Investigation of Structural Peculiarities of Smooth Muscle Titin Aggregates, Formed under Different In Vitro Conditions, by Small-Angle X-Ray Scattering and Fourier Transform Infrared Spectroscopy-Reference-Cited by-同舟云学术

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Investigation of Structural Peculiarities of Smooth Muscle Titin Aggregates, Formed under Different In Vitro Conditions, by Small-Angle X-Ray Scattering and Fourier Transform Infrared Spectroscopy

Published:2024-09-12 Issue: Volume: Page:
ISSN:0007-4888
Container-title:Bulletin of Experimental Biology and Medicine
language:en
Short-container-title:Bull Exp Biol Med

Author:

Timchenko M. A.,Timchenko A. A.,Kazakov A. S.,Vikhlyantsev I. M.,Bobyleva L. G.,Bobylev A. G.

Publisher

Springer Science and Business Media LLC

Link

https://link.springer.com/content/pdf/10.1007/s10517-024-06207-8.pdf

Reference20 articles.

1. Chiti F, Dobson CM. Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade. Annu. Rev. Biochem. 2017;86:27-68. https://doi.org/10.1146/annurev-biochem-061516-045115

2. Dobson CM. Protein folding and misfolding. Nature. 2003;426:884-890. https://doi.org/10.1038/nature02261

3. Fowler DM, Koulov AV, Alory-Jost C, Marks MS, Balch WE, Kelly JW. Functional amyloid formation within mammalian tissue. PLoS Biol. 2006;4(1):e6. https://doi.org/10.1371/journal.pbio.0040006

4. Yakupova EI, Bobyleva LG, Shumeyko SA, Vikhlyantsev IM, Bobylev AG. Amyloids: the history of toxicity and functionality. Biology (Basel). 2021;10(5):394. https://doi.org/10.3390/biology10050394

5. Maruyama K, Kimura S, Ohashi K, Kuwano Y. Connectin, an elastic protein of muscle. Identification of “titin” with connectin. J. Biochem. 1981;89(3):701-709. https://doi.org/10.1093/oxfordjournals.jbchem.a133249

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