Cultural advice

The Australian National University acknowledges, celebrates and pays our respects to the Ngunnawal and Ngambri people of the Canberra region and to all First Nations Australians on whose traditional lands we meet and work, and whose cultures are among the oldest continuing cultures in human history.

Aboriginal and Torres Strait Islander peoples are advised that ANU Library collections may include images, names, voices, and other representations of deceased persons.

Material in the collection may contain terms, language or views that reflect the period in which the item was created and may be considered inappropriate today.

Structures of the flax-rust effector AvrM reveal insights into the molecular basis of plant-cell entry and effector-triggered immunity

Thumbnail Image

Date

2013

Authors

Ve, Thomas
Williams, Simon
Catanzariti, Ann-Maree
Rafiqi, Maryam
Rahman , Motiur
Ellis, Jeffrey G
Hardham, Adrienne
Jones, David
Anderson , Peter A
Dodds, Peter N

Journal Title

Journal ISSN

Volume Title

Publisher

National Academy of Sciences (USA)

Abstract

Description

Keywords

Keywords: AvrM protein; dimer; phosphatidylinositide; protein; unclassified drug; vegetable protein; article; crystal structure; hydrophobicity; innate immunity; internalization; mutational analysis; plant cell; plant immunity; priority journal; protein binding; pr Avirulence protein; Innate immunity; Lipid binding; Plant cell internalization; Plant disease resistance

Citation

URI

http://hdl.handle.net/1885/152382

Collections

ANU Research Publications

Source

PNAS - Proceedings of the National Academy of Sciences of the United States of America

Type

Journal article

Book Title

Entity type

Access Statement

Open Access

License Rights

DOI

10.1073/pnas.1307614110

Restricted until

Downloads

File
Description
01_Ve_Structures_of_the_flax-rust_2013.pdf (1.47 MB)

DSpace software copyright © 2002-2026 LYRASIS