Paulistine--The Functional Duality of a Wasp Venom Peptide Toxin.

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Paulistine--The Functional Duality of a Wasp Venom Peptide Toxin.

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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

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Paulistine--The Functional Duality of a Wasp Venom Peptide Toxin.

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Paulistine--The Functional Duality of a Wasp Venom Peptide Toxin.

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Paulistine--The Functional Duality of a Wasp Venom Peptide Toxin.

@en

Paulistine--The Functional Duality of a Wasp Venom Peptide Toxin.

@nl

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Paulistine--The Functional Duality of a Wasp Venom Peptide Toxin.

@en

Paulistine--The Functional Duality of a Wasp Venom Peptide Toxin.

@nl

P1476

Paulistine--The Functional Duality of a Wasp Venom Peptide Toxin.

@en

P2093

Bibiana Monson de Souza

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Helen Andrade Arcuri

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

Mario Sergio Palma

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

Nathalia Baptista Dias

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

Paulo Cesar Gomes

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P2860

Human cyclooxygenase-2 cDNA

Comparison between prostaglandin E1 and epoprostenol (prostacyclin) in infants after heart surgery.

Human cyclooxygenase-2 is a sequence homodimer that functions as a conformational heterodimer

Differential sensitivity and mechanism of inhibition of COX-2 oxygenation of arachidonic acid and 2-arachidonoylglycerol by ibuprofen and mefenamic acid

PROCHECK: a program to check the stereochemical quality of protein structures

Structural insights into the stereochemistry of the cyclooxygenase reaction

A novel mechanism of cyclooxygenase-2 inhibition involving interactions with Ser-530 and Tyr-385

The novel benzopyran class of selective cyclooxygenase-2 inhibitors. Part 2: the second clinical candidate having a shorter and favorable human half-life

Oxicams Bind in a Novel Mode to the Cyclooxygenase Active Site via a Two-water-mediated H-bonding Network

The structural basis of aspirin activity inferred from the crystal structure of inactivated prostaglandin H2 synthase

P31

scholarly article

P356

10.3390/TOXINS8030061

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P433

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

P478

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

P50

Rodrigo Stabeli

Patrícia Brigatte

P577

2016-02-29T00:00:00Z

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P5875

296477600

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P698

26938560

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P921

venom

P932

4810206

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