A strategy for analyzing bond strength and interaction kinetics between Pleckstrin homology domains and PI(4,5)P2 phospholipids using force distance spectroscopy and surface plasmon resonance-Reference-Cited by-同舟云学术

A strategy for analyzing bond strength and interaction kinetics between Pleckstrin homology domains and PI(4,5)P2 phospholipids using force distance spectroscopy and surface plasmon resonance

Published:2015 Issue:13 Volume:140 Page:4558-4565
ISSN:0003-2654
Container-title:The Analyst
language:en
Short-container-title:Analyst

Author:

Malkovskiy A. V.¹²³,Wagh D. A.¹²³,Longo F. M.⁴⁵²³,Rajadas J.¹²³

Affiliation:

1. Stanford BioADD Laboratory

2. Stanford

3. USA

4. Department of Neurology and Neurological Sciences

5. Stanford University School of Medicine

Abstract

Use of AFM force–distance spectroscopy and SPR analysis to assess strong single-molecule binding between PH protein domains and phosphatidylinositol phospholipids.

Publisher

Royal Society of Chemistry (RSC)

Subject

Electrochemistry,Spectroscopy,Environmental Chemistry,Biochemistry,Analytical Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/AN/C5AN00498E

Reference48 articles.

1. Localised PtdIns(3,4,5)P3 or PtdIns(3,4)P2 at the phagocytic cup is required for both phagosome closure and Ca2+ signalling in HL60 neutrophils

2. PI(3,5)P2 controls membrane trafficking by direct activation of mucolipin Ca2+ release channels in the endolysosome

3. Therapeutic potential of phosphoinositide 3-kinase inhibitors

4. Therapeutic Potential of Phosphoinositide 3-Kinase Inhibitors

5. Hepatitis C Virus Stimulates the Phosphatidylinositol 4-Kinase III Alpha-Dependent Phosphatidylinositol 4-Phosphate Production That Is Essential for Its Replication

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