A 22-mer Segment in the Structurally Pliable Regulatory Domain of Metazoan CTP: Phosphocholine Cytidylyltransferase Facilitates Both Silencing and Activating Functions
Published 2012 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
A 22-mer Segment in the Structurally Pliable Regulatory Domain of Metazoan CTP: Phosphocholine Cytidylyltransferase Facilitates Both Silencing and Activating Functions
Authors
Keywords
-
Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 46, Pages 38980-38991
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2012-09-18
DOI
10.1074/jbc.m112.402081
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- The amphipathic helix of an enzyme that regulates phosphatidylcholine synthesis remodels membranes into highly curved nanotubules
- (2012) Svetla G. Taneva et al. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
- Membrane Trafficking: Decoding Vesicle Identity with Contrasting Chemistries
- (2011) Adam Frost CURRENT BIOLOGY
- The Intrinsically Disordered Nuclear Localization Signal and Phosphorylation Segments Distinguish the Membrane Affinity of Two Cytidylyltransferase Isoforms
- (2011) Melissa K. Dennis et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- α-Synuclein Populates Both Elongated and Broken Helix States on Small Unilamellar Vesicles
- (2011) Sowmya Bekshe Lokappa et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- The N-Terminal Amphipathic Helix of the Topological Specificity Factor MinE Is Associated with Shaping Membrane Curvature
- (2011) Yu-Ling Shih et al. PLoS One
- The Lipid-binding Domain of Wild Type and Mutant α-Synuclein
- (2010) Elka R. Georgieva et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Functions of Membrane Binding Domain of CTP:Phosphocholine Cytidylyltransferase in Alveolar Type II Cells
- (2009) Ross Ridsdale et al. AMERICAN JOURNAL OF RESPIRATORY CELL AND MOLECULAR BIOLOGY
- Identification of hydrophobic amino acids required for lipid activation of C. elegans CTP:phosphocholine cytidylyltransferase
- (2009) Jay D. Braker et al. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
- Linking folding and binding
- (2009) Peter E Wright et al. CURRENT OPINION IN STRUCTURAL BIOLOGY
- Amphipathic helices and membrane curvature
- (2009) Guillaume Drin et al. FEBS LETTERS
- Crystal Structure of a Mammalian CTP: Phosphocholine Cytidylyltransferase Catalytic Domain Reveals Novel Active Site Residues within a Highly Conserved Nucleotidyltransferase Fold
- (2009) Jaeyong Lee et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- New insights into the membrane-binding and activation mechanism of pyruvate oxidase from Escherichia coli
- (2009) Annett Weidner et al. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
- Intrinsic disorder prediction from the analysis of multiple protein fold recognition models
- (2008) Liam J. McGuffin BIOINFORMATICS
- HELIQUEST: a web server to screen sequences with specific -helical properties
- (2008) R. Gautier et al. BIOINFORMATICS
- The Hydrophobic Insertion Mechanism of Membrane Curvature Generation by Proteins
- (2008) Felix Campelo et al. BIOPHYSICAL JOURNAL
- Contribution of Each Membrane Binding Domain of the CTP:Phosphocholine Cytidylyltransferase-α Dimer to Its Activation, Membrane Binding, and Membrane Cross-bridging
- (2008) Svetla Taneva et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Nuclear export of the rate-limiting enzyme in phosphatidylcholine synthesis is mediated by its membrane binding domain
- (2008) Karsten Gehrig et al. JOURNAL OF LIPID RESEARCH
- Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli
- (2008) P. Neumann et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Find Funding. Review Successful Grants.
Explore over 25,000 new funding opportunities and over 6,000,000 successful grants.
ExploreAsk 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