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
Transfer RNA-mediated posttranslational protein modification by arginine has been demonstrated in vitro in axoplasm extruded from the giant axons of squid and in injured and regenerating vertebrate nerves. In nerve and axoplasm, the highest activity is found in a fraction of a 150,000 × g supernatant containing high molecular weight protein/RNA complexes but lacking molecules of <5 kDa. Arginylation (and protein modification by other amino acids) is not found in more purified, reconstituted fractions. The data are interpreted as indicating that it is critical to recover the reaction components in high molecular weight protein/RNA complexes in order to maintain maximum physiological activity. The level of arginylation is greatest in injured and growing vertebrate nerves compared with intact nerves, suggesting a role for these reactions in nerve injury/repair and during axonal growth.
Download full-text PDF |
Source |
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http://dx.doi.org/10.1007/978-1-4939-2935-1_4 | DOI Listing |
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