Role of the P2 residue of human alpha 1-antitrypsin in determining target protease specificity.

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Role of the P2 residue of human alpha 1-antitrypsin in determining target protease specificity.

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2017 nî lūn-bûn

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2017年の論文

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2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

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2017年論文

@zh-tw

2017年论文

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2017年论文

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2017年论文

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Role of the P2 residue of huma ...... g target protease specificity.

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Role of the P2 residue of huma ...... g target protease specificity.

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Role of the P2 residue of huma ...... g target protease specificity.

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P1476

Role of the P2 residue of huma ...... ng target protease specificity

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P2093

Hye-Shin Chung

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Ji-Sun Kim

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Sang Mee Lee

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P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Structure of a serpin-protease complex shows inhibition by deformation

Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase

An overview of the serpin superfamily

A 2.1 A resolution structure of an uncleaved alpha(1)-antitrypsin shows variability of the reactive center and other loops

UCSF Chimera--a visualization system for exploratory research and analysis

On the size of the active site in proteases. I. Papain

Serpin structure, mechanism, and function

The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature

Serpin structure, function and dysfunction.

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e0185074

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scholarly article

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10.1371/JOURNAL.PONE.0185074

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English

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P478

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Soon Jae Park

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2017-09-18T00:00:00Z

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28922398

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5602671

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