Home > Archive>Volume 15, Issue 10, 2015 >1727-1729. DOI:10.3980/j.issn.1672-5123.2015.10.13
PDF HTML XML Export Cite reminder
Influence of protein unwinding on conformational diseases
Author:
Fund Project:

National Natural Science Foundation of China(No. 81170834); National Natural Science Foundation of China(Youth Science Foundation)(No.81300748)

  • Article
    • | |
  • Metrics
    • |
  • Reference [26]
    • |
  • Related [20]
    • | | |
  • Comments
    Abstract:

    Protein unwinding includes advanced structure changes, the formation and fracture of disulfide bond and so on. Protein unwinding is widely involved in the physiological and pathological processes in vivo, of which advanced structure changes have important influences on the occurrence and development of conformational diseases. In order to seek for the common pathological mechanism and corresponding intervention approach, this review summarizes the current information about conformational diseases, especially about cataract and Alzheimer's disease.

    Reference
    1 Carrell RW, Lomas DA. Conformational disease.Lancet1997; 350(9071):134-138
    2 Lee C, Yu MH. Protein folding and diseases.Ksbmb 2005; 38(3):275-280
    3 Berrocal R, Vasquez V, Krs S, et al. α-synuclein misfolding versus aggregation relevance to parkinson's disease: critical assessment and modeling. Mol Neurobiol 2015; 51(3):1417-1431
    4 Chu Y, Kordower J. The prion hypothesis of Parkinson's disease. Curr Neurol Neurosci Rep 2015; 15(5):28
    5唐媛, 李春花, 张瑗. 蛋白质的二级结构预测研究进展. 现代生物医学进展 2013; 13(26):5180-5182
    6 Cohen AS, Calkins E. Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature 1959; 183(4669):1202-1203
    7 Sunde M, Serpell LC, Bartlam M, et al. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J Mol Biol 1997; 273(3):729-739
    8 Serpell LC, Blake CC, Fraser PE. Molecular structure of a fibrillar Alzheimer's A beta fragment. Biochemistry 2000; 39(43):13269-13275
    9 Francioso A, Punzi P, Boffi A, et al. β-sheet interfering molecules acting against β-amyloid aggregation and fibrillogenesis. Bioorg Med Chem 2015; 23(8):1671-1683
    10 Csermely P, Sandhu KS, Hazai E, et al. Disordered proteins and network disorder in network descriptions of protein structure, dynamics and function: hypotheses and a comprehensive review. Curr Protein Pept Sci 2012; 13(1):19-33
    11 Santucci R, Sinibaldi F, Fiorucci L. Protein folding, unfolding and misfolding: role played by intermediate States. Mini Rev Med Chem 2008; 8(1):57-62
    12胡红雨, 许根俊. 蛋白质的结构转换. 生物化学与生物物理进展 1999; 1:9-11
    13徐国恒. 二硫键与蛋白质的结构. 生物学通报 2010; 45(5):5-7
    14张可可, 竺向佳. 晶状体蛋白的外消旋化及其在白内障发病机制中的研究进展. 中华实验眼科杂志 2014; 32(6):563-567
    15 You D, Lee J, Kim J, et al. Effect of nitric oxide on conformational changes of ovalbumin accompanying self-assembly into non-disease-associated fibrils. Nitric Oxide 2015; 47:1-9
    16 Surguchev A, Surguchov A. Conformational diseases: looking into the eyes. Brain Res Bull 2010; 81(1):12-24
    17 Hipp MS, Park SH, Hartl FU. Proteostasis impairment in protein-misfolding and -aggregation diseases. Trends Cell Biol 2014; 24(9):506-514
    18 Duttler S, Pechmann S, Frydman J. Principles of cotranslational ubiquitination and quality control at the ribosome. Mol Cell 2013; 50(3):379-393
    19 Väliaho J, Faisal I, Ortutay C, et al. Characterization of all possible single-nucleotide change caused amino acid substitutions in the kinase domain of bruton tyrosine kinase. Hum Mutat 2015; 36(6):638-647
    20 Parthasarathy S, Inoue M, Xiao Y, et al. Structural insight into an Alzheimer's Brain-Derived Spherical Assembly of Amyloid β by Solid-State NMR. J Am Chem Soc 2015; 137(20):6480-6483
    21 Chakraborty S, Basu S. Structural insight into the mechanism of amyloid precursor protein recognition by β-secretase 1: a molecular dynamics study. Biophys Chem 2015; 202:1-12
    22 Berhanu W, Masunov A. Atomistic mechanism of polyphenol amyloid aggregation inhibitors: molecular dynamics study of curcumin, exifone, and myricetin interaction with the segment of tau peptide oligomer. J Biomol Struct Dyn 2015; 33(7):1399-1411
    23 Zhou Z, Xiao G. Conformational conversion of prion protein in prion diseases. ABBS 2013; 45(6):465-476
    24 Xie T,Yan C,Zhou R,et al. Crystal structure of the γ-secretase component nicastrin. Proc Natl Acad Sci USA 2014; 111(37):13349-13354
    25 付清, 耿宇, 张建荣,等. 二硫苏糖醇复合物对SD大鼠硒性白内障的抑制作用. 国际眼科杂志 2008; 8(9):1767-1769
    26李静, 薛炼, 张军,等. 叔丁醇治疗SD大鼠硒性白内障的疗效观察. 第二军医大学学报 2008; 29(9):1056-1059
    Cited by
    Comments
    Comments
    分享到微博
    Submit
Get Citation

Han-Xiao Ren, Qian Gao, Yin Jia,/et al.Influence of protein unwinding on conformational diseases. Guoji Yanke Zazhi( Int Eye Sci) 2015;15(10):1727-1729

Copy
Share
Article Metrics
  • Abstract:1707
  • PDF: 1244
  • HTML: 0
  • Cited by: 0
Publication History
  • Received:June 16,2015
  • Revised:September 08,2015
  • Online: September 25,2015
You are the 26184 Visitors
Governing Body：Department of Health, Provincial Government of Shaanxi, China
Organizer：Xi'an Medical Association of China
Address：Room 11707-08, Building 2, Unit 1, Wanda Plaza, No.8 Yanta North Road, Xi'an 710054, Shaanxi Province, China
Fax：(8629)82245172 Phone：(+8629)82245172/82210956
Email：ijopress@163.com
® 2025 All Rights Reserved   The terms of CC BY-NC-ND 4.0 are applicable to all open access content.