QM/MM MD and free energy simulations of G9a-like protein (GLP) and its mutants: understanding the factors that determine the product specificity (Q34280128)

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English	QM/MM MD and free energy simulations of G9a-like protein (GLP) and its mutants: understanding the factors that determine the product specificity	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

1 August 2017

QM/MM MD and free energy simulations of G9a-like protein (GLP) and its mutants: understanding the factors that determine the product specificity (English)

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Europe PubMed Central

PubMed publication ID

1 August 2017

author name string

Yuzhuo Chu

1

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

Jianzhuang Yao

2

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Europe PubMed Central

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1 August 2017

Hong Guo

3

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Europe PubMed Central

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1 August 2017

language of work or name

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publication date

18 May 2012

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Europe PubMed Central

PubMed publication ID

1 August 2017

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Europe PubMed Central

PubMed publication ID

1 August 2017

7

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Europe PubMed Central

PubMed publication ID

1 August 2017

5

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

e37674

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

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Creative Commons Attribution 4.0 International

18 May 2012

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April 2022 Public Data File from Crossref

copyright status

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All-atom empirical potential for molecular modeling and dynamics studies of proteins

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Modeling a new water channel that allows SET9 to dimethylate p53

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Structural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding

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SET7/9 Catalytic Mutants Reveal the Role of Active Site Water Molecules in Lysine Multiple Methylation

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6 July 2018

Structural Biology of Human H3K9 Methyltransferases

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6 July 2018

Structural origins for the product specificity of SET domain protein methyltransferases

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Enzymatic mechanism and product specificity of SET-domain protein lysine methyltransferases

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How do SET-domain protein lysine methyltransferases achieve the methylation state specificity? Revisited by Ab initio QM/MM molecular dynamics simulations

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

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Mechanism of histone methylation catalyzed by protein lysine methyltransferase SET7/9 and origin of product specificity

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Ab initio quantum mechanical/molecular mechanical molecular dynamics simulation of enzyme catalysis: the case of histone lysine methyltransferase SET7/9.

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The diverse functions of histone lysine methylation

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

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Specificity and mechanism of the histone methyltransferase Pr-Set7.

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In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases

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6 July 2018

Structural basis for the product specificity of histone lysine methyltransferases

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6 July 2018

Structure of SET domain proteins: a new twist on histone methylation

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Structure and catalytic mechanism of the human histone methyltransferase SET7/9

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Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase

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The language of covalent histone modifications

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VMD: visual molecular dynamics

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Active site dynamics in protein molecules: a stochastic boundary molecular-dynamics approach.

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The epigenetic magic of histone lysine methylation.

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Reading signals on the nucleosome with a new nomenclature for modified histones

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Energy triplets for writing epigenetic marks: insights from QM/MM free-energy simulations of protein lysine methyltransferases

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Product specificity and mechanism of protein lysine methyltransferases: insights from the histone lysine methyltransferase SET8.

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21 January 2018

Catalytic mechanism and product specificity of the histone lysine methyltransferase SET7/9: an ab initio QM/MM-FE study with multiple initial structures.

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A combined quantum mechanical and molecular mechanical potential for molecular dynamics simulations

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CHARMM: A program for macromolecular energy, minimization, and dynamics calculations

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Comparison of simple potential functions for simulating liquid water

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THE weighted histogram analysis method for free-energy calculations on biomolecules. I. The method

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Communication: Conformation state diagram of polypeptides: a chain length induced α-β transition.

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Primers on chromatin

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Boxed molecular dynamics: a simple and general technique for accelerating rare event kinetics and mapping free energy in large molecular systems

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10.1371/JOURNAL.PONE.0037674

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Europe PubMed Central

PubMed publication ID

1 August 2017

2012PLoSO...737674C

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PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

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