Computational analysis of histidine mutations on the structural stability of human tyrosinases leading to albinism insurgence-Reference-Cited by-同舟云学术

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Computational analysis of histidine mutations on the structural stability of human tyrosinases leading to albinism insurgence

Published:2017 Issue:8 Volume:13 Page:1534-1544
ISSN:1742-206X
Container-title:Molecular BioSystems
language:en
Short-container-title:Mol. BioSyst.

Author:

Hassan Mubashir¹²³⁴⁵,Abbas Qamar¹²³⁴⁵,Raza Hussain¹²³⁴⁵,Moustafa Ahmed A.⁶⁷⁸⁹⁷,Seo Sung-Yum¹²³⁴⁵^ORCID

Affiliation:

1. Department of Biological Sciences

2. College of Natural Sciences

3. Kongju National University

4. Chungnam 32588

5. Republic of Korea

6. School of Social Sciences and Psychology

7. Western Sydney University

8. Australia

9. MARCS Institute for Brain and Behaviour

Abstract

Misfolding and structural alteration in proteins lead to serious malfunctions and cause various diseases in humans.

Publisher

Royal Society of Chemistry (RSC)

Subject

Molecular Biology,Biotechnology

Link

http://pubs.rsc.org/en/content/articlepdf/2017/MB/C7MB00211D

Reference57 articles.

1. The Protein-Folding Problem, 50 Years On

2. Detailed computational analysis revealed mutation V210I on PrP induced conformational conversion on β2–α2 loop and α2–α3

3. Mechanisms of protein-folding diseases at a glance

4. A three-dimensional model of mammalian tyrosinase active site accounting for loss of function mutations

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