about
Molecular mechanisms for the conversion of zymogens to active proteolytic enzymesStructural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor DThe energetic cost of induced fit catalysis: Crystal structures of trypsinogen mutants with enhanced activity and inhibitor affinityActive site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cationsCrystal structure of prethrombin-1Crystal Structures of Prethrombin-2 Reveal Alternative Conformations under Identical Solution Conditions and the Mechanism of Zymogen ActivationLong-range Electrostatic Complementarity Governs Substrate Recognition by Human Chymotrypsin C, a Key Regulator of Digestive Enzyme ActivationAutoactivation of Thrombin PrecursorsRezymogenation of active urokinase induced by an inhibitory antibodyActivation of pro-astacin. Immunological and model peptide studies on the processing of immature astacin, a zinc-endopeptidase from the crayfish Astacus astacus.Discovery of an allosteric site in the caspasesAnalysis of an engineered plasma kallikrein inhibitor and its effect on contact activation.Application of pulse radiolysis to the study of proteins: chymotrypsin and trypsin.Allostery in trypsin-like proteases suggests new therapeutic strategies.Mackerel trypsin purified from defatted viscera by supercritical carbon dioxide.Kinetic dissection of the pre-existing conformational equilibrium in the trypsin fold.Conformational selection in trypsin-like proteases.In vitro mutagenesis of trypsinogen: role of the amino terminus in intracellular protein targeting to secretory granulesStructure and function of microplasminogen: I. Methionine shuffling, chemical proteolysis, and proenzyme activation.Trypanosoma brucei S-adenosylmethionine decarboxylase N terminus is essential for allosteric activation by the regulatory subunit prozymeHerpesvirus proteinase: site-directed mutagenesis used to study maturational, release, and inactivation cleavage sites of precursor and to identify a possible catalytic site serine and histidine.Expression of rat chymotrypsinogen in yeast: a study on the structural and functional significance of the chymotrypsinogen propeptide.Tighter Control by Chymotrypsin C (CTRC) Explains Lack of Association between Human Anionic Trypsinogen and Hereditary Pancreatitis.Slow thrombin is zymogen-likeTrypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiology.Variants of tissue-type plasminogen activator with substantially enhanced response and selectivity toward fibrin co-factors.Expression of human cationic trypsinogen with an authentic N terminus using intein-mediated splicing in aminopeptidase P deficient Escherichia coli.A single mutation in the activation site of bovine trypsinogen enhances its accumulation in the fermentation broth of the yeast Pichia pastoris.Mass spectrometric detection of tyrosine sulfation in human pancreatic trypsinogens, but not in tumor-associated trypsinogen.Nonenzymatic anticoagulant activity of the mutant serine protease Ser360Ala-activated protein C mediated by factor VaProtein flexibility, not disorder, is intrinsic to molecular recognition.Modelling of the serine-proteinase fold by X-ray and neutron scattering and sedimentation analyses: occurrence of the fold in factor D of the complement system.Crystallization and preliminary X-ray diffraction studies of trypsin-like proteases from the gastric fluid of the marine crab Cancer pagurus.Kinetic analysis of ligand-induced autocatalytic reactionsA ribonuclease zymogen activated by the NS3 protease of the hepatitis C virus.Purification and characterization of three trypsin isoforms from viscera of sardinelle (Sardinella aurita).Converting tissue-type plasminogen activator into a zymogen.Identification of a hydrophobic exosite on tissue type plasminogen activator that modulates specificity for plasminogen.Reconstitution of human azurocidin catalytic triad and proteolytic activity by site-directed mutagenesis."How I chose research on proteases or, more correctly, how it chose me".
P2860
Q24673104-BDE1438B-5517-415B-B844-F4F930BE92B6Q27617260-EC25B081-46B3-471A-917C-F176F9C74B17Q27632749-EF0AECB2-BBF6-4FF1-9C81-A841E07F1206Q27655102-2E45C59A-9703-4B74-8640-66AAE4828B42Q27665368-4ABBD205-A2DA-4848-8CFA-406FCF12AC8EQ27675359-69B0D4C8-8D7F-4816-A807-7906ACC5C02CQ27676497-5FD74D32-A2C3-462D-B826-C03DCD5B2992Q27676718-30373D7B-9F17-4C62-8E21-B9BE61F44428Q27682519-A02CF11E-4C8F-45E2-BD4D-90D18855A979Q30666002-22FF15D2-53C7-4FE2-9994-36C4735F4B91Q30831384-6DEA33F5-AE1E-4BF9-AF83-C9077A03114AQ33533851-502BD4B3-D3C7-4B3D-8C79-A7806B4CA0F4Q34657514-47B04FF0-D564-4B8D-8F84-651CCE178D6DQ35317139-AC17260D-B531-4FC5-9FC8-BDA6C3DFF4FAQ35706902-E8694D6C-3F6C-4DE1-95E5-8D1456110C5EQ36049897-6327A6E0-0739-43AC-89AD-654E4BE2BBD3Q36177002-B735023F-2A09-4A6F-97BE-74AD65069705Q36217339-6BBD1851-9257-4505-8925-B804F2E78EB1Q36279346-ADDEA98B-CA22-4BFF-B746-3013852C9B34Q36620918-1DB0ADD3-6421-4447-8A53-BAF4767451E8Q36655290-B74C687F-532A-42F5-97EB-0E4D95BC8F21Q36799585-BCC96F86-C00C-415F-ABBC-9B22AF58A0B0Q37065823-29CEED85-989F-4142-88EA-1D71E715CB76Q37278697-0C570065-CAB1-40F2-A39C-40CEE8880607Q38246368-439F9202-504A-4409-92C5-B7A5173FBC9AQ38290601-B6851F1F-45CE-41D8-AFC3-A7840BCE7CB5Q38605810-14FA30E3-4D65-4326-8874-B4B761BA897DQ39708854-87AE5B57-0920-4AE9-874F-78A0F4338E02Q40036264-1DC16DA2-DA11-4741-B1B6-2F8954DC3435Q41142483-74934499-2F14-4033-95A9-F09E12EAD459Q41842857-80902DA7-90B9-4686-BACF-391FE2F6D681Q41977792-FBEED5BE-760F-40FA-A170-57E6A203AB12Q42054537-FEFE8B0E-97D8-47B8-8F8E-B7171BB03A76Q42133495-428021E5-D414-430E-8A60-DA8D176D0A58Q43033809-89434100-BA90-4E62-BBE6-D290D0ABA8F3Q44610436-C0987315-191C-4353-B97E-555F14A09679Q45968900-2FA4D364-06C3-4E53-A82F-C2307D0AFCE3Q45975726-4D994E02-39EA-42BB-94E7-EB1161140B56Q46483671-7F045DCE-E576-41FF-A864-F463D7458CA9Q48343036-98C32F73-1F3D-4644-8550-A5ADC44B5AAA
P2860
description
1977 nî lūn-bûn
@nan
1977 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1977 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1977年の論文
@ja
1977年学术文章
@wuu
1977年学术文章
@zh-cn
1977年学术文章
@zh-hans
1977年学术文章
@zh-my
1977年学术文章
@zh-sg
1977年學術文章
@yue
name
Structure of bovine trypsinogen at 1.9 A resolution
@ast
Structure of bovine trypsinogen at 1.9 A resolution
@en
Structure of bovine trypsinogen at 1.9 A resolution
@nl
type
label
Structure of bovine trypsinogen at 1.9 A resolution
@ast
Structure of bovine trypsinogen at 1.9 A resolution
@en
Structure of bovine trypsinogen at 1.9 A resolution
@nl
prefLabel
Structure of bovine trypsinogen at 1.9 A resolution
@ast
Structure of bovine trypsinogen at 1.9 A resolution
@en
Structure of bovine trypsinogen at 1.9 A resolution
@nl
P2093
P356
P1433
P1476
Structure of bovine trypsinogen at 1.9 A resolution
@en
P2093
A A Kossiakoff
J L Chambers
R M Stroud
P304
P356
10.1021/BI00623A016
P407
P577
1977-02-22T00:00:00Z