Morris VK - Search Results

1

Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16^INK4A.

Göbl C, Morris VK, van Dam L, Visscher M, Polderman PE, Hartlmüller C, de Ruiter H, Hora M, Liesinger L, Birner-Gruenberger R, Vos HR, Reif B, Madl T, Dansen TB. Göbl C, et al. Among authors: morris vk. Redox Biol. 2020 Jan;28:101316. doi: 10.1016/j.redox.2019.101316. Epub 2019 Sep 3. Redox Biol. 2020. PMID: 31539802 Free PMC article.

2

Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains.

Hora M, Carballo-Pacheco M, Weber B, Morris VK, Wittkopf A, Buchner J, Strodel B, Reif B. Hora M, et al. Among authors: morris vk. Sci Rep. 2017 Jan 27;7:41515. doi: 10.1038/srep41515. Sci Rep. 2017. PMID: 28128355 Free PMC article.

3

MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors.

Hora M, Sarkar R, Morris V, Xue K, Prade E, Harding E, Buchner J, Reif B. Hora M, et al. PLoS One. 2017 Jul 26;12(7):e0181799. doi: 10.1371/journal.pone.0181799. eCollection 2017. PLoS One. 2017. PMID: 28746363 Free PMC article.

4

The neuronal S100B protein is a calcium-tuned suppressor of amyloid-β aggregation.

Cristóvão JS, Morris VK, Cardoso I, Leal SS, Martínez J, Botelho HM, Göbl C, David R, Kierdorf K, Alemi M, Madl T, Fritz G, Reif B, Gomes CM. Cristóvão JS, et al. Among authors: morris vk. Sci Adv. 2018 Jun 29;4(6):eaaq1702. doi: 10.1126/sciadv.aaq1702. eCollection 2018 Jun. Sci Adv. 2018. PMID: 29963623 Free PMC article.

5

Amyloid formation and depolymerization of tumor suppressor p16^INK4a are regulated by a thiol-dependent redox mechanism.

Heath SG, Gray SG, Hamzah EM, O'Connor KM, Bozonet SM, Botha AD, de Cordovez P, Magon NJ, Naughton JD, Goldsmith DLW, Schwartfeger AJ, Sunde M, Buell AK, Morris VK, Göbl C. Heath SG, et al. Among authors: morris vk. Nat Commun. 2024 Jul 1;15(1):5535. doi: 10.1038/s41467-024-49581-7. Nat Commun. 2024. PMID: 38951545 Free PMC article.

6

Probing transient non-native states in amyloid beta fiber elongation by NMR.

Brender JR , Ghosh A , Kotler SA , Krishnamoorthy J , Bera S , Morris V , Sil TB , Garai K , Reif B , Bhunia A , Ramamoorthy A . Brender JR , et al. Chem Commun (Camb). 2019 Apr 11;55(31):4483-4486. doi: 10.1039/c9cc01067j. Chem Commun (Camb). 2019. PMID: 30917192 Free PMC article.

7

Analysis of the structure and conformational states of DewA gives insight into the assembly of the fungal hydrophobins.

Morris VK, Kwan AH, Sunde M. Morris VK, et al. J Mol Biol. 2013 Jan 23;425(2):244-56. doi: 10.1016/j.jmb.2012.10.021. Epub 2012 Nov 5. J Mol Biol. 2013. PMID: 23137797

8

The Cys3-Cys4 loop of the hydrophobin EAS is not required for rodlet formation and surface activity.

Kwan AH, Macindoe I, Vukasin PV, Morris VK, Kass I, Gupte R, Mark AE, Templeton MD, Mackay JP, Sunde M. Kwan AH, et al. Among authors: morris vk. J Mol Biol. 2008 Oct 10;382(3):708-20. doi: 10.1016/j.jmb.2008.07.034. Epub 2008 Jul 22. J Mol Biol. 2008. PMID: 18674544

9

Solid-state NMR spectroscopy of functional amyloid from a fungal hydrophobin: a well-ordered β-sheet core amidst structural heterogeneity.

Morris VK, Linser R, Wilde KL, Duff AP, Sunde M, Kwan AH. Morris VK, et al. Angew Chem Int Ed Engl. 2012 Dec 7;51(50):12621-5. doi: 10.1002/anie.201205625. Epub 2012 Nov 4. Angew Chem Int Ed Engl. 2012. PMID: 23125123

10

Formation of amphipathic amyloid monolayers from fungal hydrophobin proteins.

Morris VK, Sunde M. Morris VK, et al. Methods Mol Biol. 2013;996:119-29. doi: 10.1007/978-1-62703-354-1_7. Methods Mol Biol. 2013. PMID: 23504421

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