A structural insight into the P1S1 binding mode of diaminoethylphosphonic and phosphinic acids, selective inhibitors of alanine aminopeptidases.

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M1 aminopeptidases as drug targets: broad applications or therapeutic niche?Phosphonic acid: preparation and applications.

P2860

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P2860

A structural insight into the P1S1 binding mode of diaminoethylphosphonic and phosphinic acids, selective inhibitors of alanine aminopeptidases.

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http://www.wikidata.org/entity/Q36902177

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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name

A structural insight into the ...... rs of alanine aminopeptidases.

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type

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A structural insight into the ...... rs of alanine aminopeptidases.

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A structural insight into the ...... rs of alanine aminopeptidases.

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P1476

A structural insight into the ...... rs of alanine aminopeptidases.

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P2093

Andrzej Joachimiak

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Artur Mucha

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Bogusław Nocek

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P2860

Crystal structure of aminopeptidase N from human pathogen Neisseria meningitidis

The X-ray Crystal Structure of Human Aminopeptidase N Reveals a Novel Dimer and the Basis for Peptide Processing

Discovery of α,β- and α,γ-diamino acid scaffolds for the inhibition of M1 family aminopeptidases

Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 A resolution in a new crystal form

Aminopeptidase fingerprints, an integrated approach for identification of good substrates and optimal inhibitors.

Aminopeptidase N1 (EtAPN1), an M1 metalloprotease of the apicomplexan parasite Eimeria tenella, participates in parasite development.

Aminopeptidase N (CD13) as a target for cancer chemotherapy.

Fingerprinting the substrate specificity of M1 and M17 aminopeptidases of human malaria, Plasmodium falciparum.

An integrated approach to the ligand binding specificity of Neisseria meningitidis M1 alanine aminopeptidase by fluorogenic substrate profiling, inhibitory studies and molecular modeling.

Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.

P304

187-196

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scholarly article

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10.1016/J.EJMECH.2016.04.018

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P478

117

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Łukasz Berlicki

Malgorzata Pawelczak

Ewelina Węglarz-Tomczak

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2016-04-09T00:00:00Z

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27100031

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4867306

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A structural insight into the P1S1 binding mode of diaminoethylphosphonic and phosphinic acids, selective inhibitors of alanine aminopeptidases.

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P2860

P2860

A structural insight into the P1S1 binding mode of diaminoethylphosphonic and phosphinic acids, selective inhibitors of alanine aminopeptidases.

description

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type

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P1433

P1476

P2093

P2860

P304

P31

P356

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P478

P50

P577

P698

P932