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16799046
Source:
http://linkedlifedata.com/resource/pubmed/id/16799046
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Statements in which the resource exists as a subject.
Predicate
Object
rdf:type
pubmed:Citation
lifeskim:mentions
umls-concept:C0003765
,
umls-concept:C0023317
,
umls-concept:C0041485
,
umls-concept:C0729223
,
umls-concept:C1522492
,
umls-concept:C1709915
,
umls-concept:C2003941
pubmed:issue
7
pubmed:dateCreated
2006-6-26
pubmed:abstractText
To identify new mouse models for studying roles of alphaAlpha-crystallin in vivo and to investigate why and how different mutations of the alphaAlpha-crystallin gene lead to dominant or recessive cataracts.
pubmed:grant
http://linkedlifedata.com/resource/pubmed/grant/EY015073
,
http://linkedlifedata.com/resource/pubmed/grant/EY03897
,
http://linkedlifedata.com/resource/pubmed/grant/EY07758
,
http://linkedlifedata.com/resource/pubmed/grant/EY13849
pubmed:language
eng
pubmed:journal
http://linkedlifedata.com/resource/pubmed/journal/7703701
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Actins
,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine
,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins
,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Crystallin A Chain
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0146-0404
pubmed:author
pubmed-author:ChangBoB
,
pubmed-author:ChengCatherineC
,
pubmed-author:CheungDebraD
,
pubmed-author:GongXiaohuaX
,
pubmed-author:HorwitzJosephJ
,
pubmed-author:HuangQinglingQ
,
pubmed-author:LiuHaiquanH
,
pubmed-author:WangMengM
,
pubmed-author:XiaChun-hongCH
pubmed:issnType
Print
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3004-10
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:16799046-Actins
,
pubmed-meshheading:16799046-Animals
,
pubmed-meshheading:16799046-Arginine
,
pubmed-meshheading:16799046-Cataract
,
pubmed-meshheading:16799046-Chromosome Mapping
,
pubmed-meshheading:16799046-Disease Models, Animal
,
pubmed-meshheading:16799046-Electrophoresis, Gel, Two-Dimensional
,
pubmed-meshheading:16799046-Epithelial Cells
,
pubmed-meshheading:16799046-Female
,
pubmed-meshheading:16799046-Genes, Dominant
,
pubmed-meshheading:16799046-Genes, Recessive
,
pubmed-meshheading:16799046-Genetic Linkage
,
pubmed-meshheading:16799046-Green Fluorescent Proteins
,
pubmed-meshheading:16799046-Lens, Crystalline
,
pubmed-meshheading:16799046-Male
,
pubmed-meshheading:16799046-Mice
,
pubmed-meshheading:16799046-Mice, Inbred C3H
,
pubmed-meshheading:16799046-Mice, Inbred C57BL
,
pubmed-meshheading:16799046-Mitochondria
,
pubmed-meshheading:16799046-Phenotype
,
pubmed-meshheading:16799046-Point Mutation
,
pubmed-meshheading:16799046-Tyrosine
,
pubmed-meshheading:16799046-alpha-Crystallin A Chain
pubmed:year
2006
pubmed:articleTitle
Arginine 54 and Tyrosine 118 residues of {alpha}A-crystallin are crucial for lens formation and transparency.
pubmed:affiliation
School of Optometry and Vision Science Program, University of California, Berkeley, Berkeley, California 94720-2020, USA.
pubmed:publicationType
Journal Article
,
Research Support, N.I.H., Extramural