Arginase Structure and Inhibition: Catalytic Site Plasticity Reveals New Modulation Possibilities.

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Arginase Structure and Inhibition: Catalytic Site Plasticity Reveals New Modulation Possibilities.

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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

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2017年論文

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2017年論文

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2017年論文

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2017年論文

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2017年论文

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2017年论文

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2017年论文

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Arginase Structure and Inhibit ...... New Modulation Possibilities.

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Arginase Structure and Inhibit ...... New Modulation Possibilities.

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Arginase Structure and Inhibit ...... New Modulation Possibilities.

@en

Arginase Structure and Inhibit ...... New Modulation Possibilities.

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Arginase Structure and Inhibit ...... New Modulation Possibilities.

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Arginase Structure and Inhibit ...... New Modulation Possibilities.

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P1476

Arginase Structure and Inhibit ...... New Modulation Possibilities.

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P2093

Christian Omieczynski

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Julien R C Prévost

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Sabine Teuchert

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P2860

Canonical dynamics: Equilibrium phase-space distributions

Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response.

Improved side-chain torsion potentials for the Amber ff99SB protein force field

Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster

Arginase-boronic acid complex highlights a physiological role in erectile function

Probing erectile function: S-(2-boronoethyl)-L-cysteine binds to arginase as a transition state analogue and enhances smooth muscle relaxation in human penile corpus cavernosum

Human arginase II: crystal structure and physiological role in male and female sexual arousal

Design of amino acid sulfonamides as transition-state analogue inhibitors of arginase

Inhibition of human arginase I by substrate and product analogues

2-Aminoimidazole Amino Acids as Inhibitors of the Binuclear Manganese Metalloenzyme Human Arginase I

P2888

s41598-017-13366-4

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13616

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scholarly article

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10.1038/S41598-017-13366-4

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English

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P478

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P577

2017-10-19T00:00:00Z

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P6179

1092212931

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P698

29051526

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P932

5648838

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