Severity: Warning
Message: file_get_contents(https://...@pubfacts.com&api_key=b8daa3ad693db53b1410957c26c9a51b4908&a=1): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 176
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 176
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 250
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3122
Function: getPubMedXML
File: /var/www/html/application/controllers/Detail.php
Line: 575
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 489
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 316
Function: require_once
To respond to environmental changes, plants have developed complex mechanisms that allow them to rapidly perceive and respond to abiotic stresses. Late embryogenesis abundant (LEA) proteins are a large and diverse family that play important roles in environmental stress tolerance in plants. Dehydrins belong to group II LEA proteins, which are considered stress proteins involved in the formation of plants' protective reactions to dehydration. Some studies have demonstrated that dehydrins could binding metal ions or lipid vesicles. experiments revealed that dehydrins could protect the activity of enzyme from damage caused by environmental stress. Although many studies have been conducted to understand their roles in abiotic stresses, the molecular function of dehydrins is still unclear. In this review, to generate new ideas for elucidating dehydrins' functions, we highlight the functional characteristics of dehydrins to understand their roles under environmental stress in plants.
Download full-text PDF |
Source |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5465263 | PMC |
http://dx.doi.org/10.3389/fpls.2017.01018 | DOI Listing |
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