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Items: 1 to 20 of 216

1.

The Parkinson's disease-associated H50Q mutation accelerates α-Synuclein aggregation in vitro.

Ghosh D, Mondal M, Mohite GM, Singh PK, Ranjan P, Anoop A, Ghosh S, Jha NN, Kumar A, Maji SK.

Biochemistry. 2013 Oct 8;52(40):6925-7. doi: 10.1021/bi400999d. Epub 2013 Sep 23.

PMID:
24047453
2.

The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity.

Khalaf O, Fauvet B, Oueslati A, Dikiy I, Mahul-Mellier AL, Ruggeri FS, Mbefo MK, Vercruysse F, Dietler G, Lee SJ, Eliezer D, Lashuel HA.

J Biol Chem. 2014 Aug 8;289(32):21856-76. doi: 10.1074/jbc.M114.553297. Epub 2014 Jun 16.

3.

The newly discovered Parkinson's disease associated Finnish mutation (A53E) attenuates α-synuclein aggregation and membrane binding.

Ghosh D, Sahay S, Ranjan P, Salot S, Mohite GM, Singh PK, Dwivedi S, Carvalho E, Banerjee R, Kumar A, Maji SK.

Biochemistry. 2014 Oct 21;53(41):6419-21. doi: 10.1021/bi5010365. Epub 2014 Oct 10.

PMID:
25268550
4.

Divergent effects of the H50Q and G51D SNCA mutations on the aggregation of α-synuclein.

Rutherford NJ, Moore BD, Golde TE, Giasson BI.

J Neurochem. 2014 Dec;131(6):859-67. doi: 10.1111/jnc.12806. Epub 2014 Jul 21.

5.

Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid.

Conway KA, Harper JD, Lansbury PT Jr.

Biochemistry. 2000 Mar 14;39(10):2552-63.

PMID:
10704204
6.

Alteration of Structure and Aggregation of α-Synuclein by Familial Parkinson's Disease Associated Mutations.

Sahay S, Ghosh D, Singh PK, Maji SK.

Curr Protein Pept Sci. 2017;18(7):656-676. doi: 10.2174/1389203717666160314151706. Review.

PMID:
26972727
7.

The Involvement of His50 during Protein Disulfide Isomerase Binding Is Essential for Inhibiting α-Syn Fibril Formation.

Ranjan P, Kumar A.

Biochemistry. 2016 May 17;55(19):2677-80. doi: 10.1021/acs.biochem.6b00280. Epub 2016 May 6.

PMID:
27142583
8.

Defective membrane interactions of familial Parkinson's disease mutant A30P alpha-synuclein.

Jo E, Fuller N, Rand RP, St George-Hyslop P, Fraser PE.

J Mol Biol. 2002 Jan 25;315(4):799-807.

PMID:
11812148
9.

Aggregation-defective alpha-synuclein mutants inhibit the fibrillation of Parkinson's disease-linked alpha-synuclein variants.

Koo HJ, Choi MY, Im H.

Biochem Biophys Res Commun. 2009 Aug 14;386(1):165-9. doi: 10.1016/j.bbrc.2009.06.002. Epub 2009 Jun 6.

PMID:
19501571
10.
11.

Formation of a high affinity lipid-binding intermediate during the early aggregation phase of alpha-synuclein.

Smith DP, Tew DJ, Hill AF, Bottomley SP, Masters CL, Barnham KJ, Cappai R.

Biochemistry. 2008 Feb 5;47(5):1425-34. doi: 10.1021/bi701522m. Epub 2008 Jan 8.

PMID:
18179253
12.

The H50Q mutation induces a 10-fold decrease in the solubility of α-synuclein.

Porcari R, Proukakis C, Waudby CA, Bolognesi B, Mangione PP, Paton JF, Mullin S, Cabrita LD, Penco A, Relini A, Verona G, Vendruscolo M, Stoppini M, Tartaglia GG, Camilloni C, Christodoulou J, Schapira AH, Bellotti V.

J Biol Chem. 2015 Jan 23;290(4):2395-404. doi: 10.1074/jbc.M114.610527. Epub 2014 Dec 10.

13.

Altered ion channel formation by the Parkinson's-disease-linked E46K mutant of alpha-synuclein is corrected by GM3 but not by GM1 gangliosides.

Di Pasquale E, Fantini J, Chahinian H, Maresca M, Taïeb N, Yahi N.

J Mol Biol. 2010 Mar 19;397(1):202-18. doi: 10.1016/j.jmb.2010.01.046. Epub 2010 Jan 28.

PMID:
20114052
14.

The remarkable conformational plasticity of alpha-synuclein: blessing or curse?

Deleersnijder A, Gerard M, Debyser Z, Baekelandt V.

Trends Mol Med. 2013 Jun;19(6):368-77. doi: 10.1016/j.molmed.2013.04.002. Epub 2013 May 3. Review.

PMID:
23648364
15.

Copper Binding and Subsequent Aggregation of α-Synuclein Are Modulated by N-Terminal Acetylation and Ablated by the H50Q Missense Mutation.

Mason RJ, Paskins AR, Dalton CF, Smith DP.

Biochemistry. 2016 Aug 30;55(34):4737-41. doi: 10.1021/acs.biochem.6b00708. Epub 2016 Aug 18.

PMID:
27517125
16.

Site-specific fluorescence dynamics of α-synuclein fibrils using time-resolved fluorescence studies: effect of familial Parkinson's disease-associated mutations.

Sahay S, Anoop A, Krishnamoorthy G, Maji SK.

Biochemistry. 2014 Feb 11;53(5):807-9. doi: 10.1021/bi401543z. Epub 2014 Jan 27.

PMID:
24450731
17.

A sensitive assay reveals structural requirements for α-synuclein fibril growth.

Dhavale DD, Tsai C, Bagchi DP, Engel LA, Sarezky J, Kotzbauer PT.

J Biol Chem. 2017 Jun 2;292(22):9034-9050. doi: 10.1074/jbc.M116.767053. Epub 2017 Apr 3.

PMID:
28373279
18.

Structures of the E46K mutant-type α-synuclein protein and impact of E46K mutation on the structures of the wild-type α-synuclein protein.

Wise-Scira O, Dunn A, Aloglu AK, Sakallioglu IT, Coskuner O.

ACS Chem Neurosci. 2013 Mar 20;4(3):498-508. doi: 10.1021/cn3002027. Epub 2013 Jan 30.

19.

Oligomers of Parkinson's Disease-Related α-Synuclein Mutants Have Similar Structures but Distinctive Membrane Permeabilization Properties.

Stefanovic AN, Lindhoud S, Semerdzhiev SA, Claessens MM, Subramaniam V.

Biochemistry. 2015 May 26;54(20):3142-50. doi: 10.1021/bi501369k. Epub 2015 May 14.

PMID:
25909158
20.

The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of α-synuclein, and enhances its secretion and nuclear localization in cells.

Fares MB, Ait-Bouziad N, Dikiy I, Mbefo MK, Jovičić A, Kiely A, Holton JL, Lee SJ, Gitler AD, Eliezer D, Lashuel HA.

Hum Mol Genet. 2014 Sep 1;23(17):4491-509. doi: 10.1093/hmg/ddu165. Epub 2014 Apr 11.

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