Alpha Helices Are More Robust to Mutations than Beta Strands

по Abrusán, György, Marsh, Joseph A.
Опубликовано в: PLoS Comput Biol (2016)

Ligand Binding Site Structure Influences the Evolution of Protein Complex Function and Topology

по Abrusán, György, Marsh, Joseph A.
Опубликовано в: Cell Rep (2018)

Ligand-Binding-Site Structure Shapes Allosteric Signal Transduction and the Evolution of Allostery in Protein Complexes

по Abrusán, György, Marsh, Joseph A
Опубликовано в: Mol Biol Evol (2019)

Ligand Binding Site Structure Shapes Folding, Assembly and Degradation of Homomeric Protein Complexes

по Abrusán, György, Marsh, Joseph A.
Опубликовано в: J Mol Biol (2019)

Ligands and Receptors with Broad Binding Capabilities Have Common Structural Characteristics: An Antibiotic Design Perspective

по Abrusán, György, Marsh, Joseph A.
Опубликовано в: J Med Chem (2019)

Correction to Ligands and Receptors with Broad Binding Capabilities Have Common Structural Characteristics: An Antibiotic Design Perspective

по Abrusán, György, Marsh, Joseph A.
Опубликовано в: J Med Chem (2019)

How do proteins gain new domains?

по Marsh, Joseph A, Teichmann, Sarah A
Опубликовано 2010

Relative Solvent Accessible Surface Area Predicts Protein Conformational Changes upon Binding

по Marsh, Joseph A., Teichmann, Sarah A.
Опубликовано 2011

Protein Flexibility Facilitates Quaternary Structure Assembly and Evolution

по Marsh, Joseph A., Teichmann, Sarah A.
Опубликовано 2014

Functional determinants of protein assembly into homomeric complexes

по Bergendahl, L. Therese, Marsh, Joseph A.
Опубликовано в: Sci Rep (2017)

Using deep mutational scanning to benchmark variant effect predictors and identify disease mutations

по Livesey, Benjamin J, Marsh, Joseph A
Опубликовано в: Mol Syst Biol (2020)

Sequence Determinants of Compaction in Intrinsically Disordered Proteins

по Marsh, Joseph A., Forman-Kay, Julie D.
Опубликовано 2010

Identification of pathogenic missense mutations using protein stability predictors

по Gerasimavicius, Lukas, Liu, Xin, Marsh, Joseph A.
Опубликовано в: Sci Rep (2020)

Operon Gene Order Is Optimized for Ordered Protein Complex Assembly

по Wells, Jonathan N., Bergendahl, L. Therese, Marsh, Joseph A.
Опубликовано в: Cell Rep (2016)

The Structural Signature of the MYPT1:PP1 Interaction

по Pinheiro, Anderson S., Marsh, Joseph A., Forman-Kay, Julie D., Peti, Wolfgang
Опубликовано 2010

Fast and Accurate Resonance Assignment of Small-to-Large Proteins by Combining Automated and Manual Approaches

по Niklasson, Markus, Ahlner, Alexandra, Andresen, Cecilia, Marsh, Joseph A., Lundström, Patrik
Опубликовано в: PLoS Comput Biol (2015)

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

по Marsh, Joseph A., Singh, Vinay K., Jia, Zongchao, Forman-Kay, Julie D.
Опубликовано 2006

Evolution of condensin and cohesin complexes driven by replacement of Kite by Hawk proteins

по Wells, Jonathan N., Gligoris, Thomas G., Nasmyth, Kim A., Marsh, Joseph A.
Опубликовано в: Curr Biol (2017)

The genetic basis and evolution of red blood cell sickling in deer

по Esin, Alexander, Bergendahl, L. Therese, Savolainen, Vincent, Marsh, Joseph A., Warnecke, Tobias
Опубликовано в: Nat Ecol Evol (2017)

The Role of Salt Bridges, Charge Density, and Subunit Flexibility in Determining Disassembly Routes of Protein Complexes

по Hall, Zoe, Hernández, Helena, Marsh, Joseph A., Teichmann, Sarah A., Robinson, Carol V.
Опубликовано 2013