Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8 A resolution
about
X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia BThe X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificityThe structure of the human betaII-tryptase tetramer: fo(u)r better or worseMolecular 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 crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex.The refined 1.9-Å X-ray crystal structure of d-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationshipsStabilization of the E* Form Turns Thrombin into an AnticoagulantMutant N143P Reveals How Na+ Activates ThrombinCrystal structure of prethrombin-1Crystal Structures of Prethrombin-2 Reveal Alternative Conformations under Identical Solution Conditions and the Mechanism of Zymogen ActivationAutoactivation of Thrombin PrecursorsA Molecular Switch Governs the Interaction between the Human Complement Protease C1s and Its Substrate, Complement C4Exposure of R169 controls protein C activation and autoactivationStaphylococcal SplB Serine Protease Utilizes a Novel Molecular Mechanism of ActivationThe 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 segmentLoop Electrostatics Asymmetry Modulates the Preexisting Conformational Equilibrium in ThrombinThe three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen CCrystal structure of bovine procarboxypeptidase A-S6 subunit III, a highly structured truncated zymogen ECoagulation factor XII protease domain crystal structure.Lyophilization-induced reversible changes in the secondary structure of proteins.Using the water signal to detect invisible exchanging protons in the catalytic triad of a serine protease.Simulation of the activation of alpha-chymotrypsin: analysis of the pathway and role of the propeptide.Molecular origins of osmotic second virial coefficients of proteins.Modeling zymogen protein C.Crystal structure of a clip-domain serine protease and functional roles of the clip domains.Evidence of the E*-E equilibrium from rapid kinetics of Na+ binding to activated protein C and factor Xa.Probing the catalytic activity of a cell division-specific transpeptidase in vivo with beta-lactams.Toward computer-aided site-directed mutagenesis of enzymesKinetic dissection of the pre-existing conformational equilibrium in the trypsin fold.Conformational selection in trypsin-like proteases.Models of the serine protease domain of the human antithrombotic plasma factor activated protein C and its zymogen.The co-crystal structure of unliganded bovine alpha-thrombin and prethrombin-2: movement of the Tyr-Pro-Pro-Trp segment and active site residues upon ligand bindingStructural features that specify tyrosine kinase activity deduced from homology modeling of the epidermal growth factor receptor.Identification of 31 novel mutations in the F8 gene in Spanish hemophilia A patients: structural analysis of 20 missense mutations suggests new intermolecular binding sites.Calculation of translational friction and intrinsic viscosity. II. Application to globular proteinsSerine proteases.Accurate optimization of amino acid form factors for computing small-angle X-ray scattering intensity of atomistic protein structures.Glutamyl Endopeptidases: The Puzzle of Substrate SpecificityProtein engineering. The design, synthesis and characterization of factitious proteins.
P2860
Q24562944-ACA5D3A5-D157-4A0D-B079-6AFA2C0089E2Q24596245-CFD6B119-8AEF-452B-833E-98CEB3EA31A1Q24615069-051D092B-B472-4EDB-BC7E-38AC70BE7575Q24673104-5C42093C-0E10-4B2E-A87C-DE8C0F082ED2Q27617260-B0F4AE35-7E5E-468E-ABA5-C53CE4BF3F41Q27637552-B2E58B7B-211C-4075-BF36-73380D810AE3Q27642041-74AE4B66-F055-4834-AE0E-E6464C5D0FEAQ27655637-0F571817-6B51-4D27-B709-342EF50D5149Q27657884-D446517D-A076-4314-B250-8FE7549BDAE2Q27665368-B2241865-FB51-42B8-8345-ABD8D9CC24F7Q27675359-E17F0A4A-D0F7-4C94-AA22-259AC9B5E58BQ27676718-C2058A1A-FD84-4F18-BBF1-E00D1D7E890FQ27677421-EEF1598F-B8CA-4233-A39E-7D948A76E81AQ27678741-33AFFFC1-2D8D-414A-8875-DB66768B9D7DQ27683108-84A72D4E-85B5-42CD-A1BF-F9CB5D3FC3E0Q27700069-9185727A-A6DB-4822-9B78-C394AC5D501BQ27714094-35E0A39D-13FA-4467-B933-0B5D49132508Q27729482-2AA3C1F6-A4BC-419C-9DE2-1DC85F2F1078Q27731296-3580FE8E-37B6-4A4B-8E37-2A83EF6BC9BEQ30370920-7A6737D7-8353-4169-89B1-AC36738D00C9Q33746835-26BE9FDA-35E9-480F-AEA9-FCD953BBF57AQ33978526-DD5DCCEE-C74E-4FB8-B1E3-347C10D3DE50Q33983248-0C967B57-2E99-4A26-966B-A48972DED94AQ34169400-815EDB74-8E84-46B7-80FA-5F757856A713Q34174481-070162F2-9DD0-4918-BBF5-04E64AD8256FQ34324966-53C0A7D7-A67E-40D9-B32D-BF556FA6E7BBQ34630229-9A004A57-62E2-4C6E-8009-BAC0E2F943DBQ35098282-58678F64-77EA-44B0-8595-83876305D24BQ35608162-E3BB934F-C353-4F7D-94DB-6E8C83388D6DQ36049897-9D84AEC2-1EE8-4E6A-A8A5-865C2B68EB9FQ36177002-1269147B-6716-4F85-9351-E2D58542EA39Q36278723-A3123588-32EE-4A46-85C9-4D689D1E4495Q36280463-6A6C3451-DB7B-453E-972F-4824F5459D49Q36331374-7A97E4B7-5AA6-4871-ACE6-2DD60B2BB6ADQ36508875-058CA705-86B0-4958-8D56-D5E463881608Q36795615-A8E84EBB-A292-426F-BE55-7062B0E4DCFFQ37175533-1BDCF791-E8B8-4F54-A1EA-F51056DD9385Q37576156-55214B58-F492-4AC2-8B0B-7065E0D32D9EQ38663294-4A999574-C563-4F28-A8EA-3E4CF5DEE12DQ39677448-30A94E54-DB6F-44CC-8134-7A50392D6EE5
P2860
Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8 A resolution
description
1985 nî lūn-bûn
@nan
1985 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1985 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1985年の論文
@ja
1985年学术文章
@wuu
1985年学术文章
@zh-cn
1985年学术文章
@zh-hans
1985年学术文章
@zh-my
1985年学术文章
@zh-sg
1985年學術文章
@yue
name
Bovine chymotrypsinogen A X-ra ...... ystal form at 1.8 A resolution
@ast
Bovine chymotrypsinogen A X-ra ...... ystal form at 1.8 A resolution
@en
Bovine chymotrypsinogen A X-ra ...... ystal form at 1.8 A resolution
@nl
type
label
Bovine chymotrypsinogen A X-ra ...... ystal form at 1.8 A resolution
@ast
Bovine chymotrypsinogen A X-ra ...... ystal form at 1.8 A resolution
@en
Bovine chymotrypsinogen A X-ra ...... ystal form at 1.8 A resolution
@nl
prefLabel
Bovine chymotrypsinogen A X-ra ...... ystal form at 1.8 A resolution
@ast
Bovine chymotrypsinogen A X-ra ...... ystal form at 1.8 A resolution
@en
Bovine chymotrypsinogen A X-ra ...... ystal form at 1.8 A resolution
@nl
P2093
P1476
Bovine chymotrypsinogen A X-ra ...... ystal form at 1.8 A resolution
@en
P2093
P304
P407
P577
1985-10-05T00:00:00Z