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The same amino acid can be carried by different tRNA'S.

Drag-and-Drop Protein Synthesis: Quiz - zeroBio

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Ahmed AS, Dew T, Lawton FG, PapadopoulosAJ, Devaja O, Raju KS and Sherwood RA: M2-PK as a novel marker inovarian cancer. A prospective cohort study. Eur J Gynaecol Oncol.28:83–88. 2007.

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The dissociative chemisorption of methane on a metal catalyst is the rate limiting step in the steam reforming of natural gas, our primary source for the molecular hydrogen used in the Haber-Bosch process. In collaboration with the experimental group of Rainer Beck at the École Polytechnic Fédéral de Lausanne, we examined this reaction on a Pt surface containing step defects. We were able to differentiate between reactions at the step edges and the terrace sites, using both UHV molecular beam experiments and high-dimensional quantum scattering theory. Both approaches were also able to resolve the reaction probability with respect to the velocity and vibrational state of the methane molecule and the surface temperature, providing additional details about the reaction mechanism.

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Weinberger R, Appel B, Stein A, Metz Y,Neheman A and Barak M: The pyruvate kinase isoenzyme M2 (Tu M2-PK)as a tumour marker for renal cell carcinoma. Eur J Cancer Care(Engl). 16:333–337. 2007. : :

Bonnet S, Archer SL, Allalunis-Turner J,Haromy A, Beaulieu C, Thompson R, Lee CT, Lopaschuk GD, PuttaguntaL, Bonnet S, et al: A mitochondria-K+ channel axis issuppressed in cancer and its normalization promotes apoptosis andinhibits cancer growth. Cancer Cell. 11:37–51. 2007. : :

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PKM2 acts as a proliferative agent through itsinteraction with nuclear proteins, and as a differentiating agentthrough its interaction with octamer-binding transcription factor 4(Oct4), which is a key regulator in cancer stem cell self-renewaland differentiation (). In gliomastem cells, the interaction between PKM2 and Oct4 inhibits theability of PKM2 to maintain cell stemness, thereby promoting celldifferentiation and enhancing the sensitivity of cells to celldeath, which is concomitant with an alteration between the dimerand tetramer states of PKM2 ().Notably, dichloroacetate, which is known as an inhibitor of PDK1and is involved in the mitochondrial tricarboxylic acid cycle,increases the number of PKM2/Oct4 complexes ().

PKM2 not only acts as a coactivator, but may alsoact as a protein kinase that phosphorylates substrates involved inmetabolic reprogramming. Nuclear dimeric PKM2 directlyphosphorylates signal transducer and activator of transcription 3(STAT3), which is activated in response to inflammatory cytokines,including interleukin-6 (). PKM2uses PEP as a phosphate donor to phosphorylate STAT3 attyrosine-705, which activates the transcription ofmitogen-activated protein kinase kinase 5. The activation of STAT3in malignant cancer cells is possibly one of the most importantmolecular signatures for promoting the progression of cancer. PKM2overexpression facilitates STAT3 nuclear translocation, whichregulates the aggressive progression of colorectal cancer (). The functional implications of thestudy by Yang ()indicate that PKM2 activates β1-integrin-focal adhesion kinase andsnail-2-E-cadherin signaling, and also upregulates the expressionof matrix metalloproteinase-2 and 9, which induces cell migrationand adhesion. Similarly to STAT3, histone H3 is a substrate forPKM2 kinase activity (). PKM2directly binds and phosphorylates histone H3 at threonine-11, whichleads to the removal of HDAC3 from CCND1 and Myc promoter regions,subsequent to acetylation at lysine-9 and gene transcription(). PKM2-dependent histone H3modifications are key to EGF stimulation (). Furthermore, nuclear PKM2 levels areassociated with phosphorylation at proline-3/threonine-11 inmalignant glioma (). Recently, astudy reported that the PKM2-SAICAR interaction is required andsufficient to induce robust protein kinase activity in PKM2 and in cancer cells ().It was also reported that the PKM2-SAICAR complex phosphorylates>100 human proteins, the majority of which were previouslyunrecognized. In particular, PKM2-SAICAR directly activates ERK1; however, activated ERK1/2 phosphorylates PKM2,creating a positive feedback loop (). Additionally, when EGFR is activated,the concentration of cellular SAICAR is increased, which isrequired to sustain the activation of ERK1/2 and proliferativesignaling via PKM2 ().

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  • epidermal growth factor receptor

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  • nuclear factor κ enhancer bindingprotein

    When amino acids are brought in by tRNA, they are joined together by hydrolysis reactions to form the growing protein.

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    Whenever a cell needs to, it can unzip DNA and make a transcript of a sequence so that a protein can be made.

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PKM2 detected in the blood of patients withgastrointestinal, pancreatic, lung and ovarian cancer and renalcell carcinoma revealed that PKM2 is released into the circulation(). The PKM2 levels in thecirculation of patients may be used as a diagnostic marker fornumerous types of cancer (). Arecent study suggested that PKM2 in the blood circulationfacilitated tumor growth by promoting tumor angiogenesis (). The study demonstrated that PKM2promoted tumor angiogenesis by increasing endothelial cellproliferation, migration and extracellular matrix-cell adhesions;only dimeric PKM2 was observed to be involved in tumorangiogenesis.

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Cancer-specific metabolism, which is closelyassociated with tumorigenicity, cancer aggressive progression andinherent or acquired therapeutic resistance, is an attractivetarget for cancer therapy. The role of PKM2 in glycolysis and theproliferation of cancer cells has been revealed, and has beendemonstrated to balance the production of biomolecular buildingblocks and the generation of pyruvate and ATP. Consequently, thereare two therapeutic strategies for targeting PKM2. The first isinhibitors that block the catalytic activity of PKM2, and thesecond is activators that induce tetramerization of PKM2 toincrease glycolysis.

Most proteins fold into unique 3-dimensional structures

Inhibitors of PKM2 appear to rely on the hypothesisthat proliferating cells are highly dependent on energy, and areduced activity of PKM2 inhibits energy regeneration. Using a highthroughput screen, small molecules have been identified thatselectively inhibit PKM2 (). Thesemolecules target the allosteric FBP binding site of PKM2; however,since PKL and PKR are also activated by FBP, there may be toxicityissues for human cancer therapy if PK activity is inhibited in theliver and red blood cells. Natural products, such as shikonin andits analog alkannin, which belong to a family of necroptoticinducers, demonstrated potent and promising selective inhibition ofPKM2 that did not inhibit PKM1 and PKL (). However, PKM2 inhibition by these drugsis partially reversed by the addition of FBP to proteinlysates.

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PKM2 is not only present in the cytoplasm of cellsas a PK enzyme, but also translocates to the nucleus, whichsuggests PKM2 has functions in addition to glycolysis (,). Therehas been a resurgence of interest in the metabolic effects of PKM2,and there have been recent studies revealing non-metabolicfunctions of PKM2. It has been reported that PKM2 translocates intothe nucleus and interacts directly with the HIF-1α subunit andpromotes transactivation of HIF-1 target genes by enhancing HIF-1binding and recruitment of p300, a transcriptional coactivator,which regulates HIF-1 activity (,). PKM2gene transcription is also activated by HIF-1, which creates apositive feedback loop that promotes HIF-1 transactivation andalters glucose metabolism in cancer cells (). The Jumonji C domain-containingdioxygenase Jumonji domain-containing protein 5 (JMJD5) directlyinteracts with PKM2, which induces the translocation of PKM2 intothe nucleus and promotes HIF-1α mediated transactivation (). The JMJD5-PKM2 interaction occurs atthe intersubunit interface region of PKM2, which hinders PKM2tetramerization and blocks PK activity.

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