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
Selective protein degradation depends on their quality being controlled by the cellular system, which includes chaperones involved in protein folding and two degradation systems, the proteasomal and lysosomal. CHIP (carboxyl terminus of Hsp70-interacting protein), an E3 ubiquitin ligase and co-chaperone, serves as a chaperone-degradation system interface. This article reviews the molecular characteristics of CHIP protein, the mechanism of its action, and its role in cellular metabolism and discusses how CHIP dysfunction may lead to neurodegenerative diseases.
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