Whole-protein alanine-scanning mutagenesis of allostery: A large percentage of a protein can contribute to mechanism
Published 2017 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Whole-protein alanine-scanning mutagenesis of allostery: A large percentage of a protein can contribute to mechanism
Authors
Keywords
-
Journal
HUMAN MUTATION
Volume 38, Issue 9, Pages 1132-1143
Publisher
Wiley
Online
2017-04-14
DOI
10.1002/humu.23231
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- What Mutagenesis Can and Cannot Reveal About Allostery
- (2016) Gerald M. Carlson et al. BIOPHYSICAL JOURNAL
- Distinguishing the Interactions in the Fructose 1,6-Bisphosphate Binding Site of Human Liver Pyruvate Kinase That Contribute to Allostery
- (2015) Arjun Ishwar et al. BIOCHEMISTRY
- Sites Involved in Intra- and Interdomain Allostery Associated with the Activation of Factor VIIa Pinpointed by Hydrogen-Deuterium Exchange and Electron Transfer Dissociation Mass Spectrometry
- (2014) Hongjian Song et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Nitric Oxide-Induced Conformational Changes in Soluble Guanylate Cyclase
- (2014) Eric S. Underbakke et al. STRUCTURE
- Identification of Regions of Rabbit Muscle Pyruvate Kinase Important for Allosteric Regulation by Phenylalanine, Detected by H/D Exchange Mass Spectrometry
- (2013) Charulata B. Prasannan et al. BIOCHEMISTRY
- Investigating Models of Protein Function and Allostery With a Widespread Mutational Analysis of a Light-Activated Protein
- (2013) Josiah P. Zayner et al. BIOPHYSICAL JOURNAL
- PDBsum additions
- (2013) Tjaart A. P. de Beer et al. NUCLEIC ACIDS RESEARCH
- Activation of AMP-Activated Protein Kinase Revealed by Hydrogen/Deuterium Exchange Mass Spectrometry
- (2013) Rachelle R. Landgraf et al. STRUCTURE
- Distinguishing the Chemical Moiety of Phosphoenolpyruvate That Contributes to Allostery in Muscle Pyruvate Kinase
- (2012) James M. Urness et al. BIOCHEMISTRY
- Energetic Coupling between an Oxidizable Cysteine and the Phosphorylatable N-Terminus of Human Liver Pyruvate Kinase
- (2012) Todd Holyoak et al. BIOCHEMISTRY
- Effector Analogues Detect Varied Allosteric Roles for Conserved Protein−Effector Interactions in Pyruvate Kinase Isozymes
- (2011) Aileen Y. Alontaga et al. BIOCHEMISTRY
- DEPTH: a web server to compute depth and predict small-molecule binding cavities in proteins
- (2011) Kuan Pern Tan et al. NUCLEIC ACIDS RESEARCH
- The pH dependence of the allosteric response of human liver pyruvate kinase to fructose-1,6-bisphosphate, ATP, and alanine
- (2009) Aron W. Fenton et al. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
- An Activating Interaction between the Unphosphorylated N-Terminus of Human Liver Pyruvate Kinase and the Main Body of the Protein Is Interrupted by Phosphorylation
- (2009) Aron W. Fenton et al. BIOCHEMISTRY
- Mapping of the Allosteric Network in the Regulation of α-Isopropylmalate Synthase fromMycobacterium tuberculosisby the Feedback Inhibitorl-Leucine: Solution-Phase H/D Exchange Monitored by FT-ICR Mass Spectrometry
- (2009) Patrick A. Frantom et al. BIOCHEMISTRY
- Allostery: an illustrated definition for the ‘second secret of life’
- (2008) Aron W. Fenton TRENDS IN BIOCHEMICAL SCIENCES
Become a Peeref-certified reviewer
The Peeref Institute provides free reviewer training that teaches the core competencies of the academic peer review process.
Get StartedAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started