Endothioxopeptides: A conformational overview. - Wikidata - wikimedia - TriplyDB

Endothioxopeptides: A conformational overview.

Endothioxopeptides: A conformational overview.

http://www.wikidata.org/entity/Q38880136

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Endothioxopeptides: A conformational overview.

http://www.wikidata.org/entity/Q38880136

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2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Endothioxopeptides: A conformational overview.

@en

type

label

Endothioxopeptides: A conformational overview.

@en

prefLabel

Endothioxopeptides: A conformational overview.

@en

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Endothioxopeptides: A conformational overview.

@en

P2093

Barbara Biondi

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

Claudio Toniolo

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

Fernando Formaggio

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

P2860

Sulfur incorporation generally improves Ricin inhibition in pterin-appended glycine-phenylalanine dipeptide mimics

Rapid nitrogen inversion pathway in the cis/trans isomerization of selenoxo peptide bonds.

Atomic polarizability dominates the electronic properties of peptide bonds upon thioxo or selenoxo substitution.

Modulation of the peptide backbone conformation by the selenoxo photoswitch.

A nearly isosteric photosensitive amide-backbone substitution allows enzyme activity switching in ribonuclease s.

cis/trans photoisomerization of secondary thiopeptide bonds.

Effect of thioxopeptide bonds on alpha-helix structure and stability.

Mapping of the modular closthioamide architecture reveals crucial motifs of polythioamide antibiotics.

Thiomyristoyl peptides as cell-permeable Sirt6 inhibitors.

Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction

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697-713

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

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scholarly article

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10.1002/BIP.22899

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

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5

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106

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Cristina Peggion

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2016-06-29T00:00:00Z

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27353976

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