Quinlan RA - Search Results

1

Alexander-disease mutation of GFAP causes filament disorganization and decreased solubility of GFAP.

Hsiao VC, Tian R, Long H, Der Perng M, Brenner M, Quinlan RA, Goldman JE. Hsiao VC, et al. Among authors: quinlan ra. J Cell Sci. 2005 May 1;118(Pt 9):2057-65. doi: 10.1242/jcs.02339. Epub 2005 Apr 19. J Cell Sci. 2005. PMID: 15840648

2

Oligomers of mutant glial fibrillary acidic protein (GFAP) Inhibit the proteasome system in alexander disease astrocytes, and the small heat shock protein alphaB-crystallin reverses the inhibition.

Tang G, Perng MD, Wilk S, Quinlan R, Goldman JE. Tang G, et al. J Biol Chem. 2010 Apr 2;285(14):10527-37. doi: 10.1074/jbc.M109.067975. Epub 2010 Jan 28. J Biol Chem. 2010. PMID: 20110364 Free PMC article.

3

GFAP and its role in Alexander disease.

Quinlan RA, Brenner M, Goldman JE, Messing A. Quinlan RA, et al. Exp Cell Res. 2007 Jun 10;313(10):2077-87. doi: 10.1016/j.yexcr.2007.04.004. Epub 2007 Apr 6. Exp Cell Res. 2007. PMID: 17498694 Free PMC article. Review.

4

Glial fibrillary acidic protein mutations in infantile, juvenile, and adult forms of Alexander disease.

Li R, Johnson AB, Salomons G, Goldman JE, Naidu S, Quinlan R, Cree B, Ruyle SZ, Banwell B, D'Hooghe M, Siebert JR, Rolf CM, Cox H, Reddy A, Gutiérrez-Solana LG, Collins A, Weller RO, Messing A, van der Knaap MS, Brenner M. Li R, et al. Ann Neurol. 2005 Mar;57(3):310-26. doi: 10.1002/ana.20406. Ann Neurol. 2005. PMID: 15732097

5

The Alexander disease-causing glial fibrillary acidic protein mutant, R416W, accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of alpha B-crystallin and HSP27.

Der Perng M, Su M, Wen SF, Li R, Gibbon T, Prescott AR, Brenner M, Quinlan RA. Der Perng M, et al. Among authors: quinlan ra. Am J Hum Genet. 2006 Aug;79(2):197-213. doi: 10.1086/504411. Epub 2006 Jun 12. Am J Hum Genet. 2006. PMID: 16826512 Free PMC article.

6

Site-specific phosphorylation and caspase cleavage of GFAP are new markers of Alexander disease severity.

Battaglia RA, Beltran AS, Delic S, Dumitru R, Robinson JA, Kabiraj P, Herring LE, Madden VJ, Ravinder N, Willems E, Newman RA, Quinlan RA, Goldman JE, Perng MD, Inagaki M, Snider NT. Battaglia RA, et al. Among authors: quinlan ra. Elife. 2019 Nov 4;8:e47789. doi: 10.7554/eLife.47789. Elife. 2019. PMID: 31682229 Free PMC article.

7

The specificity of the interaction between αB-crystallin and desmin filaments and its impact on filament aggregation and cell viability.

Elliott JL, Der Perng M, Prescott AR, Jansen KA, Koenderink GH, Quinlan RA. Elliott JL, et al. Among authors: quinlan ra. Philos Trans R Soc Lond B Biol Sci. 2013 Mar 25;368(1617):20120375. doi: 10.1098/rstb.2012.0375. Print 2013 May 5. Philos Trans R Soc Lond B Biol Sci. 2013. PMID: 23530264 Free PMC article.

8

Neuronal diseases: small heat shock proteins calm your nerves.

Der Perng M, Quinlan RA. Der Perng M, et al. Among authors: quinlan ra. Curr Biol. 2004 Aug 10;14(15):R625-6. doi: 10.1016/j.cub.2004.07.047. Curr Biol. 2004. PMID: 15296780 Free article. Review.

9

αB-crystallin is a sensor for assembly intermediates and for the subunit topology of desmin intermediate filaments.

Sharma S, Conover GM, Elliott JL, Der Perng M, Herrmann H, Quinlan RA. Sharma S, et al. Among authors: quinlan ra. Cell Stress Chaperones. 2017 Jul;22(4):613-626. doi: 10.1007/s12192-017-0788-7. Epub 2017 May 3. Cell Stress Chaperones. 2017. PMID: 28470624 Free PMC article.

10

Intermediate filament interactions can be altered by HSP27 and alphaB-crystallin.

Perng MD, Cairns L, van den IJssel P, Prescott A, Hutcheson AM, Quinlan RA. Perng MD, et al. Among authors: quinlan ra. J Cell Sci. 1999 Jul;112 ( Pt 13):2099-112. doi: 10.1242/jcs.112.13.2099. J Cell Sci. 1999. PMID: 10362540

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