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Reconstruction of ancestral metabolic enzymes reveals molecular mechanisms underlying evolutionary innovation through gene duplicationThe sequence of human betaB1-crystallin cDNA allows mass spectrometric detection of betaB1 protein missing portions of its N-terminal extensionMolecular structure of the human muscle-specific enolase gene (ENO3)Argininosuccinate lyase deficiencyExpression of the murine alpha B-crystallin gene is not restricted to the lensGene sharing by delta-crystallin and argininosuccinate lyaseHuman argininosuccinate lyase: a structural basis for intragenic complementationEvolution of antifreeze glycoprotein gene from a trypsinogen gene in Antarctic notothenioid fishFunctional annotation by identification of local surface similarities: a novel tool for structural genomicsStructure analysis of Entamoeba histolytica enolaseThe intracellular location of yeast heat-shock protein 26 varies with metabolism.CREB-binding protein/p300 co-activation of crystallin gene expressionIdentification of His141 in the active site of Bacillus subtilis adenylosuccinate lyase by affinity labeling with 6-(4-bromo-2,3-dioxobutyl)thioadenosine 5'-monophosphatePitx3 controls multiple aspects of lens developmentPhysical Features of Intracellular Proteins that Moonlight on the Cell SurfacePurification, cloning, and characterization of a profibrinolytic plasminogen-binding protein, TIP49aStructure of the rat argininosuccinate lyase gene: close similarity to chicken delta-crystallin genesAntagonistic action of Six3 and Prox1 at the gamma-crystallin promoterThe housekeeping gene xanthine oxidoreductase is necessary for milk fat droplet enveloping and secretion: gene sharing in the lactating mammary glandA role for lengsin, a recruited enzyme, in terminal differentiation in the vertebrate lensTau-crystallin/alpha-enolase: one gene encodes both an enzyme and a lens structural proteinFunctions of crystallins in and out of lens: roles in elongated and post-mitotic cellsWhy study moonlighting proteins?Moonlighting is mainstream: paradigm adjustment required.Developmental regulation of hypomethylation of delta-crystallin genes in chicken embryo lens cells.Life Music: The Sonification of ProteinsUbiquitous lens alpha-, beta-, and gamma-crystallins accumulate in anuran cornea as corneal crystallins.Puzzle of crystallin diversity in eye lenses.Duck lens epsilon-crystallin and lactate dehydrogenase B4 are identical: a single-copy gene product with two distinct functions.Expression and functional characteristics of calpain 3 isoforms generated through tissue-specific transcriptional and posttranscriptional eventsEvidence for neutral and selective processes in the recruitment of enzyme-crystallins in avian lensesAlphaB-crystallin: a Golgi-associated membrane protein in the developing ocular lensMetabolism of ethanol and carcinogens by glutathione transferasesJ3-crystallin of the jellyfish lens: similarity to saposinsZeta-crystallin versus other members of the alcohol dehydrogenase super-family. Variability as a functional characteristic.The twelfth Frederick H. Verhoeff Lecture: gene sharing in the visual system.Ultraviolet radiation and the eye: an epidemiologic study.Enzymes on microbial pathogens and Trichomonas vaginalis: molecular mimicry and functional diversity.A variety of DNA-binding and multimeric proteins contain the histone fold motif.Structural similarity of a developmentally regulated bacterial spore coat protein to beta gamma-crystallins of the vertebrate eye lens.
P2860
Q21145729-132584D5-4824-4997-AEB8-AB9DF6CCE4B0Q24310387-A01DD24C-0C7E-4A24-B9E2-E6C4CB5D7629Q24529549-7E4C36EF-ED60-4534-94EB-D4DAD0482967Q24601202-78AADAD3-7A6E-4D3D-B62E-AAFE2F891D0BQ24633848-DAC751B1-FB76-42D3-9D19-C19AA2CE36D8Q24650635-43030AD4-8424-40C6-9CB3-E7D284E4C6F5Q24653392-8DF91482-BDEE-4E8E-8CA4-835735A59B49Q24685502-B178FF78-49EA-4EC7-93F5-8B118ECD1078Q24815200-9FF14CB6-47F3-43B4-AA8B-41BB818847D3Q27670521-2B41BE15-A3F6-4B55-9AB0-0893C0ADDD63Q27940352-38C76EE4-7D4D-491C-9E14-DBB6B706BE03Q28214240-ED6D7170-19B4-45A4-85ED-13D8AFBB68A9Q28488981-E1616717-FC53-4818-B936-B510051A4FFFQ28508017-EB4FB21F-CBF5-42DC-A881-4BDF42E47049Q28545748-9BAB9A09-1DC3-4A28-9D31-AD24083284AFQ28578865-AC70DA44-3E79-4432-AA3F-C987288F7F12Q28580740-CEB0EFDA-ED45-4BC5-85E7-AC9BF38696E3Q28587045-5239D932-1B2C-4F20-86C6-22B666BB32DFQ28587308-24638835-5E87-43E6-8518-EB7FFF0A58A0Q28593940-B4DDE936-278A-4D66-A191-CB29D38772D1Q28636672-8D9CC9A3-8707-4A30-A5B4-F267867502BAQ28655525-F461EEFC-649B-4EA6-9DBD-4E326CCD38A0Q30376394-1F5C09BA-EE37-41E9-9DA1-FBCDE5AAEB8AQ30417976-185867A8-9C13-413A-AEC3-52E5E6FF1704Q30450394-0EE80916-4628-4C39-A205-19AB0A474D94Q30474109-4C540E73-2DF1-436A-8349-A367FA7C99E1Q33282517-2A85B221-F2B3-4F4C-A0E4-4894C30A2274Q33367343-DBE9ECF9-1AB3-47BA-9313-10692386C7E8Q33650579-2905880F-E370-451B-9411-B9C8CBD8F36FQ33651766-E1A1470D-1D36-43F5-8724-4E2DCEFA6897Q33747549-0328449A-0C61-4474-8FE3-444D957AA258Q33856414-D5AB2D3D-BC48-4F28-8070-AC029497C0BCQ33861742-9E183D7C-1C92-4AD1-9025-39BE89DE5163Q33947698-8CBA57EF-9096-4A97-9C26-4324D537B7FFQ34061937-646835C1-36D5-4FCE-A415-2041B0175133Q34163946-B1A67AA3-E2B4-45BC-A587-0CD7E83B6A06Q34164362-D058BCB2-D37A-4F7E-89DD-0C686C571FCDQ34291286-C0FB871C-270B-464D-933D-85074B5CDA77Q34303525-8A09A821-F685-4AF0-99F6-8B03C8072A6AQ34341216-D0CC1740-7578-4523-AB58-6D06847B7FAC
P2860
description
1987 nî lūn-bûn
@nan
1987 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
Recruitment of enzymes as lens structural proteins
@ast
Recruitment of enzymes as lens structural proteins
@en
Recruitment of enzymes as lens structural proteins.
@nl
type
label
Recruitment of enzymes as lens structural proteins
@ast
Recruitment of enzymes as lens structural proteins
@en
Recruitment of enzymes as lens structural proteins.
@nl
altLabel
Recruitment of enzymes as lens structural proteins.
@ast
Recruitment of enzymes as lens structural proteins.
@en
prefLabel
Recruitment of enzymes as lens structural proteins
@ast
Recruitment of enzymes as lens structural proteins
@en
Recruitment of enzymes as lens structural proteins.
@nl
P2093
P356
P1433
P1476
Recruitment of enzymes as lens structural proteins
@en
Recruitment of enzymes as lens structural proteins.
@en
P2093
J Piatigorsky
Piatigorsky J
P304
P356
10.1126/SCIENCE.3589669
P407
P577
1987-06-01T00:00:00Z
1987-06-19T00:00:00Z