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
Malaria is a devastating human parasitic disease that receives enhanced attention due to the emergence of resistance to traditional drugs. Thus, the search for new molecular targets is a major goal. PfAM1 is an aminopeptidase from Plasmodium falciparum, William H. Welch 1897, belonging to the M1 family of metalloproteases, which is a promising target of inhibitors to block the intra-erythrocytic stages of the parasite. Since its identification in 1998, many efforts have been done to validate PfAM1 as an appropriate target of antimalarials. The present work is a critical review of the main structural, functional and kinetic characteristics of PfAM1, as well as a summary of the effects of key inhibitors at molecular and cellular levels. The systematization of experimental results should contribute to a better understanding of the properties of PfAM1 as a target of antimalarials and promote research projects focused on the development of PfAM1 inhibitors.
Download full-text PDF |
Source |
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http://dx.doi.org/10.2174/1389450115666141024115641 | DOI Listing |
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