Tautomeric state of alpha-sarcin histidines. Ndelta tautomers are a common feature in the active site of extracellular microbial ribonucleases.

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Fungal ribotoxins: molecular dissection of a family of natural killers.Tautomeric stabilities of 4-fluorohistidine shed new light on mechanistic experiments with labeled ribonuclease A.The ribotoxin restrictocin recognizes its RNA substrate by selective engagement of active site residues.

P2860

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P2860

Tautomeric state of alpha-sarcin histidines. Ndelta tautomers are a common feature in the active site of extracellular microbial ribonucleases.

Item

http://www.wikidata.org/entity/Q44277961

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年学术文章

@wuu

2003年学术文章

@zh

2003年学术文章

@zh-cn

2003年学术文章

@zh-hans

2003年学术文章

@zh-my

2003年学术文章

@zh-sg

2003年學術文章

@yue

2003年學術文章

@zh-hant

name

Tautomeric state of alpha-sarc ...... lular microbial ribonucleases.

@en

Tautomeric state of alpha-sarc ...... lular microbial ribonucleases.

@nl

type

Item

label

Tautomeric state of alpha-sarc ...... lular microbial ribonucleases.

@en

Tautomeric state of alpha-sarc ...... lular microbial ribonucleases.

@nl

prefLabel

Tautomeric state of alpha-sarc ...... lular microbial ribonucleases.

@en

Tautomeric state of alpha-sarc ...... lular microbial ribonucleases.

@nl

P1476

Tautomeric state of alpha-sarc ...... llular microbial ribonucleases

@en

P2093

Ma Flor García-Mayoral

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

Manuel Rico

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

P2860

The two faces of the Escherichia coli 23 S rRNA sarcin/ricin domain: the structure at 1.11 A resolution

The highly refined solution structure of the cytotoxic ribonuclease alpha-sarcin reveals the structural requirements for substrate recognition and ribonucleolytic activity

Ribonuclease T1 with free recognition and catalytic site: crystal structure analysis at 1.5 A resolution

Crystal structure of Ustilago sphaerogena ribonuclease U2 at 1.8 A resolution

Crystal structure of ribonuclease Ms (as a ribonuclease T1 homologue) complexed with a guanylyl-3',5'-cytidine analogue

Crystal structures of ribonuclease F1 of Fusarium moniliforme in its free form and in complex with 2'GMP

Insights into specificity of cleavage and mechanism of cell entry from the crystal structure of the highly specific Aspergillus ribotoxin, restrictocin

Limits of NMR structure determination using variable target function calculations: ribonuclease T1, a case study

Crystal structure of the ribosomal RNA domain essential for binding elongation factors

Ribotoxins are a more widespread group of proteins within the filamentous fungi than previously believed.

P304

197-201

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P31

scholarly article

P356

10.1016/S0014-5793(02)03844-9

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P407

English

P433

1-3

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P478

534

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P50

José G Gavilanes

Marta Bruix

Douglas V Laurents

Alvaro Martínez-del-Pozo

Jose Manuel Pérez-Cañadillas

P577

2003-01-01T00:00:00Z

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

P5875

247016602

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P698

12527386

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Tautomeric state of alpha-sarcin histidines. Ndelta tautomers are a common feature in the active site of extracellular microbial ribonucleases.

about

P2860

P2860

Tautomeric state of alpha-sarcin histidines. Ndelta tautomers are a common feature in the active site of extracellular microbial ribonucleases.

description

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P1433

P1476

P2093

P2860

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P356

P407

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P478

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P1476

P2093

P2860

P304

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P478

P50

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P698