Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Jaie C. Woodard"'
Publikováno v:
PLoS Computational Biology, Vol 11, Iss 4, p e1004207 (2015)
Design of proteins with desired thermal properties is important for scientific and biotechnological applications. Here we developed a theoretical approach to predict the effect of mutations on protein stability from non-equilibrium unfolding simulati
Externí odkaz:
https://doaj.org/article/0de565c5f8ba4e83acf0d1ba075a7893
Autor:
Barbara Scalvini, Jana Aupič, Alireza Mashaghi, Vahid Sheikhhassani, Remus T. Dame, Roman Jerala, Jaie C. Woodard
Publikováno v:
Trends in Chemistry, 2(7), 609-622. Elsevier BV
The topology of biological polymers such as proteins and nucleic acids is an important aspect of their 3D structure. Recently, two applications of topology to molecular chains have emerged as important theoretical developments that are beginning to f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ac89c0e87e4c68701cd54226bd7006b
https://hdl.handle.net/1887/3245505
https://hdl.handle.net/1887/3245505
Autor:
Song Yi, Chris Cotsapas, Jesse V. Kurland, Anastasia Vedenko, Trevor Siggers, Jaie C. Woodard, David E. Hill, Leila Shokri, Stephen S. Gisselbrecht, Julia M. Rogers, Manolis Kellis, Luis A. Barrera, Marc Vidal, Tong Hao, Raluca Gordân, Elizabeth J. Rossin, Kian Hong Kock, Sachi Inukai, Mark J. Daly, Nidhi Sahni, Martha L. Bulyk, Luca Mariani
Publikováno v:
PMC
Sequencing of exomes and genomes has revealed abundant genetic variation affecting the coding sequences of human transcription factors (TFs), but the consequences of such variation remain largely unexplored. We developed a computational, structure-ba
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0fcec79c58b646b16cf493848563e2f
https://doi.org/10.1126/science.aad2257
https://doi.org/10.1126/science.aad2257
Autor:
Jaie C. Woodard, Laura C. Dilley, Nikaela Losievski, Matthew Lehet, Meisam K. Arjmandi, Yuanyuan Wang, Derek M. Houston
Publikováno v:
The Journal of the Acoustical Society of America. 146:2956-2956
Automated audio processing systems, such as the Language Environment Analysis (LENA) system, are useful tools for understanding developmental language behaviors for clinical and basic research purposes. However, it is still unclear how accurate they
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7a75f93f56ac33531ac331f0940f2aa6
https://doi.org/10.1121/1.5137267
https://doi.org/10.1121/1.5137267
Autor:
Jaie C. Woodard, Eugene I. Shakhnovich, Eugene Serebryany, Mohammed Shabab, Jonathan King, Bharat V. Adkar
Considerable mechanistic insight has been gained into amyloid aggregation; however, a large class of non-amyloid protein aggregates are considered 'amorphous,' and in most cases little is known about their mechanisms. Amorphous aggregation of ��-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c5fa0640a52bc2d12f3f8273d9a8c18
Publikováno v:
Biophysical journal. 110(11)
Domain swapping in proteins is an important mechanism of functional and structural innovation. However, despite its ubiquity and importance, the physical mechanisms that lead to domain swapping are poorly understood. Here, we present a simple two-dim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::972fddccba1a3bca6afb94ce2fa7e642
https://pubmed.ncbi.nlm.nih.gov/27276255
https://pubmed.ncbi.nlm.nih.gov/27276255
Autor:
Mohammed Shabab, Bharat V. Adkar, Jaie C. Woodard, Eugene I. Shakhnovich, Jonathan King, Eugene Serebryany
Publikováno v:
Biophysical Journal. 112:167a-168a
Considerable mechanistic insight has been gained into amyloid aggregation; however, a large class of non-amyloid protein aggregates are considered 'amorphous,' and in most cases little is known about their mechanisms. Amorphous aggregation of {\gamma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::faab7d393d09acecde3ef2c583569b4b
https://doi.org/10.1016/j.bpj.2016.11.923
https://doi.org/10.1016/j.bpj.2016.11.923
Publikováno v:
PLoS Computational Biology, Vol 11, Iss 4, p e1004207 (2015)
PLoS Computational Biology
PLoS Computational Biology
Design of proteins with desired thermal properties is important for scientific and biotechnological applications. Here we developed a theoretical approach to predict the effect of mutations on protein stability from non-equilibrium unfolding simulati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc68c5d82a20a918705eaa6bf9886b13
https://doaj.org/article/0de565c5f8ba4e83acf0d1ba075a7893
https://doaj.org/article/0de565c5f8ba4e83acf0d1ba075a7893
Autor:
Eduardo R. Cruz-Chu, Klaus Schulten, Logan Liu, Manas Ranjan Gartia, Jaie C. Woodard, Yi-Chun Chen
Surface immobilized biomolecular probes are used in many areas of biomedical research, such as genomics, proteomics, immunology, and pathology. Although the structural conformations of small DNA and peptide molecules in free solution are well studied
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a93d002581aa30adab55e7e090858e1d
https://europepmc.org/articles/PMC3482133/
https://europepmc.org/articles/PMC3482133/
Publikováno v:
Journal of the American Chemical Society. 131(27)
The NMR chemical shift is a sensitive reporter of peptide secondary structure and its solvation environment, and it is potentially rich with information about both backbone dihedral angles and hydrogen bonding. We report results from solution- and so
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::397d4e637e8e9bc3b0f72c0871e8da1f
https://pubmed.ncbi.nlm.nih.gov/19537718
https://pubmed.ncbi.nlm.nih.gov/19537718