Selenopeptide analogs of EETI-II retain potent trypsin inhibitory activities.

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http://www.wikidata.org/entity/Q46220995

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2010 nî lūn-bûn

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2010年の論文

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年学术文章

@zh-my

2010年学术文章

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2010年學術文章

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2010年學術文章

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2010年學術文章

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name

Selenopeptide analogs of EETI-II retain potent trypsin inhibitory activities.

@en

Selenopeptide analogs of EETI-II retain potent trypsin inhibitory activities.

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type

Item

label

Selenopeptide analogs of EETI-II retain potent trypsin inhibitory activities.

@en

Selenopeptide analogs of EETI-II retain potent trypsin inhibitory activities.

@nl

prefLabel

Selenopeptide analogs of EETI-II retain potent trypsin inhibitory activities.

@en

Selenopeptide analogs of EETI-II retain potent trypsin inhibitory activities.

@nl

P1476

Selenopeptide analogs of EETI-II retain potent trypsin inhibitory activities

@en

P2093

Anna Jaśkiewicz

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

Grzegorz Bulaj

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

P2860

Use of restrained molecular dynamics in water to determine three-dimensional protein structure: prediction of the three-dimensional structure of Ecballium elaterium trypsin inhibitor II

The cystine knot of a squash-type protease inhibitor as a structural scaffold for Escherichia coli cell surface display of conformationally constrained peptides.

New binding specificities derived from Min-23, a small cystine-stabilized peptidic scaffold.

Conotoxins as research tools and drug leads.

Engineered cystine knot peptides that bind alphavbeta3, alphavbeta5, and alpha5beta1 integrins with low-nanomolar affinity.

Thermodynamics and kinetics of single residue replacements in avian ovomucoid third domains: effect on inhibitor interactions with serine proteinases.

Natural protein proteinase inhibitors and their interaction with proteinases.

Isosteric replacement of sulfur with other chalcogens in peptides and proteins.

Studies on deprotection of cysteine and selenocysteine side-chain protecting groups.

Site-specific effects of diselenide bridges on the oxidative folding of a cystine knot peptide, omega-selenoconotoxin GVIA.

P304

93-97

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P31

scholarly article

P356

10.1111/J.1747-0285.2010.01046.X

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P433

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

P478

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

P50

Krzysztof Rolka

Aleksandra Walewska

P577

2010-10-19T00:00:00Z

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

P698

20958922

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