The influence of angiotensin converting enzyme mutations on the kinetics and dynamics of N-domain selective inhibition.

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Crystal structures of sampatrilat and sampatrilat-Asp in complex with human ACE - a molecular basis for domain selectivity.

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The influence of angiotensin converting enzyme mutations on the kinetics and dynamics of N-domain selective inhibition.

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http://www.wikidata.org/entity/Q38820520

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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

The influence of angiotensin c ...... N-domain selective inhibition.

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type

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The influence of angiotensin c ...... N-domain selective inhibition.

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The influence of angiotensin c ...... N-domain selective inhibition.

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P1476

The influence of angiotensin c ...... N-domain selective inhibition

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P2093

Brian T Sewell

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Edward D Sturrock

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P2860

Canonical dynamics: Equilibrium phase-space distributions

PHENIX: a comprehensive Python-based system for macromolecular structure solution

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Comparison of simple potential functions for simulating liquid water

ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis

Probing the basis of domain-dependent inhibition using novel ketone inhibitors of Angiotensin-converting enzyme

Fragment-based design for the development of N-domain-selective angiotensin-1-converting enzyme inhibitors

VMD: visual molecular dynamics

Features and development of Coot

A new antifibrotic target of Ac-SDKP: inhibition of myofibroblast differentiation in rat lung with silicosis

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scholarly article

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10.1111/FEBS.13900

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English

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283

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Lizelle Lubbe

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2016-10-05T00:00:00Z

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27636235

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The influence of angiotensin converting enzyme mutations on the kinetics and dynamics of N-domain selective inhibition.

about

P2860

P2860

The influence of angiotensin converting enzyme mutations on the kinetics and dynamics of N-domain selective inhibition.

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