Chemical Bypass of General Base Catalysis in Hedgehog Protein Cholesterolysis Using a Hyper-Nucleophilic Substrate.

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Chemical Bypass of General Base Catalysis in Hedgehog Protein Cholesterolysis Using a Hyper-Nucleophilic Substrate.

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2017 nî lūn-bûn

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2017年学术文章

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Chemical Bypass of General Bas ...... Hyper-Nucleophilic Substrate.

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Chemical Bypass of General Bas ...... Hyper-Nucleophilic Substrate.

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Chemical Bypass of General Bas ...... Hyper-Nucleophilic Substrate.

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Chemical Bypass of General Bas ...... Hyper-Nucleophilic Substrate.

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Chemical Bypass of General Bas ...... Hyper-Nucleophilic Substrate.

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Chemical Bypass of General Bas ...... Hyper-Nucleophilic Substrate.

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P1476

Chemical Bypass of General Bas ...... a Hyper-Nucleophilic Substrate

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P2093

Daniel A Ciulla

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José-Luis Giner

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Michael T Jorgensen

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P2860

How does a symmetric dimer recognize an asymmetric substrate? A substrate complex of HIV-1 protease

Evaluation of the Catalytic Contribution from a Positioned General Base in Ketosteroid Isomerase

Crystal structure of a Hedgehog autoprocessing domain: homology between Hedgehog and self-splicing proteins

Cholesterol modification of hedgehog signaling proteins in animal development

Hedgehog patterning activity: role of a lipophilic modification mediated by the carboxy-terminal autoprocessing domain

Reactivity of intein thioesters: appending a functional group to a protein.

Förster resonance energy transfer-based cholesterolysis assay identifies a novel hedgehog inhibitor.

Novel lipid modifications of secreted protein signals.

Transition state analog inhibitors and enzyme catalysis.

A Single Aspartate Coordinates Two Catalytic Steps in Hedgehog Autoprocessing

P304

916-918

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scholarly article

P356

10.1021/JACS.7B05161

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P407

English

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140

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Brian P. Callahan

P577

2017-09-25T00:00:00Z

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P698

28930454

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P932

6054137

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