Structural analysis of zinc substitutions in the active site of thermolysin. - Test2 - elhamkhani - TriplyDB

Structural analysis of zinc substitutions in the active site of thermolysin.

Structural analysis of zinc substitutions in the active site of thermolysin.

http://www.wikidata.org/entity/Q41837299

about

Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis Structures and metal-binding properties of Helicobacter pylori neutrophil-activating protein with a di-nuclear ferroxidase center Characterization of the hepatitis C virus NS2/3 processing reaction by using a purified precursor protein Experimental and computational mapping of the binding surface of a crystalline protein Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site The functional role of the binuclear metal center in D-aminoacylase: one-metal activation and second-metal attenuation Structure and Function of Non-Native Metal Clusters in Human Arginase I Pyridinylquinazolines Selectively Inhibit Human Methionine Aminopeptidase-1 in Cells Molecular insight into bacterial cleavage of oceanic dimethylsulfoniopropionate into dimethyl sulfide.Synthesis of Aspartame by Thermolysin: An X-ray Structural Study Substrate recognition of anthrax lethal factor examined by combinatorial and pre-steady-state kinetic approaches Inhibition of a Putative Dihydropyrimidinase from Pseudomonas aeruginosa PAO1 by Flavonoids and Substrates of Cyclic Amidohydrolases Comparison of the Internal Dynamics of Metalloproteases Provides New Insights on Their Function and Evolution.Analysis of substructural variation in families of enzymatic proteins with applications to protein function prediction.Thermolysin and mitochondrial processing peptidase: how far structure-functional convergence goes.Bifunctional role of the Treponema pallidum extracellular matrix binding adhesin Tp0751.Carboxylate binding modes in zinc proteins: a theoretical study Flexibility of the Kir6.2 inward rectifier K(+) channel pore Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals.Protein surface analysis for function annotation in high-throughput structural genomics pipeline.Hydrogen bond residue positioning in the 599-611 loop of thimet oligopeptidase is required for substrate selection Competitive cobalt for zinc substitution in mammalian methionine sulfoxide reductase B1 overexpressed in E. coli: structural and functional insight.Automated identification of elemental ions in macromolecular crystal structures.Efficient docking of peptides to proteins without prior knowledge of the binding site.Conservation and diversity of the IrrE/DdrO-controlled radiation response in radiation-resistant Deinococcus bacteria.Reversible inhibition of the second step of splicing suggests a possible role of zinc in the second step of splicing.ANODE: anomalous and heavy-atom density calculation Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family.Defining the metal binding pathways of human metallothionein 1a: balancing zinc availability and cadmium seclusion.Substrate specificity of the metalloproteinase pregnancy-associated plasma protein-A (PAPP-A) assessed by mutagenesis and analysis of synthetic peptides: substrate residues distant from the scissile bond are critical for proteolysis Structural modeling and biochemical characterization of recombinant KPN_02809, a zinc-dependent metalloprotease from Klebsiella pneumoniae MGH 78578.Docking small peptides remains a great challenge: an assessment using AutoDock Vina.Burkholderia cenocepacia ZmpB is a broad-specificity zinc metalloprotease involved in virulence.Vibrio vulnificus secretes a broad-specificity metalloprotease capable of interfering with blood homeostasis through prothrombin activation and fibrinolysis.Thermoanaerobacter brockii alcohol dehydrogenase: characterization of the active site metal and its ligand amino acids.Effects of site-directed mutagenesis in the N-terminal domain of thermolysin on its stabilization.Archaeal JAB1/MPN/MOV34 metalloenzyme (HvJAMM1) cleaves ubiquitin-like small archaeal modifier proteins (SAMPs) from protein-conjugates.Widespread distribution of cell defense against D-aminoacyl-tRNAs.A Transferable Non-bonded Pairwise Force Field to Model Zinc Interactions in Metalloproteins.Cavity scaling: automated refinement of cavity-aware motifs in protein function prediction.

P2860

Q24680165-C8465C24-8F31-4099-B726-CEB50FECE703 Q26999811-6C4516C6-2612-44D5-A0A1-FDF4BD4F49CD Q27469874-A784A3F1-1A71-4364-B85A-D3A242F382E4 Q27631035-6D94CD98-04A2-449C-8904-909E99D5B3A8 Q27634804-94F95BFC-D276-4AA4-9FAD-8CC91C0C1193 Q27643008-469DC5EE-4B12-4D63-92F2-826032E76985 Q27674466-50E033A5-9B64-4043-A00E-B1517B59848F Q27677949-02A004D3-1560-452C-B345-EA94B28B7922 Q27681210-B74D2487-F906-4969-BFB5-091164B2B302 Q27684394-08A70751-853A-4368-BA54-15173A8542E7 Q28389793-A23E35F6-B3E3-4BCD-92EA-7FE3DA4BE419 Q28547343-C80B1602-F1DE-4E30-899E-94D065F413C7 Q30379469-D8A86634-82F3-4DB7-A90A-BC869CB72669 Q30389018-AA74B10F-D1AA-4F6E-B678-D9CF6CE168B7 Q30826963-6F1E18FD-ECC8-4375-9B25-6966F0E3F594 Q33768367-56FC6B54-5054-4389-92B8-5BCABCAACB6D Q34171799-63A94778-ED79-48BA-AE89-C65824019564 Q35061235-AE213DCF-51E0-4355-9C56-66E7DE95A571 Q35427600-EE382273-D2A2-411C-833A-72B7BE44842B Q36476631-28F0B1EC-5EEF-4110-8B12-F0CB3497E848 Q37113595-A2AC39A4-E1CE-4012-A496-852A6808CFDA Q37470716-8F639649-53E8-4151-A803-FCB370464D88 Q37685016-56C551E8-05FC-4547-B57D-C65F39E62358 Q38270145-401D1920-68CC-46A5-9963-6475E94D1241 Q38843113-AA9DD235-5F9E-469A-8AC6-8CFE7C2FC35A Q39698187-55EAA126-66D5-4906-AB8E-BC9C0AFB9520 Q40010756-894AF11A-0ECA-4CF9-9882-FACDDC51E059 Q40125665-FC0CE603-E97F-4C9F-9324-569C18202C51 Q40303644-1912918E-0FDC-4EFB-9295-EB93F864D479 Q40702779-B5D62673-5D2C-4C36-A8CF-B53781113544 Q40772408-55766AA2-30B5-4A76-A5A2-419B713FCB31 Q41030976-6CE54807-3BB0-4100-AEF4-DF65049DD344 Q41475202-074AA0EA-6A59-423E-BD97-03E5D98ACA8D Q41843964-D5874A57-85E4-4D7D-A1E2-B0CDF15663B1 Q41892824-3025155A-09AB-4F77-BCAB-F4A7827BC682 Q41962606-F8160E91-0C8C-4D10-A268-24B7DFFD6938 Q41971949-FC39B245-6421-4E54-AC72-F24E9F81BC2C Q42081618-CB81F190-A362-4504-AFAE-7A7C8F0C3EA2 Q42150041-1D422D61-C377-47AA-8051-E62056C21051 Q42624473-23658245-5276-4A01-8F78-B01CBE2DC06C

P2860

Structural analysis of zinc substitutions in the active site of thermolysin.

http://www.wikidata.org/entity/Q41837299

description

1995 nî lūn-bûn

@nan

1995年の論文

@ja

1995年論文

@yue

1995年論文

@zh-hant

1995年論文

@zh-hk

1995年論文

@zh-mo

1995年論文

@zh-tw

1995年论文

@wuu

1995年论文

@zh

1995年论文

@zh-cn

name

Structural analysis of zinc substitutions in the active site of thermolysin.

@en

type

label

Structural analysis of zinc substitutions in the active site of thermolysin.

@en

prefLabel

Structural analysis of zinc substitutions in the active site of thermolysin.

@en

P1433

Q41837299-90293A90-BC6B-4993-A67D-001DE5FE5558

P1476

Q41837299-EB9FCEC9-4D13-4743-975F-8864FC3590F0

P2093

Q41837299-0232FE7D-63FD-4C08-ACB6-A6052759BB11

Q41837299-4EAC07BF-13D3-450B-BEC5-3812F4C82DDE

Q41837299-D1077484-8AAD-4F03-94D1-C2314F265E62

Q41837299-F76EECC5-439E-4D6B-AFD4-564D335E3532

P2860

Q41837299-02EF5C57-CEE4-453D-9B50-9A730FA16714

Q41837299-34B3035A-BB99-4E47-A618-6AA8EF4FDA76

Q41837299-3660B1BD-E9F1-4287-B8A4-D93BCC62354E

Q41837299-46CD1C8B-973D-4D05-A374-18634EADFF28

Q41837299-56F4644A-53C4-4CC9-BE17-4E127A3EECC4

Q41837299-98B4E67E-B733-45B4-BF13-BC5EFEA9C8DC

Q41837299-A70B5773-0E36-427A-A1E4-A3D7DD33FF31

Q41837299-A78051C3-E99B-46B7-A382-DF2D6AAE60DD

Q41837299-A8B31C12-F851-462E-AFBE-440231AEDC99

Q41837299-AE64FB33-3535-4487-A736-54305B613296

P304

Q41837299-5193B004-C0A5-4311-A409-B1525D7EE210

P31

Q41837299-B6188FDC-2DEF-4F16-8A4C-BD98AC60D465

P356

Q41837299-47C173C7-6EAB-43BD-B25C-CC11D3863328

P433

Q41837299-FB73D88E-C9EF-452F-AF4F-F380E2E19819

P478

Q41837299-23F51663-7FF8-486A-B2A4-59CCC14DAE2F

P577

Q41837299-E5349C9D-04A4-4AD2-AAC6-C4A5FE64C1C3

P5875

Q41837299-22617284-81B9-4B45-BDE9-3F090BBDADA2

P698

Q41837299-74472C7A-FFD3-410D-B424-A3F61695E7B5

P932

Q41837299-B3342597-3462-4BB0-83C9-5730A82A10CC

P356

P1433

Protein Science

P1476

Structural analysis of zinc substitutions in the active site of thermolysin.

@en

P2093

A C Hausrath

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

B W Matthews

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

D Juers

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

D R Holland

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

P2860

Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis

Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution

Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues

The conformation of thermolysin

An interactive computer graphics study of thermolysin-catalyzed peptide cleavage and inhibition by N-carboxymethyl dipeptides

Structure of thermolysin refined at 1.6 A resolution

Structural biology of zinc.

Crystal structure of neutral protease from Bacillus cereus refined at 3.0 A resolution and comparison with the homologous but more thermostable enzyme thermolysin.

Metalloenzymes: the entatic nature of their active sites.

Esterase activity of zinc neutral proteases.

P304

1955-1965

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

P31

scholarly article

P356

10.1002/PRO.5560041001

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

P433

10

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

P478

4

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

P577

1995-10-01T00:00:00Z

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

P5875

14665728

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

P698

8535232

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

P932

2142975

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