Molecular dynamics simulations on human fibulin-4 mutants D203A and E126K reveal conformational changes in EGF domains potentially responsible for enhanced protease lability and impaired extracellular matrix assembly-Reference-Cited by-同舟云学术

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Molecular dynamics simulations on human fibulin-4 mutants D203A and E126K reveal conformational changes in EGF domains potentially responsible for enhanced protease lability and impaired extracellular matrix assembly

Published:2019-09 Issue:9 Volume:1867 Page:748-756
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Sasaki Takako,von der Mark Klaus,Lanig Harald

Funder

Deutsche Forschungsgemeinschaft

Japanese Ministry of Education, Culture, Sports, Science, and Technology

Cluster of Excellence Engineering of Advanced Materials

Central Institute for Scientific Computing ZISC

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference45 articles.

1. Fibulins: physiological and disease perspectives;Argraves;EMBO Rep.,2003

2. Fibulins: a versatile family of extracellular matrix proteins;Timpl;Nat. Rev. Mol. Cell Biol.,2003

3. A comparative analysis of the fibulin protein family. Biochemical characterization, binding interactions, and tissue localization;Kobayashi;J. Biol. Chem.,2007

4. Fibulins: multiple roles in matrix structures and tissue functions;de Vega;Cell. Mol. Life Sci. CMLS,2009

5. Sequence, recombinant expression and tissue localization of two novel extracellular matrix proteins, fibulin-3 and fibulin-4;Giltay;Matrix Biol. J. Int. Soc. Matrix Biol.,1999

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