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15971201
Source:
http://linkedlifedata.com/resource/pubmed/id/15971201
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55
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Statements in which the resource exists as a subject.
Predicate
Object
rdf:type
pubmed:Citation
lifeskim:mentions
umls-concept:C0031715
,
umls-concept:C0033774
,
umls-concept:C0077678
,
umls-concept:C0678594
,
umls-concept:C1514562
,
umls-concept:C1880389
,
umls-concept:C1883204
,
umls-concept:C1883221
pubmed:issue
3
pubmed:dateCreated
2005-7-18
pubmed:databankReference
http://linkedlifedata.com/resource/pubmed/xref/PDB/1YIU
pubmed:language
eng
pubmed:journal
http://linkedlifedata.com/resource/pubmed/journal/8700181
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Serine
,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine
,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1097-0134
pubmed:author
pubmed-author:MaciasMaria JMJ
,
pubmed-author:Martin-MalpartidaPauP
,
pubmed-author:MoralesBegoñaB
,
pubmed-author:RoyoMiriamM
,
pubmed-author:ShawAlison ZAZ
,
pubmed-author:YraolaFrancescF
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
60
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
558-60
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:15971201-Amino Acid Motifs
,
pubmed-meshheading:15971201-Amino Acid Sequence
,
pubmed-meshheading:15971201-Animals
,
pubmed-meshheading:15971201-Binding Sites
,
pubmed-meshheading:15971201-Biophysics
,
pubmed-meshheading:15971201-Magnetic Resonance Spectroscopy
,
pubmed-meshheading:15971201-Mice
,
pubmed-meshheading:15971201-Molecular Sequence Data
,
pubmed-meshheading:15971201-Phosphorylation
,
pubmed-meshheading:15971201-Protein Binding
,
pubmed-meshheading:15971201-Protein Folding
,
pubmed-meshheading:15971201-Protein Structure, Tertiary
,
pubmed-meshheading:15971201-Proteomics
,
pubmed-meshheading:15971201-Serine
,
pubmed-meshheading:15971201-Threonine
,
pubmed-meshheading:15971201-Ubiquitin-Protein Ligases
pubmed:year
2005
pubmed:articleTitle
Phosphorylation of either Ser16 or Thr30 does not disrupt the structure of the Itch E3 ubiquitin ligase third WW domain.
pubmed:affiliation
ICREA and the Biomedical Research Institute of Barcelona, Barcelona Science Park, Barcelona, Spain.
pubmed:publicationType
Journal Article
,
Research Support, Non-U.S. Gov't