Uversky VN - Search Results

1

Structures of the Wild-Type and S59L Mutant CHCHD10 Proteins Important in Amyotrophic Lateral Sclerosis-Frontotemporal Dementia.

Alici H, Uversky VN, Kang DE, Woo JA, Coskuner-Weber O. Alici H, et al. Among authors: uversky vn. ACS Chem Neurosci. 2022 Apr 20;13(8):1273-1280. doi: 10.1021/acschemneuro.2c00011. Epub 2022 Mar 29. ACS Chem Neurosci. 2022. PMID: 35349255

2

Intrinsic disorder in proteins involved in amyotrophic lateral sclerosis.

Santamaria N, Alhothali M, Alfonso MH, Breydo L, Uversky VN. Santamaria N, et al. Among authors: uversky vn. Cell Mol Life Sci. 2017 Apr;74(7):1297-1318. doi: 10.1007/s00018-016-2416-6. Epub 2016 Nov 12. Cell Mol Life Sci. 2017. PMID: 27838743 Free PMC article.

3

The roles of intrinsic disorder-based liquid-liquid phase transitions in the "Dr. Jekyll-Mr. Hyde" behavior of proteins involved in amyotrophic lateral sclerosis and frontotemporal lobar degeneration.

Uversky VN. Uversky VN. Autophagy. 2017;13(12):2115-2162. doi: 10.1080/15548627.2017.1384889. Epub 2017 Dec 17. Autophagy. 2017. PMID: 28980860 Free PMC article. Review.

4

Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.

Coskuner-Weber O, Uversky VN. Coskuner-Weber O, et al. Among authors: uversky vn. Int J Mol Sci. 2018 Jan 24;19(2):336. doi: 10.3390/ijms19020336. Int J Mol Sci. 2018. PMID: 29364151 Free PMC article. Review.

5

Alanine Scanning Effects on the Biochemical and Biophysical Properties of Intrinsically Disordered Proteins: A Case Study of the Histidine to Alanine Mutations in Amyloid-β₄₂.

Coskuner-Weber O, Uversky VN. Coskuner-Weber O, et al. Among authors: uversky vn. J Chem Inf Model. 2019 Feb 25;59(2):871-884. doi: 10.1021/acs.jcim.8b00926. Epub 2019 Feb 7. J Chem Inf Model. 2019. PMID: 30694660

6

Biophysical Elucidation of Amyloid Fibrillation Inhibition and Prevention of Secondary Nucleation by Cholic Acid: An Unexplored Function of Cholic Acid.

Majid N, Siddiqi MK, Khan AN, Shabnam S, Malik S, Alam A, Uversky VN, Khan RH. Majid N, et al. Among authors: uversky vn. ACS Chem Neurosci. 2019 Nov 20;10(11):4704-4715. doi: 10.1021/acschemneuro.9b00482. Epub 2019 Oct 29. ACS Chem Neurosci. 2019. PMID: 31661243

7

Epitope region identification challenges of intrinsically disordered proteins in neurodegenerative diseases: Secondary structure dependence of α-synuclein on simulation techniques and force field parameters.

Mandaci SY, Caliskan M, Sariaslan MF, Uversky VN, Coskuner-Weber O. Mandaci SY, et al. Among authors: uversky vn. Chem Biol Drug Des. 2020 Jul;96(1):659-667. doi: 10.1111/cbdd.13662. Epub 2020 Jan 20. Chem Biol Drug Des. 2020. PMID: 31903719

8

Current Challenges and Limitations in the Studies of Intrinsically Disordered Proteins in Neurodegenerative Diseases by Computer Simulations.

Akbayrak IY, Caglayan SI, Ozcan Z, Uversky VN, Coskuner-Weber O. Akbayrak IY, et al. Among authors: uversky vn. Curr Alzheimer Res. 2020;17(9):805-818. doi: 10.2174/1567205017666201109094908. Curr Alzheimer Res. 2020. PMID: 33167839 Review.

9

Secondary structure dependence of amyloid-β(1-40) on simulation techniques and force field parameters.

Caliskan M, Mandaci SY, Uversky VN, Coskuner-Weber O. Caliskan M, et al. Among authors: uversky vn. Chem Biol Drug Des. 2021 May;97(5):1100-1108. doi: 10.1111/cbdd.13830. Epub 2021 Feb 22. Chem Biol Drug Des. 2021. PMID: 33580600

10

Structures of MERS-CoV macro domain in aqueous solution with dynamics: Impacts of parallel tempering simulation techniques and CHARMM36m and AMBER99SB force field parameters.

Akbayrak IY, Caglayan SI, Durdagi S, Kurgan L, Uversky VN, Ulver B, Dervisoğlu H, Haklidir M, Hasekioglu O, Coskuner-Weber O. Akbayrak IY, et al. Among authors: uversky vn. Proteins. 2021 Oct;89(10):1289-1299. doi: 10.1002/prot.26150. Epub 2021 May 26. Proteins. 2021. PMID: 34008220 Free PMC article.

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