Electrostatic complementarity within the substrate-binding pocket of trypsin - Wikidata - wikimedia - TriplyDB

Electrostatic complementarity within the substrate-binding pocket of trypsin

Electrostatic complementarity within the substrate-binding pocket of trypsin

http://www.wikidata.org/entity/Q33630901

about

Substrate specificity of trypsin investigated by using a genetic selection The three-dimensional structure of Asp189Ser trypsin provides evidence for an inherent structural plasticity of the protease Swapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidase Determinants of Affinity and Proteolytic Stability in Interactions of Kunitz Family Protease Inhibitors with Mesotrypsin Binding of tetracycline and chlortetracycline to the enzyme trypsin: spectroscopic and molecular modeling investigations Structural determinants of the half-life and cleavage site preference in the autolytic inactivation of chymotrypsin Structural basis of substrate specificity in the serine proteases VASP-E: specificity annotation with a volumetric analysis of electrostatic isopotentials.Elastase digests: new ammunition for shotgun membrane proteomics Structural and energetic determinants of the S1-site specificity in serine proteases.VASP: a volumetric analysis of surface properties yields insights into protein-ligand binding specificity.A trypsin homolog in amphioxus: expression, enzymatic activity and evolution.Specificity of trypsin and chymotrypsin: loop-motion-controlled dynamic correlation as a determinant.Investigate the binding of catechins to trypsin using docking and molecular dynamics simulation Engineering the substrate specificity of rhizopuspepsin: the role of Asp 77 of fungal aspartic proteinases in facilitating the cleavage of oligopeptide substrates with lysine in P1 Identification and Functional Characterizations of N-Terminal α-N-Methylation and Phosphorylation of Serine 461 in Human Poly(ADP-ribose) Polymerase 3.Substrate recognition by recombinant serine collagenase 1 from Uca pugilator.Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes Evolution of a mass spectrometry-grade protease with PTM-directed specificity.Glutamyl Endopeptidases: The Puzzle of Substrate Specificity SERINE proteinase like activity in apolipophorin III from the hemolymph of desert locust, Schistocerca gregaria.Isolation of suppressors of temperature-sensitive folding mutations Hereditary pancreatitis-associated mutation asn(21) --> ile stabilizes rat trypsinogen in vitro.Modeling regionalized volumetric differences in protein-ligand binding cavities.Proteolytic enzyme production by strains of the insect pathogen xenorhabdus and characterization of an early-log-phase-secreted protease as a potential virulence factor.The specificity of carboxypeptidase Y may be altered by changing the hydrophobicity of the S'1 binding pocket.Acidic residues important for substrate binding and cofactor reactivity in eukaryotic ornithine decarboxylase identified by alanine scanning mutagenesis.Enzymic characterization with progress curve analysis of a collagen peptidase from an enthomopathogenic bacterium, Photorhabdus luminescens.Comparative binding energy analysis for binding affinity and target selectivity prediction.Molecular characterization of two trypsinogens in the orange-spotted grouper, Epinephelus coioides, and their expression in tissues during early development.Residue Asp-189 controls both substrate binding and the monovalent cation specificity of thrombin.Protonation state of a single histidine residue contributes significantly to the kinetics of the reaction of plasminogen activator inhibitor-1 with tissue-type plasminogen activator.Toxic interaction between acid yellow 23 and trypsin: spectroscopic methods coupled with molecular docking.Review Electrostatics in the active site of an alpha-amylase

P2860

Q24557444-3C88CF50-C690-44C0-859D-42B23FF5B21F Q27619244-692860F4-3621-4FEE-AC80-72446F6B766E Q27643647-EFDD7FE2-9AE8-4D51-86E0-77A7485B742C Q27664637-432F18E8-5558-42D6-A2BF-C06E37A2ECB9 Q28478472-7BB00855-5243-437C-A702-642EC2B547AF Q28579202-FD2FE435-781A-4F35-A616-EF9CA739826A Q29619675-112AB426-05C5-47FF-8433-16D6D5DCBAC3 Q30366195-DA8C5CA6-F001-412A-95B6-96605384F61C Q33396617-53C2E291-623B-4C6A-BB65-476E822572B4 Q33548213-E6F2E335-4760-411B-8E6D-BEB1A5EF61E7 Q33683387-4A9BD1F7-0506-4137-8A14-D56D6BE7ABB3 Q33916916-8C036DC7-E8A5-4F50-985E-6BDBDDBD50E4 Q33987438-D9557EE3-0C25-4881-97E8-A107A3490575 Q35621574-9979E05F-DD7B-40A2-BB96-EF47CCBD1F09 Q36279114-43657852-CC06-4B6F-B7B3-55A472BDDA44 Q36436390-F633DD12-7498-453E-87B9-526243063735 Q36798549-FD511BBF-D496-46E9-9E94-D2229033984D Q37059742-53154721-1786-4BB2-BB1F-37E999EDA016 Q37534355-33D560FC-1766-47B3-9FE7-AD28ED264954 Q38663294-1597FF6C-CBF5-4334-A094-DD7D885899C6 Q39208250-D099BF8E-2D33-421E-95E1-A62CF3AE9B6F Q39930018-D60EC862-F53C-4E26-91F1-D4414008929B Q41694955-BCB2DC38-A8DE-443E-930A-CECB1B321064 Q41889970-DD9AC635-CEF2-4FEC-86C7-A3BF4EC9A766 Q42019913-4DF92AD2-42A9-4061-8319-FEE12BC501A7 Q42142919-9FEC94B1-C432-44F3-8B39-4964C26D7FB1 Q42683936-3F7C6BF2-84BC-45ED-9078-B40589B205DC Q43003722-C7CFDB13-4323-4F29-96E9-FEC148D8E789 Q43273730-8C1F4C46-D13A-476E-A4C5-5299BC65032C Q44200804-D4856DD8-0A6A-407B-8D26-720AF55F17F0 Q44695944-1DCB92E9-855B-4690-82EA-AA6D2AF01294 Q44807445-61671985-3E75-4D92-8685-E424B0329EB3 Q51342876-B59C98C8-99FA-4A41-B941-F324E96D79D8 Q56866496-096F5462-2F75-4357-94FA-24BA0AA7062D Q57823322-25CCA1D8-0880-4B18-97DF-473A2B83BD9E

P2860

Electrostatic complementarity within the substrate-binding pocket of trypsin

http://www.wikidata.org/entity/Q33630901

description

1988 nî lūn-bûn

@nan

1988 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

1988 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

1988年の論文

@ja

1988年論文

@yue

1988年論文

@zh-hant

1988年論文

@zh-hk

1988年論文

@zh-mo

1988年論文

@zh-tw

1988年论文

@wuu

name

Electrostatic complementarity within the substrate-binding pocket of trypsin

@ast

Electrostatic complementarity within the substrate-binding pocket of trypsin

@en

type

label

Electrostatic complementarity within the substrate-binding pocket of trypsin

@ast

Electrostatic complementarity within the substrate-binding pocket of trypsin

@en

prefLabel

Electrostatic complementarity within the substrate-binding pocket of trypsin

@ast

Electrostatic complementarity within the substrate-binding pocket of trypsin

@en

P1433

Q33630901-4EDDC55B-34B8-4CEC-BE80-ADB373719378

P1476

Q33630901-6DA7B59B-C809-4616-BFD2-AD52D3710665

P2093

Q33630901-0016266C-7A06-4827-8053-E9FC75D0C692

Q33630901-3C94D41E-F07E-4D9C-BDF3-5EA3C8519D9F

Q33630901-3E4D5B76-5DCA-4504-AF66-736BB9464C09

Q33630901-584F5695-49D4-4D22-A526-D86B7D5FA7FD

Q33630901-6E076A8B-D1E8-4A9F-B479-A2996B90E956

Q33630901-AF9028AF-38F6-4504-AD12-6130EDED2CB0

Q33630901-C9FA63CF-C372-46C7-A992-7C9C4A1F68F8

Q33630901-CB9B029A-6BA9-483A-8C14-F92D149668FA

Q33630901-EA384795-7795-4365-9303-CAD7083564E9

P2860

Q33630901-18658F80-DC7C-457D-A025-602E84C5FFFC

Q33630901-271F8B39-0487-4B7F-A5CB-5AC9B6798C6F

Q33630901-29306B0A-10C3-4309-8A42-ED0AD14A4104

Q33630901-66EABE20-D3C7-43E0-A584-3916E569AFC2

Q33630901-6FBD2507-9839-43E9-99AB-41DCC8E9FF1D

Q33630901-6FF64759-AEB9-4821-8B96-00E49DDA1BFB

Q33630901-731CD6E4-CD73-40AE-8E09-9ACDACD76343

Q33630901-8E34301E-EFFB-44A2-92B3-856A1BAD1D08

Q33630901-94C3906F-BEE4-4CA2-8DB1-DDD257BBE865

Q33630901-BC809305-140C-482D-AF31-6A3C55C46132

P304

Q33630901-535E8598-AAC4-4E13-89D7-AAE5634192C9

P31

Q33630901-E63C7C1C-2A58-4EE6-A5D0-BF44AD06698B

P356

Q33630901-457E8FDE-C14D-4F37-9CE7-43F1D0E42E42

P407

Q33630901-9AB924D1-91E5-478E-8ED6-ACDCC04CB789

P433

Q33630901-9495C827-FE60-42FC-A182-1C65C8D72A40

P478

Q33630901-5EE749BF-711B-4CB2-A300-1D2AECD371AA

P577

Q33630901-DA2AF856-187E-4A7D-95D2-D01AD8EDB76F

P5875

Q33630901-5396EC04-7953-45F3-BBB6-A675A9DF2F39

P698

Q33630901-C525AFF6-CE93-4C0E-B296-E6DFD7227BE5

P921

Q33630901-8C05B05B-1184-40C6-94B2-A52037C641B1

P932

Q33630901-F876AE67-C447-4BF1-AB31-4CFE32F5C736

P356

PNAS.85.14.4961

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Electrostatic complementarity within the substrate-binding pocket of trypsin

@en

P2093

Gráf L

http://www.w3.org/2001/XMLSchema#string

Hegyi G

http://www.w3.org/2001/XMLSchema#string

Hepp J

http://www.w3.org/2001/XMLSchema#string

Jancsó A

http://www.w3.org/2001/XMLSchema#string

Medzihradszky K

http://www.w3.org/2001/XMLSchema#string

Náray-Szabó G

http://www.w3.org/2001/XMLSchema#string

Pintér K

http://www.w3.org/2001/XMLSchema#string

Rutter WJ

http://www.w3.org/2001/XMLSchema#string

Szilágyi L

http://www.w3.org/2001/XMLSchema#string

P2860

Serine proteases: structure and mechanism of catalysis

Determination of the operational molarity of solutions of bovine alpha-chymotrypsin, trypsin, thrombin and factor Xa by spectrofluorimetric titration

Stabilization of charges on isolated ionic groups sequestered in proteins by polarized peptide units.

Hydrogen bonding and biological specificity analysed by protein engineering.

Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region.

Designing substrate specificity by protein engineering of electrostatic interactions.

Structure of two related rat pancreatic trypsin genes.

The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0.

Cloning and restriction mapping of the alkaline phosphatase structural gene (phoA) of Escherichia coli and generation of deletion mutants in vitro

Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineering.

P304

4961-4965

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.85.14.4961

http://www.w3.org/2001/XMLSchema#string

P407

P433

14

http://www.w3.org/2001/XMLSchema#string

P478

85

http://www.w3.org/2001/XMLSchema#string

P577

1988-07-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

20020943

http://www.w3.org/2001/XMLSchema#string

P698

3134655

http://www.w3.org/2001/XMLSchema#string

P921

P932

281667

http://www.w3.org/2001/XMLSchema#string