Mutation of antitrypsin to antithrombin. alpha 1-antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder.
about
Challenges in the association of human single nucleotide polymorphism mentions with unique database identifiersCanonical inhibitor-like interactions explain reactivity of alpha1-proteinase inhibitor Pittsburgh and antithrombin with proteinasesFamilial thrombophilia due to a previously unrecognized mechanism characterized by poor anticoagulant response to activated protein C: prediction of a cofactor to activated protein CPoxvirus pathogenesisAlpha1-antitrypsin deficiency. 2: genetic aspects of alpha(1)-antitrypsin deficiency: phenotypes and genetic modifiers of emphysema riskAn overview of the serpin superfamilyDeficient and Null Variants of SERPINA1 Are Proteotoxic in a Caenorhabditis elegans Model of α1-Antitrypsin DeficiencyAllosteric Modulation of Hormone Release from Thyroxine and Corticosteroid-binding GlobulinsThe refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segmentHeparin binds lamprey angiotensinogen and promotes thrombin inhibition through a template mechanismInhibition of distant caspase homologues by natural caspase inhibitorsTowards engineering hormone-binding globulins as drug delivery agentsThe molecular basis of genetic dominanceImpact of genetic variation on three dimensional structure and function of proteins.The murine Spi-2 proteinase inhibitor locus: a multigene family with a hypervariable reactive site domain.Human mesotrypsin exhibits restricted S1' subsite specificity with a strong preference for small polar side chainsInhibition of Lassa virus glycoprotein cleavage and multicycle replication by site 1 protease-adapted alpha(1)-antitrypsin variants.Cloning, structure and expression of cDNA for mouse contrapsin and a related protein.SPI-1-dependent host range of rabbitpox virus and complex formation with cathepsin G is associated with serpin motifs.Retention of thrombin inhibitory activity by recombinant serpins expressed as integral membrane proteins tethered to the surface of mammalian cells.Evaluation of "at risk" alpha 1-antitrypsin genotype SZ with synthetic oligonucleotide gene probesAlpha-1-antitrypsin-Pittsburgh. A potent inhibitor of human plasma factor XIa, kallikrein, and factor XIIf.Recombinant alpha 1-antitrypsin Pittsburgh (Met 358----Arg) is a potent inhibitor of plasma kallikrein and activated factor XII fragmentUse of vaccinia virus vectors to study protein processing in human disease. Normal nerve growth factor processing and secretion in cultured fibroblasts from patients with familial dysautonomia.Miropin, a novel bacterial serpin from the periodontopathogen Tannerella forsythia, inhibits a broad range of proteases by using different peptide bonds within the reactive center loop.Fusion of the C-terminal triskaidecapeptide of hirudin variant 3 to alpha1-proteinase inhibitor M358R increases the serpin-mediated rate of thrombin inhibition.Alpha-1 proteinase inhibitors for the treatment of alpha-1 antitrypsin deficiency: safety, tolerability, and patient outcomes.Why has it been so difficult to prove the efficacy of alpha-1-antitrypsin replacement therapy? Insights from the study of disease pathogenesisProtection by recombinant alpha 1-antitrypsin Ala357 Arg358 against arterial hypotension induced by factor XII fragment.Major proteinase movement upon stable serpin-proteinase complex formationDesign and characterization of an APC-specific serpin for the treatment of hemophilia.Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into beta-sheet A.Proprotein convertase inhibition: Paralyzing the cell's master switches.A new member of the plasma protease inhibitor gene family.Dominance from the perspective of gene-gene and gene-chemical interactionsA Novel Serpin Regulatory Mechanism: SerpinB9 IS REVERSIBLY INHIBITED BY VICINAL DISULFIDE BOND FORMATION IN THE REACTIVE CENTER LOOPWhat we owe to alpha(1)-antitrypsin and to Carl-Bertil Laurell.alpha(1)-Proteinase inhibitor mutants with specificity for plasma kallikrein and C1s but not C1Identification of tissue-type plasminogen activator-specific plasminogen activator inhibitor-1 mutants. Evidence that second sites of interaction contribute to target specificity.Rabbit alpha-1-antiproteinase E: a novel recombinant serpin which does not inhibit proteinases.
P2860
Q21284327-33389A7D-4C68-4194-84C0-0E1657364331Q24308401-A1C8C23E-678F-4D99-AC65-7FA04C37D1CCQ24563608-C3E67158-FF28-46B9-8CB7-CAC607043827Q24634729-8D0B1415-E9D3-4A2D-BBA2-3E386CDBD55DQ24678705-70973C72-EAD7-46AD-85BD-86079D0DC5C2Q24684030-F886686B-086B-488B-BF96-D81E9F8E20B4Q27348851-D9EC1340-13CE-4CE7-945D-F4D611BDAEB9Q27666981-91EB6D9E-F0B4-4459-9D93-697025B1EAC4Q27700069-51AA12E7-A930-4D73-8F2B-55BC1217DAF1Q27728134-C154F9FC-D8FA-4AC9-B54D-08238473DA4CQ28343620-5CDAAEEB-B938-4916-88C4-E9FAFF19EE94Q28545213-83CFAEF7-14DA-405C-9CEC-42673766D486Q28972447-E6EEC771-3852-4FEC-A24D-E8FC74747B0FQ30491136-4325671F-6963-49DF-9748-5D03A58936B5Q30885505-E67E4324-063A-4C31-9D66-8C50F3FE8747Q33246025-E006E897-FAF1-49B5-A027-250DDC02E9F5Q33458341-751C6E39-77A4-4A48-8BFA-5C6CDFC781C2Q33583716-E668419A-873A-4531-A53B-CE76D447607BQ33822483-1E3F5DAB-55FF-47C8-A02C-420C37933C93Q34040373-744EB484-A848-4F71-9D1C-80D0542979A5Q34521234-228878F5-33F0-4048-B6B6-298A026C589FQ34522251-56236B7D-80A3-4C6C-91AC-A8AB710221BAQ34522312-3B9AC7D6-AAB2-4FD8-A77A-A66AAD20F18BQ34556446-9A6D72BD-2DDC-4DD7-9DA5-591EDC5B8495Q34801774-6A014D47-3F75-4BF1-90E5-98277FAD4C11Q35038471-4CF250E0-C751-4C5A-AD16-4937F7DF3812Q35063726-72A992A4-F2DB-4E7D-ABA3-41484403AEA0Q35233352-C743AA02-A13A-48C9-A1B0-09D1C788DA5FQ35577711-070EEF50-6627-4830-B3E2-7FD988FCD75AQ35952177-896D4385-B9A6-4B95-ADDA-C3354C567241Q36176667-D8B27231-2196-4946-B40E-40CA50E0487DQ36331710-DE936A57-FB38-43F7-84A8-827D1A98C2E8Q36358957-FD5ADC27-92F9-4FBE-ABB3-CE453196D1C5Q36424531-335C69F5-0875-4C70-8F02-53518F77A1FCQ36564341-63BB4FCA-6017-4375-AD61-982CF5DB8423Q36574044-5EFAA981-E44A-40BB-95E2-75FD626BB087Q36602296-5BC4B25D-3B85-4E9C-882E-7A8C3564B3D1Q36639349-DE05D136-05DB-4A74-8679-FD107DB62378Q36700767-96A4A03B-6444-4971-91F1-F1260FF78189Q36702188-CD0B3F8A-4959-4E41-A53B-CFB2DA50D9A5
P2860
Mutation of antitrypsin to antithrombin. alpha 1-antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder.
description
1983 nî lūn-bûn
@nan
1983 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1983 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1983年の論文
@ja
1983年論文
@yue
1983年論文
@zh-hant
1983年論文
@zh-hk
1983年論文
@zh-mo
1983年論文
@zh-tw
1983年论文
@wuu
name
Mutation of antitrypsin to ant ...... g), a fatal bleeding disorder.
@ast
Mutation of antitrypsin to ant ...... g), a fatal bleeding disorder.
@en
Mutation of antitrypsin to ant ...... g), a fatal bleeding disorder.
@nl
type
label
Mutation of antitrypsin to ant ...... g), a fatal bleeding disorder.
@ast
Mutation of antitrypsin to ant ...... g), a fatal bleeding disorder.
@en
Mutation of antitrypsin to ant ...... g), a fatal bleeding disorder.
@nl
prefLabel
Mutation of antitrypsin to ant ...... g), a fatal bleeding disorder.
@ast
Mutation of antitrypsin to ant ...... g), a fatal bleeding disorder.
@en
Mutation of antitrypsin to ant ...... g), a fatal bleeding disorder.
@nl
P2093
P1476
Mutation of antitrypsin to ant ...... g), a fatal bleeding disorder.
@en
P2093
P304
P356
10.1056/NEJM198309223091203
P407
P577
1983-09-01T00:00:00Z