Direct observation of single kinesin molecules moving along microtubules View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1996-04

AUTHORS

Ronald D. Vale, Takashi Funatsu, Daniel W. Pierce, Laura Romberg, Yoshie Harada, Toshio Yanagida

ABSTRACT

KINESIN is a two-headed motor protein that powers organelle transport along microtubules1. Many ATP molecules are hydro-lysed by kinesin for each diffusional encounter with the micro-tubule2,3. Here we report the development of a new assay in which the processive movement of individual fluorescently labelled kinesin molecules along a microtubule can be visualized directly; this observation is achieved by low-background total internal reflection fluorescence microscopy4 in the absence of attachment of the motor to a cargo (for example, an organelle or bead). The average distance travelled after a binding encounter with a microtubule is 600 nm, which reflects a ~ 1% probability of detachment per mechanical cycle. Surprisingly, processive movement could still be observed at salt concentrations as high as 0.3 M NaCl. Truncated kinesin molecules having only a single motor domain do not show detectable processive movement, which is consistent with a model in which kinesin's two force-generating heads operate by a hand-over-hand mechanism. More... »

PAGES

451-453

Journal

TITLE

Nature

ISSUE

6573

VOLUME

380

Related Patents

  • Method Of Determining The Nucleotide Sequence Of Oligonucleotides And Dna Molecules
  • Capturing With Probe, Annealing Primer, Adding Polymerase, Removing Unincorporated Nucleotides; Sonication; Point Mutations
  • Method Of Determining The Nucleotide Sequence Of Oligonucleotides And Dna Molecules
  • Molecular Hopper
  • Multichannel Microfluidic System For Sequencing Preferential Nucleotide Sequences
  • Single Molecule Sequencing Of Captured Nucleic Acids
  • Prna Chimera
  • Polymer Coatings
  • Human Kinesins And Methods Of Producing And Purifying Human Kinesins
  • Polymer Coatings
  • Polymer Coatings
  • Short Cycle Methods For Sequencing Polynucleotides
  • Method Of Determining The Nucleotide Sequence Of Oligonucleotides And Dna Molecules
  • Enzymatic Nucleic Acid Synthesis: Compositions And Methods For Inhibiting Pyrophosphorolysis
  • Method Of Determining The Nucleotide Sequence Of Oligonucleotides And Dna Molecules
  • Methods And Kits For Analyzing Polynucleotide Sequences
  • Fabricated Arrays For Obtaining Genetic Sequence Information; Single Molecules Immobilised Onto The Surface Of A Solid Support, Capable Of Being Resolved By Optical Means
  • Method Of Determining The Nucleotide Sequence Of Oligonucleotides And Dna Molecules
  • Apparatus And Methods For Analyzing Samples
  • Methods Of Localizing Nucleic Acids To Arrays
  • Short Cycle Methods For Sequencing Polynucleotides
  • Methods And Products For Analyzing Polymers
  • Method Of Determining The Nucleotide Sequence Of Oligonucleotides And Dna Molecules
  • Polymerase Chain Reactions; Exonucleases; Microfluidics
  • Enzymatic Nucleic Acid Synthesis: Compositions And Methods For Inhibiting Pyrophosphorolysis
  • Enzymatic Nucleic Acid Synthesis: Compositions And Methods For Inhibiting Pyrophosphorolysis
  • Method Of Determining The Nucleotide Sequence Of Oligonucleotides And Dna Molecules
  • Arrayed Biomolecules And Their Use In Sequencing
  • Test Compounds Are Added To Two Cytoskeletal Components - A Kinesin Motor Protein And A Tubulin Protein That Specifically Bind To Each Other - To Determine Whether The Binding Is Affected By The Test Compound
  • Prna Chimera
  • Method Of Determining The Nucleotide Sequence Of Oligonucleotides And Dna Molecules
  • Short Cycle Methods For Sequencing Polynucleotides
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/380451a0

    DOI

    http://dx.doi.org/10.1038/380451a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1016265800

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/8602245


    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/2008/06", 
            "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
            "name": "Biological Sciences", 
            "type": "DefinedTerm"
          }, 
          {
            "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"
          }, 
          {
            "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
            "name": "Amino Acid Sequence", 
            "type": "DefinedTerm"
          }, 
          {
            "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
            "name": "Animals", 
            "type": "DefinedTerm"
          }, 
          {
            "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
            "name": "Drosophila", 
            "type": "DefinedTerm"
          }, 
          {
            "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
            "name": "Escherichia coli", 
            "type": "DefinedTerm"
          }, 
          {
            "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
            "name": "Humans", 
            "type": "DefinedTerm"
          }, 
          {
            "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
            "name": "Kinesins", 
            "type": "DefinedTerm"
          }, 
          {
            "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
            "name": "Microscopy, Fluorescence", 
            "type": "DefinedTerm"
          }, 
          {
            "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
            "name": "Microtubules", 
            "type": "DefinedTerm"
          }, 
          {
            "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
            "name": "Molecular Sequence Data", 
            "type": "DefinedTerm"
          }, 
          {
            "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
            "name": "Osmolar Concentration", 
            "type": "DefinedTerm"
          }, 
          {
            "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
            "name": "Peptide Fragments", 
            "type": "DefinedTerm"
          }, 
          {
            "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
            "name": "Recombinant Fusion Proteins", 
            "type": "DefinedTerm"
          }
        ], 
        "author": [
          {
            "affiliation": {
              "alternateName": "Department of Pharmacology, University of California, 94143, San Francisco, California, USA", 
              "id": "http://www.grid.ac/institutes/grid.266102.1", 
              "name": [
                "Yanagida BioMotron Project, ERATO, JRDC, Senba-Higashi 2-4-14, 562, Mino, Osaka, Japan", 
                "Howard Hughes Medical Institute, University of California, 94143, San Francisco, California, USA", 
                "Department of Pharmacology, University of California, 94143, San Francisco, California, USA"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Vale", 
            "givenName": "Ronald D.", 
            "id": "sg:person.010253207217.13", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.010253207217.13"
            ], 
            "type": "Person"
          }, 
          {
            "affiliation": {
              "alternateName": "Yanagida BioMotron Project, ERATO, JRDC, Senba-Higashi 2-4-14, 562, Mino, Osaka, Japan", 
              "id": "http://www.grid.ac/institutes/None", 
              "name": [
                "Yanagida BioMotron Project, ERATO, JRDC, Senba-Higashi 2-4-14, 562, Mino, Osaka, Japan"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Funatsu", 
            "givenName": "Takashi", 
            "id": "sg:person.013324034511.96", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.013324034511.96"
            ], 
            "type": "Person"
          }, 
          {
            "affiliation": {
              "alternateName": "Department of Pharmacology, University of California, 94143, San Francisco, California, USA", 
              "id": "http://www.grid.ac/institutes/grid.266102.1", 
              "name": [
                "Howard Hughes Medical Institute, University of California, 94143, San Francisco, California, USA", 
                "Department of Pharmacology, University of California, 94143, San Francisco, California, USA"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Pierce", 
            "givenName": "Daniel W.", 
            "id": "sg:person.01213514720.90", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01213514720.90"
            ], 
            "type": "Person"
          }, 
          {
            "affiliation": {
              "alternateName": "Department of Pharmacology, University of California, 94143, San Francisco, California, USA", 
              "id": "http://www.grid.ac/institutes/grid.266102.1", 
              "name": [
                "Department of Pharmacology, University of California, 94143, San Francisco, California, USA"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Romberg", 
            "givenName": "Laura", 
            "id": "sg:person.01261630120.85", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01261630120.85"
            ], 
            "type": "Person"
          }, 
          {
            "affiliation": {
              "alternateName": "Yanagida BioMotron Project, ERATO, JRDC, Senba-Higashi 2-4-14, 562, Mino, Osaka, Japan", 
              "id": "http://www.grid.ac/institutes/None", 
              "name": [
                "Yanagida BioMotron Project, ERATO, JRDC, Senba-Higashi 2-4-14, 562, Mino, Osaka, Japan"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Harada", 
            "givenName": "Yoshie", 
            "id": "sg:person.016314765171.99", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.016314765171.99"
            ], 
            "type": "Person"
          }, 
          {
            "affiliation": {
              "alternateName": "Department of Biophysical Engineering, Osaka University, 560, Toyonaka, Osaka, Japan", 
              "id": "http://www.grid.ac/institutes/grid.136593.b", 
              "name": [
                "Yanagida BioMotron Project, ERATO, JRDC, Senba-Higashi 2-4-14, 562, Mino, Osaka, Japan", 
                "Department of Biophysical Engineering, Osaka University, 560, Toyonaka, Osaka, Japan"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Yanagida", 
            "givenName": "Toshio", 
            "id": "sg:person.015141357621.93", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.015141357621.93"
            ], 
            "type": "Person"
          }
        ], 
        "citation": [
          {
            "id": "sg:pub.10.1038/373671a0", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1020580541", 
              "https://doi.org/10.1038/373671a0"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/365721a0", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1026078609", 
              "https://doi.org/10.1038/365721a0"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/374555a0", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1006208507", 
              "https://doi.org/10.1038/374555a0"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/348348a0", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1029101081", 
              "https://doi.org/10.1038/348348a0"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/377448a0", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1002964516", 
              "https://doi.org/10.1038/377448a0"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/373718a0", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1042795255", 
              "https://doi.org/10.1038/373718a0"
            ], 
            "type": "CreativeWork"
          }
        ], 
        "datePublished": "1996-04", 
        "datePublishedReg": "1996-04-01", 
        "description": "KINESIN is a two-headed motor protein that powers organelle transport along microtubules1. Many ATP molecules are hydro-lysed by kinesin for each diffusional encounter with the micro-tubule2,3. Here we report the development of a new assay in which the processive movement of individual fluorescently labelled kinesin molecules along a microtubule can be visualized directly; this observation is achieved by low-background total internal reflection fluorescence microscopy4 in the absence of attachment of the motor to a cargo (for example, an organelle or bead). The average distance travelled after a binding encounter with a microtubule is 600 nm, which reflects a ~ 1% probability of detachment per mechanical cycle. Surprisingly, processive movement could still be observed at salt concentrations as high as 0.3 M NaCl. Truncated kinesin molecules having only a single motor domain do not show detectable processive movement, which is consistent with a model in which kinesin's two force-generating heads operate by a hand-over-hand mechanism.", 
        "genre": "article", 
        "id": "sg:pub.10.1038/380451a0", 
        "isAccessibleForFree": true, 
        "isFundedItemOf": [
          {
            "id": "sg:grant.2435305", 
            "type": "MonetaryGrant"
          }
        ], 
        "isPartOf": [
          {
            "id": "sg:journal.1018957", 
            "issn": [
              "0028-0836", 
              "1476-4687"
            ], 
            "name": "Nature", 
            "publisher": "Springer Nature", 
            "type": "Periodical"
          }, 
          {
            "issueNumber": "6573", 
            "type": "PublicationIssue"
          }, 
          {
            "type": "PublicationVolume", 
            "volumeNumber": "380"
          }
        ], 
        "keywords": [
          "absence of attachment", 
          "new assay", 
          "single motor domain", 
          "motor domain", 
          "kinesin molecules", 
          "single kinesin molecules", 
          "assays", 
          "microtubules", 
          "head", 
          "detachment", 
          "encounters", 
          "absence", 
          "protein", 
          "movement", 
          "molecules", 
          "motor proteins", 
          "concentration", 
          "mechanism", 
          "M NaCl", 
          "kinesin", 
          "hand mechanism", 
          "observations", 
          "development", 
          "average distance", 
          "direct observation", 
          "hand", 
          "processive movement", 
          "attachment", 
          "motor", 
          "mechanical cycles", 
          "cycle", 
          "ATP molecules", 
          "cargo", 
          "probability", 
          "model", 
          "NaCl", 
          "transport", 
          "domain", 
          "salt concentration", 
          "micro", 
          "probability of detachment", 
          "microtubules1", 
          "distance", 
          "diffusional encounter", 
          "hydro"
        ], 
        "name": "Direct observation of single kinesin molecules moving along microtubules", 
        "pagination": "451-453", 
        "productId": [
          {
            "name": "dimensions_id", 
            "type": "PropertyValue", 
            "value": [
              "pub.1016265800"
            ]
          }, 
          {
            "name": "doi", 
            "type": "PropertyValue", 
            "value": [
              "10.1038/380451a0"
            ]
          }, 
          {
            "name": "pubmed_id", 
            "type": "PropertyValue", 
            "value": [
              "8602245"
            ]
          }
        ], 
        "sameAs": [
          "https://doi.org/10.1038/380451a0", 
          "https://app.dimensions.ai/details/publication/pub.1016265800"
        ], 
        "sdDataset": "articles", 
        "sdDatePublished": "2022-09-02T15:49", 
        "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
        "sdPublisher": {
          "name": "Springer Nature - SN SciGraph project", 
          "type": "Organization"
        }, 
        "sdSource": "s3://com-springernature-scigraph/baseset/20220902/entities/gbq_results/article/article_278.jsonl", 
        "type": "ScholarlyArticle", 
        "url": "https://doi.org/10.1038/380451a0"
      }
    ]
     

    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.10.1038/380451a0'

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

    curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1038/380451a0'

    Turtle is a human-readable linked data format.

    curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/380451a0'

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

    curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/380451a0'


     

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

    224 TRIPLES      21 PREDICATES      89 URIs      75 LITERALS      19 BLANK NODES

    Subject Predicate Object
    1 sg:pub.10.1038/380451a0 schema:about N042694ed7b3a492cb202c68b0ecc1186
    2 N25efbc49645445cf81411925dc371a24
    3 N3ef58e94002649d9a538e767b087e0fa
    4 N438801918a3443f882cca173a93ee142
    5 N69122b4bdd344db9b344e942ce715567
    6 N801fb241649e4df4b8c44c156ecebfe8
    7 N822cbb1185b047f2816bb949ce73812f
    8 N95a972b1006345068d4cf2f5a688caeb
    9 Nb81a52b109cf49a2a202c86d09c9b0a8
    10 Nc3871b1c42ee4e209a40a9a5d9582b59
    11 Ncc866c7165384e0a82822266a0553b44
    12 Ndb0523a5900640f2813f9aa65ccc5e19
    13 anzsrc-for:06
    14 anzsrc-for:0601
    15 schema:author N7b6e59a62ffc42e181247a8873d2b233
    16 schema:citation sg:pub.10.1038/348348a0
    17 sg:pub.10.1038/365721a0
    18 sg:pub.10.1038/373671a0
    19 sg:pub.10.1038/373718a0
    20 sg:pub.10.1038/374555a0
    21 sg:pub.10.1038/377448a0
    22 schema:datePublished 1996-04
    23 schema:datePublishedReg 1996-04-01
    24 schema:description KINESIN is a two-headed motor protein that powers organelle transport along microtubules1. Many ATP molecules are hydro-lysed by kinesin for each diffusional encounter with the micro-tubule2,3. Here we report the development of a new assay in which the processive movement of individual fluorescently labelled kinesin molecules along a microtubule can be visualized directly; this observation is achieved by low-background total internal reflection fluorescence microscopy4 in the absence of attachment of the motor to a cargo (for example, an organelle or bead). The average distance travelled after a binding encounter with a microtubule is 600 nm, which reflects a ~ 1% probability of detachment per mechanical cycle. Surprisingly, processive movement could still be observed at salt concentrations as high as 0.3 M NaCl. Truncated kinesin molecules having only a single motor domain do not show detectable processive movement, which is consistent with a model in which kinesin's two force-generating heads operate by a hand-over-hand mechanism.
    25 schema:genre article
    26 schema:isAccessibleForFree true
    27 schema:isPartOf N285355d93ddf459e9a249846a915a7c3
    28 Ned792ed09c3b441982952e60885e1dbe
    29 sg:journal.1018957
    30 schema:keywords ATP molecules
    31 M NaCl
    32 NaCl
    33 absence
    34 absence of attachment
    35 assays
    36 attachment
    37 average distance
    38 cargo
    39 concentration
    40 cycle
    41 detachment
    42 development
    43 diffusional encounter
    44 direct observation
    45 distance
    46 domain
    47 encounters
    48 hand
    49 hand mechanism
    50 head
    51 hydro
    52 kinesin
    53 kinesin molecules
    54 mechanical cycles
    55 mechanism
    56 micro
    57 microtubules
    58 microtubules1
    59 model
    60 molecules
    61 motor
    62 motor domain
    63 motor proteins
    64 movement
    65 new assay
    66 observations
    67 probability
    68 probability of detachment
    69 processive movement
    70 protein
    71 salt concentration
    72 single kinesin molecules
    73 single motor domain
    74 transport
    75 schema:name Direct observation of single kinesin molecules moving along microtubules
    76 schema:pagination 451-453
    77 schema:productId Nd113d56d152043c690599c277f534a49
    78 Nf579d0942edc430591456d91efdcef71
    79 Nf5996d46e6a9488981a1e9fd0033c57d
    80 schema:sameAs https://app.dimensions.ai/details/publication/pub.1016265800
    81 https://doi.org/10.1038/380451a0
    82 schema:sdDatePublished 2022-09-02T15:49
    83 schema:sdLicense https://scigraph.springernature.com/explorer/license/
    84 schema:sdPublisher N4be71a842c1c41b9a34ad3b68472c0ad
    85 schema:url https://doi.org/10.1038/380451a0
    86 sgo:license sg:explorer/license/
    87 sgo:sdDataset articles
    88 rdf:type schema:ScholarlyArticle
    89 N042694ed7b3a492cb202c68b0ecc1186 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
    90 schema:name Molecular Sequence Data
    91 rdf:type schema:DefinedTerm
    92 N0d6228dffb6542c4b4b069f6e8103515 rdf:first sg:person.015141357621.93
    93 rdf:rest rdf:nil
    94 N25efbc49645445cf81411925dc371a24 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
    95 schema:name Humans
    96 rdf:type schema:DefinedTerm
    97 N285355d93ddf459e9a249846a915a7c3 schema:volumeNumber 380
    98 rdf:type schema:PublicationVolume
    99 N3ef58e94002649d9a538e767b087e0fa schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
    100 schema:name Drosophila
    101 rdf:type schema:DefinedTerm
    102 N3f0df6c854a048c0a62e6c68e563e6d1 rdf:first sg:person.01261630120.85
    103 rdf:rest N5c1a4e2c31024891b1f202783f255104
    104 N438801918a3443f882cca173a93ee142 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
    105 schema:name Recombinant Fusion Proteins
    106 rdf:type schema:DefinedTerm
    107 N4be71a842c1c41b9a34ad3b68472c0ad schema:name Springer Nature - SN SciGraph project
    108 rdf:type schema:Organization
    109 N5c1a4e2c31024891b1f202783f255104 rdf:first sg:person.016314765171.99
    110 rdf:rest N0d6228dffb6542c4b4b069f6e8103515
    111 N69122b4bdd344db9b344e942ce715567 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
    112 schema:name Microscopy, Fluorescence
    113 rdf:type schema:DefinedTerm
    114 N7b6e59a62ffc42e181247a8873d2b233 rdf:first sg:person.010253207217.13
    115 rdf:rest Nbb888a2098fd492891445c5f84fb07d1
    116 N7fd9cd67c2be46c7844f018aa73cddf4 rdf:first sg:person.01213514720.90
    117 rdf:rest N3f0df6c854a048c0a62e6c68e563e6d1
    118 N801fb241649e4df4b8c44c156ecebfe8 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
    119 schema:name Kinesins
    120 rdf:type schema:DefinedTerm
    121 N822cbb1185b047f2816bb949ce73812f schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
    122 schema:name Escherichia coli
    123 rdf:type schema:DefinedTerm
    124 N95a972b1006345068d4cf2f5a688caeb schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
    125 schema:name Microtubules
    126 rdf:type schema:DefinedTerm
    127 Nb81a52b109cf49a2a202c86d09c9b0a8 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
    128 schema:name Peptide Fragments
    129 rdf:type schema:DefinedTerm
    130 Nbb888a2098fd492891445c5f84fb07d1 rdf:first sg:person.013324034511.96
    131 rdf:rest N7fd9cd67c2be46c7844f018aa73cddf4
    132 Nc3871b1c42ee4e209a40a9a5d9582b59 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
    133 schema:name Osmolar Concentration
    134 rdf:type schema:DefinedTerm
    135 Ncc866c7165384e0a82822266a0553b44 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
    136 schema:name Amino Acid Sequence
    137 rdf:type schema:DefinedTerm
    138 Nd113d56d152043c690599c277f534a49 schema:name dimensions_id
    139 schema:value pub.1016265800
    140 rdf:type schema:PropertyValue
    141 Ndb0523a5900640f2813f9aa65ccc5e19 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
    142 schema:name Animals
    143 rdf:type schema:DefinedTerm
    144 Ned792ed09c3b441982952e60885e1dbe schema:issueNumber 6573
    145 rdf:type schema:PublicationIssue
    146 Nf579d0942edc430591456d91efdcef71 schema:name doi
    147 schema:value 10.1038/380451a0
    148 rdf:type schema:PropertyValue
    149 Nf5996d46e6a9488981a1e9fd0033c57d schema:name pubmed_id
    150 schema:value 8602245
    151 rdf:type schema:PropertyValue
    152 anzsrc-for:06 schema:inDefinedTermSet anzsrc-for:
    153 schema:name Biological Sciences
    154 rdf:type schema:DefinedTerm
    155 anzsrc-for:0601 schema:inDefinedTermSet anzsrc-for:
    156 schema:name Biochemistry and Cell Biology
    157 rdf:type schema:DefinedTerm
    158 sg:grant.2435305 http://pending.schema.org/fundedItem sg:pub.10.1038/380451a0
    159 rdf:type schema:MonetaryGrant
    160 sg:journal.1018957 schema:issn 0028-0836
    161 1476-4687
    162 schema:name Nature
    163 schema:publisher Springer Nature
    164 rdf:type schema:Periodical
    165 sg:person.010253207217.13 schema:affiliation grid-institutes:grid.266102.1
    166 schema:familyName Vale
    167 schema:givenName Ronald D.
    168 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.010253207217.13
    169 rdf:type schema:Person
    170 sg:person.01213514720.90 schema:affiliation grid-institutes:grid.266102.1
    171 schema:familyName Pierce
    172 schema:givenName Daniel W.
    173 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01213514720.90
    174 rdf:type schema:Person
    175 sg:person.01261630120.85 schema:affiliation grid-institutes:grid.266102.1
    176 schema:familyName Romberg
    177 schema:givenName Laura
    178 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01261630120.85
    179 rdf:type schema:Person
    180 sg:person.013324034511.96 schema:affiliation grid-institutes:None
    181 schema:familyName Funatsu
    182 schema:givenName Takashi
    183 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.013324034511.96
    184 rdf:type schema:Person
    185 sg:person.015141357621.93 schema:affiliation grid-institutes:grid.136593.b
    186 schema:familyName Yanagida
    187 schema:givenName Toshio
    188 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.015141357621.93
    189 rdf:type schema:Person
    190 sg:person.016314765171.99 schema:affiliation grid-institutes:None
    191 schema:familyName Harada
    192 schema:givenName Yoshie
    193 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.016314765171.99
    194 rdf:type schema:Person
    195 sg:pub.10.1038/348348a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1029101081
    196 https://doi.org/10.1038/348348a0
    197 rdf:type schema:CreativeWork
    198 sg:pub.10.1038/365721a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1026078609
    199 https://doi.org/10.1038/365721a0
    200 rdf:type schema:CreativeWork
    201 sg:pub.10.1038/373671a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1020580541
    202 https://doi.org/10.1038/373671a0
    203 rdf:type schema:CreativeWork
    204 sg:pub.10.1038/373718a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1042795255
    205 https://doi.org/10.1038/373718a0
    206 rdf:type schema:CreativeWork
    207 sg:pub.10.1038/374555a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1006208507
    208 https://doi.org/10.1038/374555a0
    209 rdf:type schema:CreativeWork
    210 sg:pub.10.1038/377448a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1002964516
    211 https://doi.org/10.1038/377448a0
    212 rdf:type schema:CreativeWork
    213 grid-institutes:None schema:alternateName Yanagida BioMotron Project, ERATO, JRDC, Senba-Higashi 2-4-14, 562, Mino, Osaka, Japan
    214 schema:name Yanagida BioMotron Project, ERATO, JRDC, Senba-Higashi 2-4-14, 562, Mino, Osaka, Japan
    215 rdf:type schema:Organization
    216 grid-institutes:grid.136593.b schema:alternateName Department of Biophysical Engineering, Osaka University, 560, Toyonaka, Osaka, Japan
    217 schema:name Department of Biophysical Engineering, Osaka University, 560, Toyonaka, Osaka, Japan
    218 Yanagida BioMotron Project, ERATO, JRDC, Senba-Higashi 2-4-14, 562, Mino, Osaka, Japan
    219 rdf:type schema:Organization
    220 grid-institutes:grid.266102.1 schema:alternateName Department of Pharmacology, University of California, 94143, San Francisco, California, USA
    221 schema:name Department of Pharmacology, University of California, 94143, San Francisco, California, USA
    222 Howard Hughes Medical Institute, University of California, 94143, San Francisco, California, USA
    223 Yanagida BioMotron Project, ERATO, JRDC, Senba-Higashi 2-4-14, 562, Mino, Osaka, Japan
    224 rdf:type schema:Organization
     




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


    ...