Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
IMMUNOCHEMICAL ANALYSIS OF THE GP120 SURFACE GLYCOPROTEIN OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 - PROBING THE STRUCTURE OF THE C4-DOMAIN AND V4-DOMAIN AND THE INTERACTION OF THE C4-DOMAIN WITH THE V3-LOOP
Autore:
MOORE JP; THALI M; JAMESON BA; VIGNAUX F; LEWIS GK; POON SW; CHARLES M; FUNG MS; SUN B; DURDA PJ; AKERBLOM L; WAHREN B; HO DD; SATTENTAU QJ; SODOROSKI J;
Indirizzi:
NYU,SCH MED,AARON DIAMOND AIDS RES CTR NEW YORK NY 10016 HARVARD UNIV,SCH MED,DANA FARBER CANC INST,DIV HUMAN RETROVIROL BOSTON MA 02115 JEFFERSON CANC INST PHILADELPHIA PA 19107 CTR IMMUNOL MARSEILLE LUMINY F-13288 MARSEILLE FRANCE UNIV MARYLAND,SCH MED BALTIMORE MD 21201 TANOX BIOSYST INC HOUSTON TX 77025 GENZYME CORP CAMBRIDGE MA 02139 BIOMED CTR S-75123 UPPSALA SWEDEN KAROLINSKA INST,NATL BACTERIOL LAB S-10521 STOCKHOLM SWEDEN
Titolo Testata:
Journal of virology
fascicolo: 8, volume: 67, anno: 1993,
pagine: 4785 - 4796
SICI:
0022-538X(1993)67:8<4785:IAOTGS>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
NEUTRALIZING MONOCLONAL-ANTIBODIES; CD4 BINDING-SITE; ENVELOPE GLYCOPROTEIN; RECEPTOR-BINDING; AMINO-ACIDS; SOLUBLE CD4; HIV-1; REGION; EPITOPE; DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
J.P. Moore et al., "IMMUNOCHEMICAL ANALYSIS OF THE GP120 SURFACE GLYCOPROTEIN OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 - PROBING THE STRUCTURE OF THE C4-DOMAIN AND V4-DOMAIN AND THE INTERACTION OF THE C4-DOMAIN WITH THE V3-LOOP", Journal of virology, 67(8), 1993, pp. 4785-4796

Abstract

We have probed the structure of the C4 and V3 domains of human immunodeficiency virus type 1 gp120 by immunochemical techniques. Monoclonalantibodies (MAbs) recognizing an exposed gp120 sequence, (E/K)VGKAMYAPP, in C4 were differentially sensitive to denaturation of gp120, implying a conformational component to some of the epitopes. The MAbs recognizing conformation-sensitive C4 structures failed to bind to a gp120mutant with an alteration in the sequence of the V3 loop, and their binding to gp120 was inhibited by both V3 and C4 MAbs. This implies an interaction between the V3 and C4 regions of gp120, which is supportedby the observation that the binding of some MAbs to the V3 loop was often enhanced by amino acid changes in and around the C4 region.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 05:31:08