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Brian C. Mackness
University of Massachusetts Medical School
4Publications
2H-index
27Citations
Publications 4
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#1Brian C. Mackness (UMMS: University of Massachusetts Medical School)H-Index: 2
#2Noah R. Cohen (UMMS: University of Massachusetts Medical School)H-Index: 1
Last.Osman Bilsel (UMMS: University of Massachusetts Medical School)H-Index: 23
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The dimeric β-barrel protein Cu, Zn superoxide dismutase (SOD1) is an optimal model system for investigating the molecular basis for toxicity in ALS. Mutations throughout the β-barrel sequence are causative for ALS and implicated in the gain-of-function toxicity. The occurrence of mutations at dozens of sites suggests a common mechanism of toxicity for SOD1 disease causing variants. Previous biophysical and structural data on SOD1 and its variants have established a fairly detailed understanding...
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#1Ben Niu (WashU: Washington University in St. Louis)H-Index: 2
#2Brian C. Mackness (UMMS: University of Massachusetts Medical School)H-Index: 2
Last.Michael L. Gross (WashU: Washington University in St. Louis)H-Index: 75
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Incorporation of a reporter peptide in solutions submitted to fast photochemical oxidation of proteins (FPOP) allows for the correction of adventitious scavengers and enables the normalization and comparison of time-dependent results. Reporters will also be useful in differential experiments to control for the inclusion of a radical-reactive species. This incorporation provides a simple and quick check of radical dosage and allows comparison of FPOP results from day-to-day and lab-to-lab. Use of...
9 CitationsSource
#1Brian C. Mackness (UMMS: University of Massachusetts Medical School)H-Index: 2
#2Meme Tran (UMMS: University of Massachusetts Medical School)
Last.Jill A. Zitzewitz (UMMS: University of Massachusetts Medical School)H-Index: 18
view all 8 authors...
#1Brian C. Mackness (UMMS: University of Massachusetts Medical School)H-Index: 2
#2Meme T. Tran (UMMS: University of Massachusetts Medical School)H-Index: 1
Last.Jill A. Zitzewitz (UMMS: University of Massachusetts Medical School)H-Index: 18
view all 5 authors...
Pathological alteration of TDP-43 (TAR DNA-binding protein-43), a protein involved in various RNA-mediated processes, is a hallmark feature of the neurodegenerative diseases amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Fragments of TDP-43, composed of the second RNA recognition motif (RRM2) and the disordered C terminus, have been observed in cytoplasmic inclusions in sporadic amyotrophic lateral sclerosis cases, suggesting that conformational changes involving RRM2 toget...
18 CitationsSource
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