Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Austin E. Smith"'
Autor:
Peggy Hsieh, Logan Spaller, Keith Weninger, Dan Burke, Austin E. Smith, Dorothy A. Erie, Zimeng M. Li, Bangchen Wang, Pengyu Hao, Kira C. Bradford, Hunter Wilkins, Edward Chan, Dong Wu, Chunwei Du, Jacob Gauer
Publikováno v:
Proc Natl Acad Sci U S A
DNA mismatch repair (MMR) corrects errors that occur during DNA replication. In humans, mutations in the proteins MutSα and MutLα that initiate MMR cause Lynch syndrome, the most common hereditary cancer. MutSα surveilles the DNA, and upon recogni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee9b8c03f700fddbbbfb0a693f7c8064
https://doi.org/10.1073/pnas.1918519117
https://doi.org/10.1073/pnas.1918519117
Publikováno v:
Protein Science. 24:706-713
A truly disordered protein lacks a stable fold and its backbone amide protons exchange with solvent at rates predicted from studies of unstructured peptides. We have measured the exchange rates of two model disordered proteins, FlgM and α-synuclein,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c88fd6c9c4acbe44ae35332fd0b7f35
https://doi.org/10.1002/pro.2643
https://doi.org/10.1002/pro.2643
Autor:
Rachel D. Cohen, Austin E. Smith, Emilio Guzman-Cisneros, Gary J. Pielak, William B. Monteith
Publikováno v:
Proceedings of the National Academy of Sciences. 112:1739-1742
Protein quinary interactions organize the cellular interior and its metabolism. Although the interactions stabilizing secondary, tertiary, and quaternary protein structure are well defined, details about the protein–matrix contacts that comprise qu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26f02e8e3f226d244172f315de4c451b
https://doi.org/10.1073/pnas.1417415112
https://doi.org/10.1073/pnas.1417415112
Autor:
Gary J. Pielak, Samantha S. Stadmiller, Austin E. Smith, Gerardo M. Perez Goncalves, Annelise H. Gorensek-Benitez
Long accepted as the most important interaction, recent work shows that steric repulsions alone cannot explain the effects of macromolecular cosolutes on the equilibrium thermodynamics of protein stability. Instead, chemical interactions have been sh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::867b0eef5c8be4883b17114ab3f0cdba
https://europepmc.org/articles/PMC5982521/
https://europepmc.org/articles/PMC5982521/
Autor:
Austin E. Smith, Lorena Rebecchi, Dough Koshland, Thomas C. Boothby, Bob Goldstein, Alexandra H. Brozena, Ilaria Giovannini, Hugo Tapia, Gary J. Pielak, Samantha Piszkiewicz
Publikováno v:
Molecular cell, vol 65, iss 6
Tardigrades are microscopic animals that survive a remarkable array of stresses, including desiccation. How tardigrades survive desiccation has remained a mystery for more than 250 years. Trehalose, a disaccharide essential for several organisms to s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ad8702add85d24c06dd1a854f4dac44
https://europepmc.org/articles/PMC5987194/
https://europepmc.org/articles/PMC5987194/
Publikováno v:
Protein Science. 22:1313-1319
Intrinsic rates of exchange are essential parameters for obtaining protein stabilities from amide 1H exchange data. To understand the influence of the intracellular environment on stability, one must know the effect of the cytoplasm on these rates. W
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::348872b49689d022440278c5b262b6af
https://doi.org/10.1002/pro.2318
https://doi.org/10.1002/pro.2318
There is abundant, physiologically relevant knowledge about protein cores; they are hydrophobic, exquisitely well packed, and nearly all hydrogen bonds are satisfied. An equivalent understanding of protein surfaces has remained elusive because protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c97f822367c9cc673335adf994b9cb60
https://europepmc.org/articles/PMC4763743/
https://europepmc.org/articles/PMC4763743/
Publikováno v:
Angewandte Chemie (International ed. in English). 55(11)
The N-terminal SH3 domain of the Drosophila signal transduction protein drk was encapsulated in reverse micelles. Both the temperature of maximum stability and the melting temperature decreased on encapsulation. Dissecting the temperature-dependent s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db745214fbffae156c45498d09d83dd2
https://pubmed.ncbi.nlm.nih.gov/26854977
https://pubmed.ncbi.nlm.nih.gov/26854977
Publikováno v:
Biochemistry. 51:9773-9775
Most theories about macromolecular crowding focus on two ideas: the macromolecular nature of the crowder and entropy. For proteins, the volume excluded by the crowder favors compact native states over expanded denatured states, enhancing protein stab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8922dd8874b2bba807714aae91e6248c
https://doi.org/10.1021/bi300909q
https://doi.org/10.1021/bi300909q
Publikováno v:
Current opinion in structural biology. 30
Proteins function in cells where the concentration of macromolecules can exceed 300g/L. The ways in which this crowded environment affects the physical properties of proteins remain poorly understood. We summarize recent NMR-based studies of protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bdb924db3673bf08098bda085692f63
https://pubmed.ncbi.nlm.nih.gov/25479354
https://pubmed.ncbi.nlm.nih.gov/25479354