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Nicholas P. Marotta
Researcher at University of Southern California
Publications - 10
Citations - 461
Nicholas P. Marotta is an academic researcher from University of Southern California. The author has contributed to research in topics: Protein aggregation & Synucleinopathies. The author has an hindex of 7, co-authored 8 publications receiving 354 citations. Previous affiliations of Nicholas P. Marotta include University of Pennsylvania.
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Journal ArticleDOI
O-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's disease
Nicholas P. Marotta,Yu Hsuan Lin,Yuka E. Lewis,Mark R. Ambroso,Balyn W. Zaro,Maxwell Taylor Roth,Don B. Arnold,Ralf Langen,Matthew R. Pratt +8 more
TL;DR: It is suggested that increasing O-GlcNAcylation may slow the progression of synucleinopathies and further support a general function for O- GlcNAc in preventing protein aggregation.
Journal ArticleDOI
Semisynthetic, Site-Specific Ubiquitin Modification of α-Synuclein Reveals Differential Effects on Aggregation
Franziska Meier,Tharindumala Abeywardana,Abhinav Dhall,Nicholas P. Marotta,Jobin Varkey,Ralf Langen,Champak Chatterjee,Matthew R. Pratt +7 more
TL;DR: This work has used protein semisynthesis to generate nine site-specifically ubiquitin modified α-synuclein derivatives and has demonstrated that different ubiquitination sites have differential effects on α- synuclein aggregation.
Journal ArticleDOI
O-GlcNAc modification prevents peptide-dependent acceleration of α-synuclein aggregation.
TL;DR: It is shown that an O-GlcNAc-modified peptide does not participate in α-synuclein aggregation, thus suggesting that O-glucosamine might directly inhibit aggregation in cells.
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The New Chemical Reporter 6-Alkynyl-6-deoxy-GlcNAc Reveals O-GlcNAc Modification of the Apoptotic Caspases That Can Block the Cleavage/Activation of Caspase-8
Kelly N. Chuh,Anna R. Batt,Balyn W. Zaro,Narek Darabedian,Nicholas P. Marotta,Caroline K. Brennan,Arya Amirhekmat,Matthew R. Pratt +7 more
TL;DR: These results provide the first evidence that the caspases may be directly affected by O-GlcNAcylation as a potential antiapoptotic mechanism and show that caspase-8 is modified at residues that can block its cleavage/activation.
Journal ArticleDOI
N-Terminal Protein Modification Using Simple Aminoacyl Transferase Substrates
Anne Wagner,Mark W Fegley,John B. Warner,Christina L. J. Grindley,Nicholas P. Marotta,E. James Petersson +5 more
TL;DR: It is demonstrated that AaT can efficiently use a minimal adenosine substrate, which can be synthesized in one to two steps from readily available starting materials and removes the substrate limitations imposed by the use of synthetases for tRNA charging and avoids the complex synthesis of an oligonucleotide donor.