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: 1034
Function: getPubMedXML
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3152
Function: GetPubMedArticleOutput_2016
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
The regulation of unfolded protein response (UPR) sensors has been studied for over 20 years, but IRE1β has remained a mystery. IRE1β is highly expressed in goblet cells: specialized epithelial cells that secrete mucus. Two articles in this issue show that IRE1β is held in an inactive state by the goblet cell-specific chaperone AGR2; upon dissociation of AGR2, IRE1β dimerizes and becomes active. This mechanism is reminiscent of the dynamic control by BiP of three other UPR sensors: IRE1α, PERK and ATF6.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10907747 | PMC |
http://dx.doi.org/10.1038/s44318-024-00041-4 | DOI Listing |
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!