Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Austin G Meyer"'
Publikováno v:
PLoS Biology, Vol 14, Iss 5, p e1002452 (2016)
Functional residues in proteins tend to be highly conserved over evolutionary time. However, to what extent functional sites impose evolutionary constraints on nearby or even more distant residues is not known. Here, we report pervasive conservation
Externí odkaz:
https://doaj.org/article/24b25204093a4fa6bf23f0afd7e8f226
Autor:
Sarabeth M. Mathis, Alexander E. Webber, Tomás M. León, Erin L. Murray, Monica Sun, Lauren A. White, Logan C. Brooks, Alden Green, Addison J. Hu, Roni Rosenfeld, Dmitry Shemetov, Ryan J. Tibshirani, Daniel J. McDonald, Sasikiran Kandula, Sen Pei, Rami Yaari, Teresa K. Yamana, Jeffrey Shaman, Pulak Agarwal, Srikar Balusu, Gautham Gururajan, Harshavardhan Kamarthi, B. Aditya Prakash, Rishi Raman, Zhiyuan Zhao, Alexander Rodríguez, Akilan Meiyappan, Shalina Omar, Prasith Baccam, Heidi L. Gurung, Brad T. Suchoski, Steve A. Stage, Marco Ajelli, Allisandra G. Kummer, Maria Litvinova, Paulo C. Ventura, Spencer Wadsworth, Jarad Niemi, Erica Carcelen, Alison L. Hill, Sara L. Loo, Clifton D. McKee, Koji Sato, Claire Smith, Shaun Truelove, Sung-mok Jung, Joseph C. Lemaitre, Justin Lessler, Thomas McAndrew, Wenxuan Ye, Nikos Bosse, William S. Hlavacek, Yen Ting Lin, Abhishek Mallela, Graham C. Gibson, Ye Chen, Shelby M. Lamm, Jaechoul Lee, Richard G. Posner, Amanda C. Perofsky, Cécile Viboud, Leonardo Clemente, Fred Lu, Austin G. Meyer, Mauricio Santillana, Matteo Chinazzi, Jessica T. Davis, Kunpeng Mu, Ana Pastore y Piontti, Alessandro Vespignani, Xinyue Xiong, Michal Ben-Nun, Pete Riley, James Turtle, Chis Hulme-Lowe, Shakeel Jessa, V. P. Nagraj, Stephen D. Turner, Desiree Williams, Avranil Basu, John M. Drake, Spencer J. Fox, Ehsan Suez, Monica G. Cojocaru, Edward W. Thommes, Estee Y. Cramer, Aaron Gerding, Ariane Stark, Evan L. Ray, Nicholas G. Reich, Li Shandross, Nutcha Wattanachit, Yijin Wang, Martha W. Zorn, Majd Al Aawar, Ajitesh Srivastava, Lauren A. Meyers, Aniruddha Adiga, Benjamin Hurt, Gursharn Kaur, Bryan L. Lewis, Madhav Marathe, Srinivasan Venkatramanan, Patrick Butler, Andrew Farabow, Naren Ramakrishnan, Nikhil Muralidhar, Carrie Reed, Matthew Biggerstaff, Rebecca K. Borchering
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract Accurate forecasts can enable more effective public health responses during seasonal influenza epidemics. For the 2021–22 and 2022–23 influenza seasons, 26 forecasting teams provided national and jurisdiction-specific probabilistic predi
Externí odkaz:
https://doaj.org/article/b22341a399b644b886f816887477dc5b
Autor:
Austin G Meyer, Claus O Wilke
Publikováno v:
PLoS Pathogens, Vol 11, Iss 5, p e1004940 (2015)
We have carried out a comprehensive analysis of the determinants of human influenza A H3 hemagglutinin evolution. We consider three distinct predictors of evolutionary variation at individual sites: solvent accessibility (as a proxy for protein fold
Externí odkaz:
https://doaj.org/article/90dbeb41b8004187a46de311c35464c6
Autor:
Viswanadham Sridhara, Austin G Meyer, Piyush Rai, Jeffrey E Barrick, Pradeep Ravikumar, Daniel Segrè, Claus O Wilke
Publikováno v:
PLoS ONE, Vol 9, Iss 12, p e114608 (2014)
A widely studied problem in systems biology is to predict bacterial phenotype from growth conditions, using mechanistic models such as flux balance analysis (FBA). However, the inverse prediction of growth conditions from phenotype is rarely consider
Externí odkaz:
https://doaj.org/article/2b9f8dd1d3a44e7ca57f85fc6e46abba
Publikováno v:
PLoS ONE, Vol 8, Iss 11, p e80635 (2013)
The relative solvent accessibility (RSA) of a residue in a protein measures the extent of burial or exposure of that residue in the 3D structure. RSA is frequently used to describe a protein's biophysical or evolutionary properties. To calculate RSA,
Externí odkaz:
https://doaj.org/article/7b8050131a3c4c59a9ddef56b3506009
Autor:
Ravi Rajmohan, Ronald C. Anderson, Dan Fang, Austin G. Meyer, Pavis Laengvejkal, Parunyou Julayanont, Greg Hannabas, Kitten Linton, John Culberson, Hafiz Khan, John De Toledo, P. Hemachandra Reddy, Michael W. O’Boyle
Publikováno v:
Frontiers in Aging Neuroscience
Frontiers in Aging Neuroscience, Vol 9 (2017)
Frontiers in Aging Neuroscience, Vol 9 (2017)
Face-labeling refers to the ability to classify faces into social categories. This plays a critical role in human interaction as it serves to define concepts of socially acceptable interpersonal behavior. The purpose of the current study was to chara
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42fc3a226dc45b6d416c01bf8ca61e99
Existing computational methods to predict protein–protein interaction affinity often perform poorly in important test cases. In particular, the effects of multiple mutations, non-alanine substitutions, and flexible loops are difficult to predict wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab83687cf2c9a8af98dada7106591812
https://doi.org/10.7287/peerj.preprints.138v1
https://doi.org/10.7287/peerj.preprints.138v1
Autor:
Kerry, Fuson, Anne, Rice, Ryan, Mahling, Adam, Snow, Kamakshi, Nayak, Prajna, Shanbhogue, Austin G, Meyer, Gregory M I, Redpath, Anne, Hinderliter, Sandra T, Cooper, R Bryan, Sutton
Publikováno v:
Structure (London, England : 1993). 22(1)
Dysferlin plays a critical role in the Ca2+-dependent repair of microlesions that occur in the muscle sarcolemma. Of the seven C2 domains in dysferlin, only C2A is reported to bind both Ca2+ and phospholipid, thus acting as a key sensor in membrane r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::26bcc129bfd1e48cbefd774cd7f0e428
https://pubmed.ncbi.nlm.nih.gov/24239457
https://pubmed.ncbi.nlm.nih.gov/24239457
Publikováno v:
PeerJ, Vol 2, p e266 (2014)
In many biological applications, we would like to be able to computationally predict mutational effects on affinity in protein–protein interactions. However, many commonly used methods to predict these effects perform poorly in important test cases
Externí odkaz:
https://doaj.org/article/ad95377c93844cdbb07f9533456d3f86
Publikováno v:
PeerJ, Vol 1, p e80 (2013)
We present a simple Python library to construct models of polypeptides from scratch. The intended use case is the generation of peptide models with pre-specified backbone angles. For example, using our library, one can generate a model of a set of am
Externí odkaz:
https://doaj.org/article/71ed51e7101e4a568801870c612f5c32