Interaction of GAPR-1 with lipid bilayers is regulated by alternative homodimerization-Reference-Cited by-同舟云学术

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Interaction of GAPR-1 with lipid bilayers is regulated by alternative homodimerization

Published:2012-09 Issue:9 Volume:1818 Page:2175-2183
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

van Galen Josse,Olrichs Nick K.,Schouten Arie,Serrano Ramon L.,Nolte-'t Hoen Esther N.M.,Eerland Ruud,Kaloyanova Dora,Gros Piet,Helms J. Bernd

Funder

Research Council for Earth and Life Sciences

Netherlands Organization for Scientific Research

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference31 articles.

1. The families of plant pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins;van Loon;Physiol. Mol. Plant Pathol.,1999

2. Significance of inducible defense-related proteins in infected plants;van Loon;Annu. Rev. Phytopathol.,2006

3. Structural analysis of the human Golgi-associated plant pathogenesis related protein GAPR-1 implicates dimerization as a regulatory mechanism;Serrano;J. Mol. Biol.,2004

4. Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex;Eberle;J. Cell Sci.,2002

5. Pathogenesis-related PR-1 proteins are antifungal. Isolation and characterization of three 14-kilodalton proteins of tomato and of a basic PR-1 of tobacco with inhibitory activity against Phytophthora infestans;Niderman;Plant Physiol.,1995

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4. Dynamic and Reversible Aggregation of the Human CAP Superfamily Member GAPR-1 in Protein Inclusions in Saccharomyces cerevisiae;Journal of Molecular Biology;2021-09

5. Regulation of Functional Protein Aggregation by Multiple Factors: Implications for the Amyloidogenic Behavior of the CAP Superfamily Proteins;International Journal of Molecular Sciences;2020-09-07

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