The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit-Reference-Cited by-同舟云学术

The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit

Published:2016-05 Issue:20 Volume:291 Page:10893-10903
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Cuevas-Velazquez Cesar L.,Saab-Rincón Gloria,Reyes José Luis,Covarrubias Alejandra A.

Funder

Consejo Nacional de Ciencia y Tecnología

Dirección General Asuntos del Personal Académico, Universidad Nacional Autónoma de México

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference60 articles.

1. Plant responses to water deficit;Bray;Trends Plant Sci,1997

2. The enigmatic LEA proteins and other hydrophilins;Battaglia;Plant Physiol,2008

3. LEA (late embryogenesis abundant) proteins and their encoding genes in Arabidopsis thaliana;Hundertmark;BMC Genomics,2008

4. Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit;Garay-Arroyo;J. Biol. Chem,2000

5. Intrinsically unstructured proteins and their functions;Dyson;Nat. Rev. Mol. Cell Biol,2005

Cited by 69 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Biomolecular condensates in plant cells: Mediating and integrating environmental signals and development;Plant Science;2024-10

2. HcLEA113, a late embryogenesis abundant protein gene, positively regulates drought‐stress responses in kenaf;Physiologia Plantarum;2024-07

3. Genome-wide identification of the LEA gene family in Panax ginseng: Evidence for the role of PgLEA2-50 in plant abiotic stress response;Plant Physiology and Biochemistry;2024-07

4. Disordered proteins interact with the chemical environment to tune their protective function during drying;2024-06-21

5. Disordered proteins interact with the chemical environment to tune their protective function during drying;2024-06-21