Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText.
Kick-your-searchterm to multiple Engines kick-your-query now !>
A dictionary by aggregated review articles of nephrology, medicine and the life sciences
Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

suck abstract from ncbi


10.1042/BCJ20170046

http://scihub22266oqcxt.onion/10.1042/BCJ20170046
suck pdf from google scholar
C5423082!5423082!28302767
unlimited free pdf from europmc28302767    free
PDF from PMC    free
html from PMC    free

suck abstract from ncbi


Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534

Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534
pmid28302767      Biochem+J 2017 ; 474 (10): 1741-54
Nephropedia Template TP

gab.com Text

Twit Text FOAVip

Twit Text #

English Wikipedia


  • Effect of different ?-subunit isoforms on the regulation of AMPK #MMPMID28302767
  • Willows R; Navaratnam N; Lima A; Read J; Carling D
  • Biochem J 2017[May]; 474 (10): 1741-54 PMID28302767show ga
  • AMP-activated protein kinase (AMPK) plays a key role in integrating metabolic pathways in response to energy demand. AMPK activation results in a wide range of downstream responses, many of which are associated with improved metabolic outcome, making AMPK an attractive target for the treatment of metabolic diseases. AMPK is a heterotrimeric complex consisting of a catalytic subunit (?) and two regulatory subunits (? and ?). The ?-subunit harbours the nucleotide-binding sites and plays an important role in AMPK regulation in response to cellular energy levels. In mammals, there are three isoforms of the ?-subunit and these respond differently to regulation by nucleotides, but there is limited information regarding their role in activation by small molecules. Here, we determined the effect of different ?-isoforms on AMPK by a direct activator, 991. In cells, 991 led to a greater activation of ?2-containing AMPK complexes compared with either ?1 or ?3. This effect was dependent on the long N-terminal region of the ?2-isoform. We were able to rule out an effect of Ser108 phosphorylation, since mutation of Ser108 to alanine in the ?2-isoform had no effect on activation of AMPK by 991 in either ?1- or ?2-complexes. The rate of dephosphorylation of Thr172 was slower for ?2- compared with ?1-complexes, both in the absence and presence of 991. Our studies show that activation of AMPK by 991 depends on the nature of the ?-isoform. This finding may have implications for the design of isoform-selective AMPK activators.
  • ä


  • DeepDyve
  • Pubget Overpricing
  • suck abstract from ncbi

    Linkout box