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
Sec1/Munc-18 (SM) proteins are essential for intracellular membrane fusion reactions. Most of them bind to membrane-associated soluble N-ethylmaleimide-sensitive fusion (NSF)-attachment protein receptors (SNAREs) of the syntaxin subfamily but it is unclear whether regulating syntaxins is their primary role. Recent studies now have shown that the mechanism of syntaxin binding is not conserved, even though the structures of both protein families are. Amazing as this might be for those considering the evolution of conserved folds, it leaves the question of how SM proteins operate in membrane fusion unanswered.
Download full-text PDF |
Source |
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http://dx.doi.org/10.1016/S0968-0004(03)00028-8 | DOI Listing |
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