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Titolo:
Structure-function analysis of the ADAM family of disintegrin-like and metalloproteinase-containing proteins (review)
Autore:
Stone, AL; Kroeger, M; Sang, QXA;
Indirizzi:
Florida State Univ, Dept Chem, Tallahassee, FL 32306 USA Florida State Univ Tallahassee FL USA 32306 em, Tallahassee, FL 32306 USA Florida State Univ, Inst Mol Biophys, Tallahassee, FL 32306 USA Florida State Univ Tallahassee FL USA 32306 ys, Tallahassee, FL 32306 USA
Titolo Testata:
JOURNAL OF PROTEIN CHEMISTRY
fascicolo: 4, volume: 18, anno: 1999,
pagine: 447 - 465
SICI:
0277-8033(199905)18:4<447:SAOTAF>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
NECROSIS-FACTOR-ALPHA; SPERM-EGG FUSION; COMPUTATIONAL SEQUENCE-ANALYSIS; SNAKE-VENOM METALLOPROTEINASES; RECOMBINANT RABBIT FERTILIN; MOLECULAR-CLONING; MATRIX METALLOPROTEINASES; CYSTEINE-RICH; PLASMA-MEMBRANE; SURFACE PROTEIN;
Keywords:
metzincin; metalloproteinase/disintegrin/cysteine-rich (MDC); computational sequence analysis; physical data calculation; homology comparison;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
93
Recensione:
Indirizzi per estratti:
Indirizzo: Sang, QXA Florida State Univ, Dept Chem, 203 Dittmer Lab Chem Bldg, Tallahassee, FL 32306 USA Florida State Univ 203 Dittmer Lab Chem Bldg Tallahassee FL USA 32306
Citazione:
A.L. Stone et al., "Structure-function analysis of the ADAM family of disintegrin-like and metalloproteinase-containing proteins (review)", J PROTEIN C, 18(4), 1999, pp. 447-465

Abstract

The ADAMs belong to a disintegrin-like and metalloproteinase-containing protein family that are zinc-dependent metalloproteinases. These proteins share all or some of the following domain structure: a signal peptide, a propeptide, a metalloproteinase, a disintegrin, a cysteine-rich, and an epidermal growth factor (EGF)-like domains, a transmembrane region, and a cytoplasmic tail. ADAMs are widely distributed in many organs, tissues, and cells, such as brain, testis, epididymis, ovary, breast, placenta, liver, heart, lung, bone, and muscle. These proteins are capable of four potential functions: proteolysis, adhesion, fusion, and intracellular signaling. Because the number of ADAM genes has grown rapidly and the biological functions of mostmembers are unclear, this review analyzes the protein structures and functions, their activation and processing, their known and potential activities, and their evolutionary relationships. A sequence alignment of human ADAMsis compiled and their homology and physical data are calculated. The conceivable functions of ADAMs in reproduction, development, and diseases are also discussed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 10:01:19