Deciphering the Molecular Effects of Mutations on ATRX Cause ATRX Syndrome: A Molecular Dynamics Study-Reference-Cited by-同舟云学术

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Deciphering the Molecular Effects of Mutations on ATRX Cause ATRX Syndrome: A Molecular Dynamics Study

Published:2017-05-03 Issue:10 Volume:118 Page:3318-3327
ISSN:0730-2312
Container-title:Journal of Cellular Biochemistry
language:en
Short-container-title:J. Cell. Biochem.

Author:

Palaniappan Chandrasekaran¹,Ramalingam Rajasekaran¹^ORCID

Affiliation:

1. Department of BiotechnologyBioinformatics LabSchool of Biosciences and TechnologyVIT UniversityVellore632014Tamil NaduIndia

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/jcb.25984

Reference36 articles.

1. Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX

2. ATRX marks the inactive X chromosome (Xi) in somatic cells and during imprinted X chromosome inactivation in trophoblast stem cells

3. GROMACS: A message-passing parallel molecular dynamics implementation

4. The Protein Data Bank

5. Structural characterization of disease-causing mutations on SAP and the functional impact on the SLAM peptide: a molecular dynamics approach

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2. Mutation-Dependent Refolding of Prion Protein Unveils Amyloidogenic-Related Structural Ramifications: Insights from Molecular Dynamics Simulations;ACS Chemical Neuroscience;2021-07-23

3. In silico analysis of the tryptophan hydroxylase 2 (TPH2) protein variants related to psychiatric disorders;PLOS ONE;2020-03-02

4. Disassociation of β1-α1-β2 from the α2-α3 domain of prion protein (PrP) is a prerequisite for the conformational conversion of PrPC into PrPSc: Driven by the free energy landscape;International Journal of Biological Macromolecules;2019-09

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