Joseph A. Marsh

Sensitivity of secondary structure propensities to sequence differences between α‐ and γ‐synuclein: Implications for fibrillation

Joseph A. Marsh, Vinay Kumar Singh, Zongchao Jia et al. · Protein Science · 2006 · 742 citations · Full text

Life Sciences, Biochemistry, Molecular Biology +17

Sequence Determinants of Compaction in Intrinsically Disordered Proteins

Joseph A. Marsh, Julie D. Forman‐Kay · Biophysical Journal · 2010 · 414 citations · Full text

Life Sciences, Biochemistry, Biophysics +15

Kinetic Analysis of Protein Stability Reveals Age-Dependent Degradation

Erik McShane, Celine Sin, Henrik Zauber et al. · Cell · 2016 · 342 citations · Full text

Life Sciences, Biochemistry, Cell Biology +17

Loss-of-function, gain-of-function and dominant-negative mutations have profoundly different effects on protein structure

Lukas Gerasimavicius, Benjamin Livesey, Joseph A. Marsh · Nature Communications · 2022 · 317 citations · Full text

Life Sciences, Bioinformatics, Genetics +13

Structure/Function Implications in a Dynamic Complex of the Intrinsically Disordered Sic1 with the Cdc4 Subunit of an SCF Ubiquitin Ligase

Tanja Mittag, Joseph A. Marsh, Alexander Grishaev et al. · Structure · 2010 · 277 citations · Full text

Life Sciences, Biophysics, Molecular Biology +17