Severity: Warning
Message: file_get_contents(https://...@gmail.com&api_key=61f08fa0b96a73de8c900d749fcb997acc09&a=1): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 197
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 197
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 271
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3165
Function: getPubMedXML
File: /var/www/html/application/controllers/Detail.php
Line: 597
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 511
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 317
Function: require_once
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Post-translational modifications (PTM) involve chemical modifications of amino acid residues within histone and non-histone proteins and are chemically diverse. PTM plays a vital role in regulating the chromatin structure in the nucleus, thus gene regulation. Among the various PTM, reversible acetylation of histone non-histone proteins has fundamental functions in various cellular processes. In all organisms, histone acetylation of lysine residues is connected with transcription activation. Acetyltransferases and deacetylases are well-known enzymes in the acetylation of the histone and non-histone proteins. This chapter will review the latest progress in histone and non-histone reversible acetylation epigenetic alterations and mechanisms and summarize how they affect development, aging, and diseases.
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http://dx.doi.org/10.1007/978-3-031-91459-1_1 | DOI Listing |