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Macromolecular Structure Laboratory
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Last updated : 16 April 2024 03:58

A positive charged patch and stabilized hydrophobic core are essential for avirulence function of AvrPib in the rice blast fungus

Authors (9)

Xin Zhang
Dan He
Yanxiang Zhao
Xilan Cheng
Wensheng Zhao
Ian Taylor
Jun Yang
Junfeng Liu
You-Liang Peng

Plant Journal

Published 1 August 2018

Crick labs

Ian Taylor

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Structure based function-annotation of hypothetical protein MGG_01005 from Magnaporthe oryzae reveals it is the dynein light chain orthologue of dynlt1/3

Authors (9)

Guorui Li
Jinguang Huang
Jun Yang
Dan He
Chao Wang
Xiaoxuan Qi
Ian Taylor
Junfeng Liu
You-Liang Peng

Scientific Reports

Published 2 March 2018

Crick labs

Ian Taylor

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A cryptic RNA-binding domain mediates Syncrip recognition and exosomal partitioning of miRNA targets

Authors (12)

Fruzsina Hobor
Andre Dallmann
Neil J Ball
Carla Cicchini
Cecilia Battistelli
Roksana Ogrodowicz
[...]
Stephen R Martin
Alfredo Castello
Marco Tripodi
Ian Taylor
Andres Ramos

Nature Communications

Published 26 February 2018

Crick labs/ facilities

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Taylor lab
Macromolecular Structure Laboratory
: Publications

Lab content

Publications

Year published

Research topics

Publication type

Journal

A positive charged patch and stabilized hydrophobic core are essential for avirulence function of AvrPib in the rice blast fungus

Structure based function-annotation of hypothetical protein MGG_01005 from Magnaporthe oryzae reveals it is the dynein light chain orthologue of dynlt1/3

A cryptic RNA-binding domain mediates Syncrip recognition and exosomal partitioning of miRNA targets

The Francis Crick Institute is a unique partnership between

Research case studies

Postdoctoral clinical fellows

Hello Brain!

News and reports

About us

Lab content

Publications

Year published

Research topics

Publication type

Journal

Publications

A positive charged patch and stabilized hydrophobic core are essential for avirulence function of AvrPib in the rice blast fungus

Structure based function-annotation of hypothetical protein MGG_01005 from Magnaporthe oryzae reveals it is the dynein light chain orthologue of dynlt1/3

A cryptic RNA-binding domain mediates Syncrip recognition and exosomal partitioning of miRNA targets

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