Gaetano T. Montelione

Affiliations: 
1989-2019 Molecular Biology and Chemistry Rutgers University, New Brunswick, New Brunswick, NJ, United States 
 2019- Chemistry Rensselaer Polytechnic Institute, Troy, NY, United States 
Area:
Biochemistry
Website:
https://science.rpi.edu/chemistry/faculty/gaetano-t-montelione
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"Gaetano Montelione"
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Publications

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Huang YJ, Zhang N, Bersch B, et al. (2021) Assessment of Prediction Methods for Protein Structures Determined by NMR in CASP14: Impact of AlphaFold2. Proteins
Koga N, Koga R, Liu G, et al. (2021) Role of backbone strain in de novo design of complex α/β protein structures. Nature Communications. 12: 3921
Bafna K, White K, Harish B, et al. (2021) Hepatitis C virus drugs that inhibit SARS-CoV-2 papain-like protease synergize with remdesivir to suppress viral replication in cell culture. Cell Reports. 109133
Mehla J, Liechti G, Morgenstein RM, et al. (2021) ZapG (YhcB/DUF1043), a novel cell division protein in gamma-proteobacteria linking the Z-ring to septal peptidoglycan synthesis. The Journal of Biological Chemistry. 100700
Aiyer S, Swapna GVT, Ma LC, et al. (2021) A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins. Structure (London, England : 1993)
Cole CA, Daigham NS, Liu G, et al. (2021) REDCRAFT: A computational platform using residual dipolar coupling NMR data for determining structures of perdeuterated proteins in solution. Plos Computational Biology. 17: e1008060
Maisuradze GG, Montelione GT, Rackovsky S, et al. (2020) Tribute to Harold A. Scheraga. The Journal of Physical Chemistry. B
Berman HM, Adams PD, Bonvin AA, et al. (2019) Federating Structural Models and Data: Outcomes from A Workshop on Archiving Integrative Structures. Structure (London, England : 1993)
Chen G, Ma LC, Wang S, et al. (2019) A double-stranded RNA platform is required for the interaction between a host restriction factor and the NS1 protein of influenza A virus. Nucleic Acids Research
Wang X, Jing X, Deng Y, et al. (2019) Evolutionary coupling saturation mutagenesis: Coevolution-guided identification of distant sites influencing Bacillus naganoensis pullulanase activity. Febs Letters
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