Molecular structure of leucine aminopeptidase at 2.7-A resolution - Wikidata - wikimedia - TriplyDB

Molecular structure of leucine aminopeptidase at 2.7-A resolution

Molecular structure of leucine aminopeptidase at 2.7-A resolution

http://www.wikidata.org/entity/Q27685398

about

Leucine aminopeptidase: bestatin inhibition and a model for enzyme-catalyzed peptide hydrolysis Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolution Structure of peptidase T from Salmonella typhimurium Crystal structure of the BcZBP, a zinc-binding protein from Bacillus cereus Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases.Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography Structure and mechanism of ADP-ribose-1''-monophosphatase (Appr-1''-pase), a ubiquitous cellular processing enzyme.Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differences Identification of residues critical for activity of the wound-induced leucine aminopeptidase (LAP-A) of tomato Overview of protein structural and functional folds.Novel small molecule nonpeptide aminopeptidase n inhibitors with a cyclic imide skeleton.The major leucyl aminopeptidase of Trypanosoma cruzi (LAPTc) assembles into a homohexamer and belongs to the M17 family of metallopeptidases.[μ-(4S,5S,15S,16S)-10,21-Di-tert-butyl-4,5,15,16-tetra-phenyl-3,6,14,17-tetra-aza-tricyclo-[17.3.1.1]tetra-cosa-1(23),8,10,12(24),19,21-hexa-ene-23,24-diolato-κN,N,O,O:NN,O,O]bis-[(acetato-κO)zinc(II)] ethanol disolvate [μ-14,29-Di-tert-butyl-3,10,18,25-tetra-azatpenta-cyclo-[25.3.1.1.0.0]dotriaconta-1(31),4,6,8,12(32),14,16,19,21,23,27,29-dodeca-ene-31,32-diol-ato]bis-[(nitrato-κO,O')zinc(II)].Pyrococcus horikoshii TET2 peptidase assembling process and associated functional regulation.Bacterial abundance, processes and diversity responses to acidification at a coastal CO2 vent.Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes The Activity of a Hexameric M17 Metallo-Aminopeptidase Is Associated With Survival of Mycobacterium tuberculosis.Cloning and genetic analysis of the Vibrio cholerae aminopeptidase gene.Temperature-regulated expression of outer membrane proteins in Shigella flexneri.Generation of AMBER force field parameters for zinc centres of M1 and M17 family aminopeptidases.Structural Characterization of Acidic M17 Leucine Aminopeptidases from the TriTryps and Evaluation of Their Role in Nutrient Starvation in Trypanosoma brucei.The thermophilic, homohexameric aminopeptidase of Borrelia burgdorferi is a member of the M29 family of metallopeptidases.Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family.Biochemical characterization and structural prediction of a novel cytosolic leucyl aminopeptidase of the M17 family from Schizosaccharomyces pombe.Crystal structure of a dodecameric tetrahedral-shaped aminopeptidase.Modulation of Streptomyces leucine aminopeptidase by calcium: identification and functional analysis of key residues in activation and stabilization by calcium.Milk Proteins Are Predigested Within the Human Mammary Gland.Catalytic mechanism of SGAP, a double-zinc aminopeptidase from Streptomyces griseus.Mechanisms of peptide hydrolysis by aspartyl and metalloproteases.Three-dimensional structural resemblance between leucine aminopeptidase and carboxypeptidase A revealed by graph-theoretical techniques.Crystal structure of XoLAP, a leucine aminopeptidase, from Xanthomonas oryzae pv. oryzae.Metallopeptidases of Toxoplasma gondii: in silico identification and gene expression.Improvement of Aminopeptidase Activity of Dizinc(II) Complexes by Increasing Substrate Accessibility

P2860

Q24563697-32729928-E30B-4D21-91E7-B3BE8DF7501F Q27628891-99E182DE-D782-4F34-85FD-AE7FEADF38CA Q27637922-9155D141-3741-466B-B37A-1BF8839FE541 Q27644769-C8000FF0-F23F-4D29-8743-450674FB53A2 Q27659580-A7DEFC1E-3388-48C3-8E36-3B1FD5FB802B Q27732175-330BC192-545F-4B0B-A428-12489B54D579 Q27937235-E3C538E7-3C29-489D-8A9F-AC656A070B78 Q28201642-0583E4B6-932D-4715-82D4-200A00AA8C02 Q28207386-E8C1C736-58B0-490A-AD8B-0D67F530C341 Q30368988-2657644F-28EA-4A73-82C1-A7DF30DCDCF9 Q33710070-E6BC43D0-242C-441D-8C46-4093FEB4E05C Q34001253-1DAE8559-6EC4-4979-A92F-6147F3F608F1 Q34264622-1931C27E-527B-4F0D-8137-29A26619B018 Q34294369-49FC4AC5-4981-4FB4-9719-E3C95E6A214F Q34346058-3845CDEB-46A1-404B-B95F-0DFD7D7F0416 Q35763955-73F0248C-BF8A-4A9F-9ABE-F88BBED4BACC Q37059742-76D8D64E-01FD-432A-AEC5-6C76C98C4CD9 Q37721237-AF2BFD97-8A04-4217-95E0-3C6E4FC72231 Q39826464-6B9D48FC-C775-43B2-9F79-A10016F44A55 Q39836106-C23A6510-F049-4B70-8832-57DB72E8D6CD Q40104381-615B7676-C0AF-4238-88A2-E370815165C0 Q41416724-9F4A0D13-3A4E-4A39-A6B9-D99D2753AF54 Q41833724-516E071A-D51F-46EA-ACBA-40134457BBE7 Q41834863-4F4D9789-689C-46D3-A5BE-8CD1FA1CF2B1 Q41941895-556D1CCC-E952-4071-9AA3-ACFDB7DDF001 Q45064158-035F6BA7-EF8F-4095-B081-6CF349124672 Q46890422-A077B78E-8876-4FC4-9EC4-EBC724CA0A34 Q49721851-2F3DEEC7-EC6D-432F-A608-B8C2DD1A2E45 Q50962681-E889CBBF-848C-42E1-852E-303589DAA859 Q51423259-9EF6B948-5110-4907-81F6-2032DE475A1A Q52421069-6C72DC74-FE49-4027-8498-E202AD8210C2 Q53310445-CF8EE79D-0CEE-4D9C-B586-407CD1319102 Q55283527-9BAEE61A-09C4-47DF-BA16-819C13B3BAC1 Q58687551-3CA25780-C682-48A3-94DB-59DBF01FF11D

P2860

Molecular structure of leucine aminopeptidase at 2.7-A resolution

http://www.wikidata.org/entity/Q27685398

description

1990 nî lūn-bûn

@nan

1990 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

1990 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

1990年の論文

@ja

1990年学术文章

@wuu

1990年学术文章

@zh-cn

1990年学术文章

@zh-hans

1990年学术文章

@zh-my

1990年学术文章

@zh-sg

1990年學術文章

@yue

name

Molecular structure of leucine aminopeptidase at 2.7-A resolution

@ast

Molecular structure of leucine aminopeptidase at 2.7-A resolution

@en

Molecular structure of leucine aminopeptidase at 2.7-A resolution

@nl

type

label

Molecular structure of leucine aminopeptidase at 2.7-A resolution

@ast

Molecular structure of leucine aminopeptidase at 2.7-A resolution

@en

Molecular structure of leucine aminopeptidase at 2.7-A resolution

@nl

prefLabel

Molecular structure of leucine aminopeptidase at 2.7-A resolution

@ast

Molecular structure of leucine aminopeptidase at 2.7-A resolution

@en

Molecular structure of leucine aminopeptidase at 2.7-A resolution

@nl

P1433

Q27685398-750F18F9-B0D8-4516-AAED-9A3C98922CF6

P1476

Q27685398-55981ABA-B027-4F2B-9F95-06EDA423A93B

P2093

Q27685398-11DFCFB8-03F7-4980-95B0-D6DFC78707CA

Q27685398-43EC39C4-4A8C-4179-9DA1-FD1170EF3C8B

Q27685398-73FC2B34-052E-4356-ABA6-6CA0AD37DF0E

Q27685398-AD0C32E5-AFF4-49E7-BF43-C3A4EE5A54E0

P2860

Q27685398-02075312-0193-4B3C-AE9A-20C8D14A4DF1

Q27685398-13BB6F2E-9C32-451E-BFBF-E6EA751E51CA

Q27685398-24F91F2C-2841-4DD0-A747-9816A155DBC0

Q27685398-3D480C62-A3F7-4D80-B589-475928F34784

Q27685398-3DA896A1-739D-45A3-9F56-5160710B3417

Q27685398-4C2E5AEC-29B2-4531-875B-CBFB85307397

Q27685398-55CF95CF-9DFD-4D24-8793-243AC1B95BB6

Q27685398-661D2D64-CEC0-4C51-A764-255029B64C76

Q27685398-66C3D3DF-6B19-42A0-A0B1-A8C83A55AA71

Q27685398-9037CE5A-3BF3-4CF2-9299-B0D03D5643F3

P304

Q27685398-554E52A5-61ED-4B86-97C1-9FD0E25EB194

P31

Q27685398-EF49E61B-8F9C-481A-93D0-620113D56DC9

P356

Q27685398-8D8EF075-74DF-4EBB-921F-BA6FFDC54BF9

P407

Q27685398-7E9244B9-6A66-45F6-ADF4-26CDDB82D362

P433

Q27685398-83EDA8F0-D4BC-4408-A7A4-FBF558BA036B

P478

Q27685398-D8B9F05B-70D3-46F0-BD58-EBF6B7428AF7

P577

Q27685398-288C8FBB-340A-4565-92A5-25A757C53534

P5875

Q27685398-DB61A5CC-BC3F-4B9F-B344-744B882E037B

P698

Q27685398-E1343099-72B2-4414-A901-CC3C29EFC913

P921

Q27685398-38358681-4827-4461-A657-BBA1DBD7856D

P932

Q27685398-6C19ECCB-0C87-4672-AD97-835995387BE0

P356

PNAS.87.17.6878

P1433

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

P1476

Molecular structure of leucine aminopeptidase at 2.7-A resolution

@en

P2093

A Taylor

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

P R David

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

S K Burley

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

W N Lipscomb

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

P2860

Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution

Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution

Crystallographic R factor refinement by molecular dynamics

Schematic drawings of protein structures

Resolution of phase ambiguity in macromolecular crystallography

Conformation of polypeptides and proteins

Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO

The structure of aconitase.

Bestatin, an inhibitor of aminopeptidase B, produced by actinomycetes.

Escherichia coli aspartate transcarbamylase: the relation between structure and function.

P304

6878-82

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

P31

scholarly article

P356

10.1073/PNAS.87.17.6878

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

P407

P433

17

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

P478

87

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

P577

1990-09-01T00:00:00Z

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

P5875

20759988

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

P698

2395881

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

P921

molecular geometry

P932

54641

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