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rdf:type |
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lifeskim:mentions |
umls-concept:C0032521,
umls-concept:C0033684,
umls-concept:C0185023,
umls-concept:C0205460,
umls-concept:C0237497,
umls-concept:C0597198,
umls-concept:C1314972,
umls-concept:C1883254,
umls-concept:C1947904,
umls-concept:C1999228,
umls-concept:C2825781
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pubmed:issue |
3
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pubmed:dateCreated |
2005-3-30
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pubmed:abstractText |
Chemical synthesis in combination with precision polymer modification allows the systematic exploration of the effect of protein properties, such as charge and hydrodynamic radius, on potency using defined, homogeneous conjugates. A series of polymer-modified synthetic erythropoiesis proteins were constructed that had a polypeptide chain similar to the amino acid sequence of human erythropoietin but differed significantly in the number and type of attached polymers. The analogs differed in charge from +5 to -26 at neutral pH and varied in molecular weight from 30 to 54 kDa. All were active in an in vitro cell proliferation assay. However, in vivo potency was found to be strongly dependent on overall charge and size. The trends observed in this study may serve as starting points for the construction of more potent synthetic EPO analogs in the future.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1074-5521
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pubmed:author |
pubmed-author:AdamsonJohn WJW,
pubmed-author:BeilanHal SHS,
pubmed-author:BozziniCarlos ECE,
pubmed-author:BradburneJames AJA,
pubmed-author:CagleE NeilEN,
pubmed-author:CarnevaliMaiaM,
pubmed-author:ChenShiah-YunSY,
pubmed-author:CressmanSonyaS,
pubmed-author:FlipD JDJ,
pubmed-author:GueriguianVincentV,
pubmed-author:KentStephen B HSB,
pubmed-author:KeoghPeter JPJ,
pubmed-author:KochendoerferGerd GGG,
pubmed-author:KungAdaA,
pubmed-author:LowDonald WDW,
pubmed-author:PorterHeatherH,
pubmed-author:SavatskiLauraL,
pubmed-author:ShaoHaiyanH,
pubmed-author:StrattonStephen MSM,
pubmed-author:WiedekeM ConMC
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
371-83
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pubmed:meshHeading |
pubmed-meshheading:15797221-Amino Acid Sequence,
pubmed-meshheading:15797221-Animals,
pubmed-meshheading:15797221-Binding Sites,
pubmed-meshheading:15797221-Cell Proliferation,
pubmed-meshheading:15797221-Dose-Response Relationship, Drug,
pubmed-meshheading:15797221-Erythropoiesis,
pubmed-meshheading:15797221-Erythropoietin,
pubmed-meshheading:15797221-Humans,
pubmed-meshheading:15797221-Macaca fascicularis,
pubmed-meshheading:15797221-Mice,
pubmed-meshheading:15797221-Molecular Sequence Data,
pubmed-meshheading:15797221-Polymers,
pubmed-meshheading:15797221-Proteins,
pubmed-meshheading:15797221-Rats
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pubmed:year |
2005
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pubmed:articleTitle |
Synthetic erythropoietic proteins: tuning biological performance by site-specific polymer attachment.
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pubmed:affiliation |
Gryphon Therapeutics, 600 Gateway Boulevard, South San Francisco, California 94080, USA.
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pubmed:publicationType |
Journal Article
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