Zobrazeno 1 - 10
of 426
pro vyhledávání: '"Gaetano T. Montelione"'
Autor:
Piotr Klukowski, Fred F. Damberger, Frédéric H.-T. Allain, Hideo Iwai, Harindranath Kadavath, Theresa A. Ramelot, Gaetano T. Montelione, Roland Riek, Peter Güntert
Publikováno v:
Scientific Data, Vol 11, Iss 1, Pp 1-13 (2024)
Abstract Multidimensional NMR spectra are the basis for studying proteins by NMR spectroscopy and crucial for the development and evaluation of methods for biomolecular NMR data analysis. Nevertheless, in contrast to derived data such as chemical shi
Externí odkaz:
https://doaj.org/article/d607f976b6f94288a6a64321321d3e7a
Autor:
Luca Mazzei, Rebecca Greene-Cramer, Khushboo Bafna, Aleksandar Jovanovic, Anna De Falco, Thomas B. Acton, Catherine Ann Royer, Stefano Ciurli, Gaetano T. Montelione
Publikováno v:
STAR Protocols, Vol 4, Iss 2, Pp 102326- (2023)
Summary: 3CLpro protease from SARS-CoV-2 is a primary target for COVID-19 antiviral drug development. Here, we present a protocol for 3CLpro production in Escherichia coli. We describe steps to purify 3CLpro, expressed as a fusion with the Saccharomy
Externí odkaz:
https://doaj.org/article/de67ec972ab7404e8418b641877bf219
Publikováno v:
Frontiers in Chemistry, Vol 10 (2022)
Considering the significant impact of the recent COVID-19 outbreak, development of broad-spectrum antivirals is a high priority goal to prevent future global pandemics. Antiviral development processes generally emphasize targeting a specific protein
Externí odkaz:
https://doaj.org/article/2650cc70537c4b1e9b4585923e0623e4
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Externí odkaz:
https://doaj.org/article/10377cc98cea457a86b8741fbfdcf201
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
The authors show that consideration of global backbone strain enables successful de novo design of larger αβ-proteins with five- and six- stranded β-sheets flanked by α-helices.
Externí odkaz:
https://doaj.org/article/2d79dbe5ccf94845993306b13efb4de2
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Recent advances in molecular modeling using deep learning have the potential to revolutionize the field of structural biology. In particular, AlphaFold has been observed to provide models of protein structures with accuracies rivaling medium-resoluti
Externí odkaz:
https://doaj.org/article/7d10623df17f4968ad4beb4698dbd1d7
Autor:
Khushboo Bafna, Kris White, Balasubramanian Harish, Romel Rosales, Theresa A. Ramelot, Thomas B. Acton, Elena Moreno, Thomas Kehrer, Lisa Miorin, Catherine A. Royer, Adolfo García-Sastre, Robert M. Krug, Gaetano T. Montelione
Publikováno v:
Cell Reports, Vol 35, Iss 7, Pp 109133- (2021)
Summary: Effective control of COVID-19 requires antivirals directed against SARS-CoV-2. We assessed 10 hepatitis C virus (HCV) protease-inhibitor drugs as potential SARS-CoV-2 antivirals. There is a striking structural similarity of the substrate bin
Externí odkaz:
https://doaj.org/article/f487dc0be1e94d1382aa92c5a7ce55f1
Autor:
Joseph R. Luft, Jennifer R. Wolfley, Eleanor Cook Franks, Angela M. Lauricella, Ellen J. Gualtieri, Edward H. Snell, Rong Xiao, John K. Everett, Gaetano T. Montelione
Publikováno v:
Structural Dynamics, Vol 2, Iss 4, Pp 041710-041710-17 (2015)
Identifying and then optimizing initial crystallization conditions is a prerequisite for macromolecular structure determination by crystallography. Improved technologies enable data collection on crystals that are difficult if not impossible to det
Externí odkaz:
https://doaj.org/article/9866f852b1d941f08eb6c88c4e015247
Autor:
Gaetano T. Montelione, Stephen Anderson, Thomas Acton, Bonnie Dixon, Yuanpeng Huang, Hunter Moseley, Daniel Monleon, Kamal Shukla, Gaetano G. V. T. Swapna, Roberto Tejero
Publikováno v:
The Scientific World Journal, Vol 2, Pp 32-32 (2002)
Externí odkaz:
https://doaj.org/article/b42c2296a2e34adebb9df4a3bbec35b2
Autor:
Arup Mondal, G.V.T. Swapna, Maria M. Lopez, Laura Klang, Jingzhou Hao, LiChung Ma, Monica J. Roth, Gaetano T. Montelione, Alberto Perez
Publikováno v:
J Chem Inf Model
Intrinsically disordered regions of proteins often mediate important protein–protein interactions. However, the folding-upon-binding nature of many polypeptide–protein interactions limits the ability of modeling tools to predict the three-dimensi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2896313d0e69f68fd897e44cc63cc0a1
https://doi.org/10.1021/acs.jcim.2c01595
https://doi.org/10.1021/acs.jcim.2c01595