Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Allen K. Kim"'
Autor:
Lauren L. Porter, Allen K. Kim, Swechha Rimal, Loren L. Looger, Ananya Majumdar, Brett D. Mensh, Mary R. Starich, Marie-Paule Strub
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
Folded proteins are composed of secondary structures, α-helices and β-sheets, that are generally assumed to be stable. Here, the authors combine computational prediction with experimental validation to show that many sequence-diverse NusG protein d
Externí odkaz:
https://doaj.org/article/974c6dda70ef42b3bcd68a1afed92e51
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
Abstract Molecular switches that respond to a biochemical stimulus in cells have proven utility as a foundation for developing molecular sensors and actuators that could be used to address important biological questions. Developing a molecular switch
Externí odkaz:
https://doaj.org/article/9cb8eb4962a94741883e9e8e641af37a
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-9 (2020)
Abstract Protein Kinase A (PKA) exists as a tetrameric holoenzyme which activates with increase of cAMP and plays an important role in many physiological processes including cardiac physiology, neuronal development, and adipocyte function. Although t
Externí odkaz:
https://doaj.org/article/bc7bba5871394f5b9099e2ddb367c9bb
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
Scientific Reports
Scientific Reports
Molecular switches that respond to a biochemical stimulus in cells have proven utility as a foundation for developing molecular sensors and actuators that could be used to address important biological questions. Developing a molecular switch unfortun
Autor:
Allen K. Kim, Lauren L. Porter
Publikováno v:
Structure
Fold-switching proteins respond to cellular stimuli by remodeling their secondary structures and changing their functions (Porter and Looger, 2018). While several previous reviews have focused on various structural, physical-chemical, and evolutionar
Autor:
Lauren L. Porter, Allen K. Kim, Swechha Rimal, Loren L. Looger, Ananya Majumdar, Brett D. Mensh, Mary Starich
SummaryHundreds of millions of structured proteins sustain life through chemical interactions and catalytic reactions1. Though dynamic, these proteins are assumed to be built upon fixed scaffolds of secondary structure, α-helices and β-sheets. Expe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4cf4d50d7eeb719207b1645783546798
https://doi.org/10.1101/2021.06.10.447921
https://doi.org/10.1101/2021.06.10.447921
Publikováno v:
Biopolymers
Although most experimentally characterized proteins with similar sequences assume the same folds and perform similar functions, an increasing number of exceptions is emerging. One class of exceptions comprises sequence‐similar fold switchers, whose
Publikováno v:
Scientific Reports
Scientific Reports, Vol 10, Iss 1, Pp 1-9 (2020)
Scientific Reports, Vol 10, Iss 1, Pp 1-9 (2020)
Protein Kinase A (PKA) exists as a tetrameric holoenzyme which activates with increase of cAMP and plays an important role in many physiological processes including cardiac physiology, neuronal development, and adipocyte function. Although this kinas
Although most proteins with known structures conform to the longstanding rule-of-thumb that high levels of aligned sequence identity tend to indicate similar folds and functions, an increasing number of exceptions is emerging. In spite of having high
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd8854aa19532b1b4604a04e8cd80824
Autor:
Takanari Inoue, Allen K. Kim
Protein Kinase A (PKA) exists as a tetrameric holoenzyme which activates with increase of cAMP and plays an important role in many physiological processes including cardiac physiology, neuronal development, and adipocyte function. Although this kinas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21d4bf00d296b238af101a7a2b5a5248
https://doi.org/10.1101/709766
https://doi.org/10.1101/709766