Membrane Allostery and Unique Hydrophobic Sites Promote Enzyme Substrate Specificity.

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Membrane Allostery and Unique Hydrophobic Sites Promote Enzyme Substrate Specificity.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

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2018年學術文章

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Membrane Allostery and Unique Hydrophobic Sites Promote Enzyme Substrate Specificity.

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Membrane Allostery and Unique Hydrophobic Sites Promote Enzyme Substrate Specificity.

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Membrane Allostery and Unique Hydrophobic Sites Promote Enzyme Substrate Specificity.

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Membrane Allostery and Unique Hydrophobic Sites Promote Enzyme Substrate Specificity.

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Membrane Allostery and Unique Hydrophobic Sites Promote Enzyme Substrate Specificity.

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Membrane Allostery and Unique Hydrophobic Sites Promote Enzyme Substrate Specificity.

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P1476

Membrane Allostery and Unique Hydrophobic Sites Promote Enzyme Substrate Specificity.

@en

P2093

J Andrew McCammon

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

Yuan Chen

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

P2860

Group VIB Ca2+-independent phospholipase A2gamma promotes cellular membrane hydrolysis and prostaglandin production in a manner distinct from other intracellular phospholipases A2

Lipidomics reveals a remarkable diversity of lipids in human plasma

Membrane lipids: where they are and how they behave

Eicosanoid storm in infection and inflammation

Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention

Insertion of the Ca²⁺-independent phospholipase A₂ into a phospholipid bilayer via coarse-grained and atomistic molecular dynamics simulations

Development of Potent and Selective Inhibitors for Group VIA Calcium-Independent Phospholipase A2 Guided by Molecular Dynamics and Structure-Activity Relationships.

Inhibition of calcium-independent phospholipase A2 prevents arachidonic acid incorporation and phospholipid remodeling in P388D1 macrophages.

Imaging decreased brain docosahexaenoic acid metabolism and signaling in iPLA(2)β (VIA)-deficient mice.

Membranes serve as allosteric activators of phospholipase A2, enabling it to extract, bind, and hydrolyze phospholipid substrates

P304

3285-3291

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P31

scholarly article

P356

10.1021/JACS.7B12045

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P407

English

P433

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

P478

140

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P50

Edward A. Dennis

Varnavas D Mouchlis

P577

2018-02-26T00:00:00Z

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P698

29342349

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P921

hydrophobicity

P932

5846079

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