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Biochimica et Biophysica Acta - Molecular Basis of Disease

Volumn 1535, Issue 3, 2001, Pages 221-235

Conformational properties of serine proteinase inhibitors (serpins) confer multiple pathophysiological roles

(1) Janciauskiene, Sabina a

a Malmo University Hospital (Sweden)

Author keywords

1 Antichymotrypsin; 1 Antitrypsin; Conformational polymorphism; Serpin

Indexed keywords

ALPHA 1 ANTICHYMOTRYPSIN; ALPHA 1 ANTITRYPSIN; SERINE PROTEINASE INHIBITOR;

ALZHEIMER DISEASE; ANGIOGENESIS; APOPTOSIS; BLOOD CLOTTING; COMPLEMENT ACTIVATION; COMPLEX FORMATION; EMPHYSEMA; ENZYME CONFORMATION; FIBRINOLYSIS; HUMAN; HYPERSENSITIVITY; INFLAMMATION; LIVER CIRRHOSIS; MENTAL DISEASE; NEOPLASM; NONHUMAN; OXIDATION; PATHOGENESIS; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FAMILY; PROTEIN POLYMORPHISM; PROTEIN STRUCTURE; REGULATORY MECHANISM; REVIEW; THROMBOSIS; VIRUS PATHOGENESIS;

ALPHA 1-ANTICHYMOTRYPSIN; ALPHA 1-ANTITRYPSIN; ALZHEIMER DISEASE; ANIMALS; HUMANS; MODELS, MOLECULAR; NEURODEGENERATIVE DISEASES; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN ISOFORMS; SERINE PROTEINASE INHIBITORS; SERPINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0035952980 PISSN: 09254439 EISSN: None Source Type: Journal
DOI: 10.1016/S0925-4439(01)00025-4 Document Type: Review

Times cited : (168)

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