000 01448 a2200397 4500
005 20250516082432.0
264 0 _c20120727
008 201207s 0 0 eng d
022 _a1520-5126
024 7 _a10.1021/ja300094r
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aMeier, Franziska
245 0 0 _aSemisynthetic, site-specific ubiquitin modification of α-synuclein reveals differential effects on aggregation.
_h[electronic resource]
260 _bJournal of the American Chemical Society
_cMar 2012
300 _a5468-71 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
650 0 4 _aAmino Acid Sequence
650 0 4 _aDisulfides
_xchemistry
650 0 4 _aHumans
650 0 4 _aModels, Molecular
650 0 4 _aMolecular Sequence Data
650 0 4 _aParkinson Disease
_xmetabolism
650 0 4 _aProtein Conformation
650 0 4 _aUbiquitin
_xchemistry
650 0 4 _aUbiquitination
650 0 4 _aalpha-Synuclein
_xchemistry
700 1 _aAbeywardana, Tharindumala
700 1 _aDhall, Abhinav
700 1 _aMarotta, Nicholas P
700 1 _aVarkey, Jobin
700 1 _aLangen, Ralf
700 1 _aChatterjee, Champak
700 1 _aPratt, Matthew R
773 0 _tJournal of the American Chemical Society
_gvol. 134
_gno. 12
_gp. 5468-71
856 4 0 _uhttps://doi.org/10.1021/ja300094r
_zAvailable from publisher's website
999 _c21609857
_d21609857