Investigating d-lysine stereochemistry for epigenetic methylation, demethylation and recognition.

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Investigating d-lysine stereochemistry for epigenetic methylation, demethylation and recognition.

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2017 nî lūn-bûn

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2017年学术文章

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2017年学术文章

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Investigating d-lysine stereoc ...... demethylation and recognition.

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Investigating d-lysine stereoc ...... demethylation and recognition.

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Investigating d-lysine stereoc ...... demethylation and recognition.

@en

Investigating d-lysine stereoc ...... demethylation and recognition.

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Investigating d-lysine stereoc ...... demethylation and recognition.

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Investigating d-lysine stereoc ...... demethylation and recognition.

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P1476

Investigating d-lysine stereoc ...... demethylation and recognition

@en

P2093

Anthony Tumber

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Catrine Johansson

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Kiran Kumar

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Roman Belle

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Udo Oppermann

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P2860

Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification

Comparison of simple potential functions for simulating liquid water

How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers

SET domain protein lysine methyltransferases: Structure, specificity and catalysis.

Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect.

D-amino acid in elderly tissues.

Lysine succinylation and lysine malonylation in histones.

Molecular insights into the recognition of N-terminal histone modifications by the BRPF1 bromodomain.

Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins.

Structural Chemistry of Human SET Domain Protein Methyltransferases.

P304

13264-13267

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P31

scholarly article

P356

10.1039/C7CC08028J

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P407

English

P433

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

P478

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P50

Robert Paton

Christopher J. Schofield

P577

2017-12-01T00:00:00Z

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P698

29186216

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P932

6345366

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