Daniel A. Nissley

发表

Ribosome occupancy profiles are conserved between structurally and evolutionarily related yeast domains

Charlotte M. Deane, Mark Chonofsky, Daniel A. Nissley, 2021, Bioinform..

Does SARS-CoV-2 Bind to Human ACE2 More Strongly Than Does SARS-CoV?

Hoang Linh Nguyen, Nguyen Quoc Thai, Daniel A. Nissley, 2020, The journal of physical chemistry. B.

Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding

Bernd Bukau, Ulrike A. Friedrich, Günter Kramer, 2016, Nature Communications.

Universal protein misfolding intermediates can bypass the proteostasis network and remain soluble and less functional

Daniel A. Nissley, E. O’Brien, S. Fried, 2022, Nature communications.

Spatially selective formation of hydrocarbon, fluorocarbon, and hydroxyl-terminated monolayers on a microelectrode array.

Kevin M. Cook, Daniel A. Nissley, G. S. Ferguson, 2013, Langmuir : the ACS journal of surfaces and colloids.

Domain topology, stability, and translation speed determine mechanical force generation on the ribosome

Daniel A. Nissley, E. O’Brien, Fabio Trovato, 2018, Proceedings of the National Academy of Sciences.

Computationally profiling peptide:MHC recognition by T-cell receptors and T-cell receptor-mimetic antibodies

Daniel A. Nissley, C. Deane, M. Raybould, 2022, bioRxiv.

Current structure predictors are not learning the physics of protein folding

Daniel A. Nissley, C. Deane, C. Outeiral, 2022, Bioinform..

Cocktail of REGN Antibodies Binds More Strongly to SARS-CoV-2 Than Its Components, but the Omicron Variant Reduces Its Neutralizing Ability

Daniel A. Nissley, Pham Dang Lan, E. O’Brien, 2022, The journal of physical chemistry. B.

Altered Co-Translational Processing Plays a Role in Huntington's Pathogenesis—A Hypothesis

Daniel A. Nissley, E. O’Brien, 2016, Front. Mol. Neurosci..

Timing is everything: unifying codon translation rates and nascent proteome behavior.

Edward P O'Brien, Daniel A. Nissley, E. O’Brien, 2014, Journal of the American Chemical Society.

Universal protein misfolding intermediates can bypass the proteostasis network and remain soluble and less functional

Daniel A. Nissley, E. O’Brien, S. Fried, 2021, Nature Communications.

Electrostatic interactions govern extreme nascent protein ejection times from ribosomes and can delay ribosome recycling.

Daniel A. Nissley, E. O’Brien, M. Li, 2020, Journal of the American Chemical Society.

Subpopulations of soluble, misfolded proteins commonly bypass chaperones: How it happens at the molecular level

Daniel A. Nissley, E. O’Brien, Ritaban Halder, 2021, bioRxiv.

Electrostatic Interactions Explain the Higher Binding Affinity of the CR3022 Antibody for SARS-CoV-2 than the 4A8 Antibody

Daniel A. Nissley, Pham Dang Lan, E. O’Brien, 2021, The journal of physical chemistry. B.

Structural Origins of FRET-Observed Nascent Chain Compaction on the Ribosome.

Daniel A. Nissley, E. O’Brien, 2018, The journal of physical chemistry. B.

Is Posttranslational Folding More Efficient Than Refolding from a Denatured State: A Computational Study

Daniel A. Nissley, E. O’Brien, M. Li, 2023, The journal of physical chemistry. B.

How soluble misfolded proteins bypass chaperones at the molecular level

Daniel A. Nissley, J. Pritchard, E. O’Brien, 2023, Nature communications.

Current protein structure predictors do not produce meaningful folding pathways

Daniel A. Nissley, C. Deane, C. Outeiral, 2021, bioRxiv.

The molecular reach of antibodies determines their SARS-CoV-2 neutralisation potency

Daniel A. Nissley, G. Screaton, Omer Dushek, 2023, bioRxiv.