Structure and function of integral membrane protein domains resolved by peptide-amphiphiles: Application to phospholamban-Reference-Cited by-同舟云学术

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Structure and function of integral membrane protein domains resolved by peptide-amphiphiles: Application to phospholamban

Published:2003 Issue:3 Volume:69 Page:283-292
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Lockwood Nathan A.,Tu Raymond S.,Zhang Zhiwen,Tirrell Matthew V.,Thomas David D.,Karim Christine B.

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference51 articles.

1. Synthetic lipidation of peptides and amino acids: monolayer structure and properties.

2. Cellular recognition of synthetic peptide amphiphiles in self-assembled monolayer films

3. Behavior of Lipid-Modified Peptides in Membrane-Mimetic Monolayers at the Air/Water Interface

4. Formation of high axial ratio microstructures from peptides modified with glutamic acid dialkyl amides

5. Proteinlike molecular architecture: Biomaterial applications for inducing cellular receptor binding and signal transduction

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1. Diffusion behavior of peptide amphiphiles containing different numbers of alkyl tails at a hydrophobic solid–liquid interface: single molecule tracking investigation;Soft Matter;2020

2. Nitroxyl (HNO) targets phospholamban cysteines 41 and 46 to enhance cardiac function;Journal of General Physiology;2019-03-06

3. Targeting protein-protein interactions for therapeutic discovery via FRET-based high-throughput screening in living cells;Scientific Reports;2018-08-22

4. Structural dynamics of calmodulin-ryanodine receptor interactions: electron paramagnetic resonance using stereospecific spin labels;Scientific Reports;2018-07-16

5. Effect of Phosphorylation on Interactions between Transmembrane Domains of SERCA and Phospholamban;Biophysical Journal;2018-06

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