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rdf:type |
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lifeskim:mentions |
umls-concept:C0001175,
umls-concept:C0007452,
umls-concept:C0007634,
umls-concept:C0019704,
umls-concept:C0026138,
umls-concept:C0035647,
umls-concept:C0199176,
umls-concept:C0205349,
umls-concept:C0220806,
umls-concept:C0332206,
umls-concept:C0449435,
umls-concept:C0597357,
umls-concept:C1332714
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pubmed:issue |
5
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pubmed:dateCreated |
1996-6-14
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pubmed:abstractText |
The chemical transformation of synthetic combinatorial libraries to increase the diversity of compounds of medicinal interest was reported recently. Chemical modification of natural products represents a complementary approach to accomplish this aim. Modification of lysines by aromatic acid anhydrides, preferentially by 3-hydroxyphthalic and trimellitic anhydrides and trimellitic anhydride chloride, converted commonly available proteins (human and bovine serum albumin and casein) into potent inhibitors of (i) binding between the HIV-1 gp 120 envelope glycoprotein and the CD4 cell receptor, probably owing to their binding to CD4, and (ii) infection by HIV-1. Modified bovine milk proteins are also potent HIV-1 inhibitors and may have potential for anti-HIV-1 prophylaxis.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Anhydrides,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD4,
http://linkedlifedata.com/resource/pubmed/chemical/Antiviral Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Milk Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine
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pubmed:status |
MEDLINE
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pubmed:issn |
0952-3499
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
304-16
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8619951-Anhydrides,
pubmed-meshheading:8619951-Animals,
pubmed-meshheading:8619951-Antibodies, Monoclonal,
pubmed-meshheading:8619951-Antigens, CD4,
pubmed-meshheading:8619951-Antiviral Agents,
pubmed-meshheading:8619951-Arginine,
pubmed-meshheading:8619951-CD4-Positive T-Lymphocytes,
pubmed-meshheading:8619951-Cattle,
pubmed-meshheading:8619951-Female,
pubmed-meshheading:8619951-HIV,
pubmed-meshheading:8619951-Humans,
pubmed-meshheading:8619951-Lysine,
pubmed-meshheading:8619951-Milk Proteins,
pubmed-meshheading:8619951-Models, Molecular,
pubmed-meshheading:8619951-Molecular Structure,
pubmed-meshheading:8619951-Protein Conformation,
pubmed-meshheading:8619951-Serum Albumin, Bovine,
pubmed-meshheading:8619951-Structure-Activity Relationship
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pubmed:articleTitle |
Blocking of CD4 cell receptors for the human immunodeficiency virus type 1 (HIV-1) by chemically modified bovine milk proteins: potential for AIDS prophylaxis.
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pubmed:affiliation |
Laboratory of Biochemical Virology, Lindsley F. Kimball Research Institute of the New York Blood Center, New York 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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