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
PIM kinases are oncogenic serine/threonine kinases, the expression and activities of which are tightly regulated in normal tissues, but upregulated in many types of human malignancies, including both hematological and solid cancers. Since high PIM expression levels have been connected to cancer progression and poor patient survival, PIM kinases have become attractive targets for drug development. Many downstream targets have also been identified, through which PIM kinases promote cell survival, proliferation and metabolism. More recently, PIM kinases have been implicated in regulation of cell motility, which also plays an important role in tumor growth and cancer progression. This review summarizes effects of PIM kinases and their substrates especially on cancer cell migration, invasion and metastatic growth, based on data from cell-based assays, animal experiments and patients.
Download full-text PDF |
Source |
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http://dx.doi.org/10.1016/j.biocel.2017.10.016 | DOI Listing |
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