f37d319201ae rdf:first sg:person.0744102055.80
50 rdf:rest rdf:nil
51 Ncfbf4c80e6fa4f6b926b1bba6a8620f9 rdf:first Nf430c2b5a90549c29965a6d8060f324a
52 rdf:rest rdf:nil
53 Nd96dae3f2cf048a88667c4ef2707ef11 schema:name doi
54 schema:value 10.1007/978-3-0348-6513-5_11
55 rdf:type schema:PropertyValue
56 Nf430c2b5a90549c29965a6d8060f324a schema:familyName Eicke
57 schema:givenName Hans-Friedrich
58 rdf:type schema:Person
59 Nfc7d832db776414b805b31fc81d6c16b schema:isbn 978-3-0348-6513-5
60 978-3-7643-1711-9
61 schema:name Modern Trends of Colloid Science in Chemistry and Biology
62 rdf:type schema:Book
63 anzsrc-for:06 schema:inDefinedTermSet anzsrc-for:
64 schema:name Biological Sciences
65 rdf:type schema:DefinedTerm
66 anzsrc-for:0601 schema:inDefinedTermSet anzsrc-for:
67 schema:name Biochemistry and Cell Biology
68 rdf:type schema:DefinedTerm
69 sg:person.01104357451.72 schema:affiliation https://www.grid.ac/institutes/grid.38142.3c
70 schema:familyName Wiley
71 schema:givenName Don C.
72 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01104357451.72
73 rdf:type schema:Person
74 sg:person.0744102055.80 schema:affiliation https://www.grid.ac/institutes/grid.38142.3c
75 schema:familyName Skehel
76 schema:givenName John J.
77 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0744102055.80
78 rdf:type schema:Person
79 sg:pub.10.1038/289366a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1016242659
80 https://doi.org/10.1038/289366a0
81 rdf:type schema:CreativeWork
82 sg:pub.10.1038/300658a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1016471617
83 https://doi.org/10.1038/300658a0
84 rdf:type schema:CreativeWork
85 sg:pub.10.1038/304076a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1011610967
86 https://doi.org/10.1038/304076a0
87 rdf:type schema:CreativeWork
88 https://doi.org/10.1016/0042-6822(74)90187-1 schema:sameAs https://app.dimensions.ai/details/publication/pub.1006631901
89 rdf:type schema:CreativeWork
90 https://doi.org/10.1016/0042-6822(75)90284-6 schema:sameAs https://app.dimensions.ai/details/publication/pub.1046990731
91 rdf:type schema:CreativeWork
92 https://doi.org/10.1016/0042-6822(77)90371-3 schema:sameAs https://app.dimensions.ai/details/publication/pub.1038868106
93 rdf:type schema:CreativeWork
94 https://doi.org/10.1017/s0033583500005072 schema:sameAs https://app.dimensions.ai/details/publication/pub.1054003074
95 rdf:type schema:CreativeWork
96 https://doi.org/10.1073/pnas.75.6.2737 schema:sameAs https://app.dimensions.ai/details/publication/pub.1049947717
97 rdf:type schema:CreativeWork
98 https://doi.org/10.1073/pnas.79.4.968 schema:sameAs https://app.dimensions.ai/details/publication/pub.1049278670
99 rdf:type schema:CreativeWork
100 https://www.grid.ac/institutes/grid.38142.3c schema:alternateName Harvard University
101 schema:name Department of Biochemistry & Molecular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA 02138, USA
102 rdf:type schema:Organization
 




Preview window. Press ESC to close (or click here)


...