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		<id>http://istoriya.soippo.edu.ua/api.php?action=feedcontributions&amp;feedformat=atom&amp;user=Plowjoke0</id>
		<title>HistoryPedia - Внесок користувача [uk]</title>
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		<link rel="alternate" type="text/html" href="http://istoriya.soippo.edu.ua/index.php?title=%D0%A1%D0%BF%D0%B5%D1%86%D1%96%D0%B0%D0%BB%D1%8C%D0%BD%D0%B0:%D0%92%D0%BD%D0%B5%D1%81%D0%BE%D0%BA/Plowjoke0"/>
		<updated>2026-04-30T15:58:02Z</updated>
		<subtitle>Внесок користувача</subtitle>
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	<entry>
		<id>http://istoriya.soippo.edu.ua/index.php?title=THYLENE-DEPENDENT_GRAVITROPISM-DEFICIENT_AND_YELLOW-GREEN-LIKE_2_(EGY2)_UBIQUITIN-SPECIFIC_PROTEASE_five_(UBP5)_UBIQUITIN-SPECIFIC_PROTEASE_6_(UBP&amp;diff=280745</id>
		<title>THYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN-LIKE 2 (EGY2) UBIQUITIN-SPECIFIC PROTEASE five (UBP5) UBIQUITIN-SPECIFIC PROTEASE 6 (UBP</title>
		<link rel="alternate" type="text/html" href="http://istoriya.soippo.edu.ua/index.php?title=THYLENE-DEPENDENT_GRAVITROPISM-DEFICIENT_AND_YELLOW-GREEN-LIKE_2_(EGY2)_UBIQUITIN-SPECIFIC_PROTEASE_five_(UBP5)_UBIQUITIN-SPECIFIC_PROTEASE_6_(UBP&amp;diff=280745"/>
				<updated>2018-01-26T16:44:37Z</updated>
		
		<summary type="html">&lt;p&gt;Plowjoke0: Створена сторінка: 7 Feasible mechanisms of transcriptome and [http://hs21.cn/comment/html/?171249.html Pitating or maintenance elements, influencing the onset, symptom profile, e...&lt;/p&gt;
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&lt;div&gt;7 Feasible mechanisms of transcriptome and [http://hs21.cn/comment/html/?171249.html Pitating or maintenance elements, influencing the onset, symptom profile, effect, course] proteome regulations by ASK1-E3s. The transcription elements are stabilized in ask1 mutant and activate or repress downstream gene transcription. TF+, transcriptional activators; TF-, transcriptional repressors. b ASK1-E3s might destabilize substrate X, which positively regulates the abundance of target proteins Y. In the ask1 mutant proteome, ASK1-E3 substrate X and their target protein Y accumulate. c ASK1-E3s may possibly destabilize substrate X, which negatively regulates the abundance of target protein Y. In the ask1 mutant proteome, ASK1-E3 substrate X accumulates but target protein Y decreases. Bars, negative regulation; horizontal arrows, constructive regulation; dashed gray bars and horizontal arrows, missing regulations; upward arrows, enhance in abundance; downward arrows, decrease in abundanceBy integrative evaluation of transcriptome and proteome information, we found that ASK1-E3s could regulate gene expression at multiple methods, ranging from transcriptional, translational, to post-translational regulations. ASK1-E3s may perhaps destabilize transcription repressors or activators to derepress or inactivate gene transcription, respectively (Fig. 7a). Within the absence of ASK1, the accumulation of these transcriptional repressors or activators results in down-regulation or upregulation of gene transcription, respectively. However, we can't rule out the possibility that the altered transcriptome and proteome may well be indirect consequences with the ask1 mutation. The proteins accumulated in ask1 may be direct substrates of ASK1-E3s, or stabilized by ASK1-E3 [https://dx.doi.org/10.1089/jir.2013.0113 title= jir.2013.0113] substrates (Fig. 7b). By way of example, ubiquitin-specific proteases UBP5 and UBP6, which accumulate inside the ask1 proteome (Table 7), could be substrates of ASK1-E3s; UBP5 and UBP6 could deubiquitinate and protect against degradation of ubiquitinated proteins, whose protein levels are then enhanced in ask1. An example in human could be the herpesvirusassociated ubiquitin-specific protease (HAUSP), whichstabilizes a tumor suppressor p53 by deubiquitination [81]. Ribosomal proteins may well share a related mechanism: accumulation of ribosomal proteins in ask1 may raise protein synthesis; alternatively, if ribosomal proteins have extraribosomal regulatory functions, they might stabilize some proteins within a similar way as these stabilizing p53 in human [67]. In a further probable situation, ASK1-E3s might destabilize some proteolytic enzymes (e.g., E3 [http://lifelearninginstitute.net/members/bongopalm41/activity/859821/ THYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN-LIKE two (EGY2) UBIQUITIN-SPECIFIC PROTEASE 5 (UBP5) UBIQUITIN-SPECIFIC PROTEASE 6 (UBP] ubiquitin ligases orLu et al. BMC Plant Biology (2016) 16:Page 13 ofpeptidases), which can degrade other proteins (Fig. 7c), forming a double unfavorable regulation cascade. The accumulation of such proteolytic enzymes in ask1 could result in reduced levels of their proteolytic substrates. Proteasome subunits and peptidases that accumulate in ask1 may be involved in degradati.THYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN-LIKE two (EGY2) UBIQUITIN-SPECIFIC PROTEASE five (UBP5) UBIQUITIN-SPECIFIC PROTEASE six (UBP6) 20S PROTEASOME ALPHA SUBUNIT E1 (PAE1) 20S PROTEASOME ALPHA SUBUNIT D2 (PAD2) 20S PROTEASOME BETA SUBUNIT C2 (PBC2) 20S PROTEASOME BETA SUBUNIT F1 (PBF1)AT2G40930 AT1G51710 AT1G53850 AT5G66140 AT1G77440 AT3Ginformation [https://dx.doi.org/10.1037/a0022827 title= a0022827] from expression and homology. Peptidases/ proteases may ordinarily be subject to damaging regulation by ASK1-E3s, hence coupling peptidase-mediated protein processing or degradation with the UPS.Probable strategies that ASK1 regulates gene expressionFig. 7 Feasible mechanisms of transcriptome and proteome regulations by ASK1-E3s. a ASK1-E3s may perhaps regulate gene transcription by destabilizing transcription things. The transcription elements are stabilized in ask1 mutant and activate or repress downstream gene transcription.&lt;/div&gt;</summary>
		<author><name>Plowjoke0</name></author>	</entry>

	<entry>
		<id>http://istoriya.soippo.edu.ua/index.php?title=Ribosomal_protein_L16p/L10e_household_protein_Ribosomal_protein_L&amp;diff=279865</id>
		<title>Ribosomal protein L16p/L10e household protein Ribosomal protein L</title>
		<link rel="alternate" type="text/html" href="http://istoriya.soippo.edu.ua/index.php?title=Ribosomal_protein_L16p/L10e_household_protein_Ribosomal_protein_L&amp;diff=279865"/>
				<updated>2018-01-24T09:24:35Z</updated>
		
		<summary type="html">&lt;p&gt;Plowjoke0: &lt;/p&gt;
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&lt;div&gt;Two ubiquitin-specific proteases UBIQUITIN-SPECIFIC PROTEASE5 (UBP5) and UBP6 were also detected in ask1-higher proteins, suggesting that deubiquitinases, which antagonize protein ubiquitination, may also be regulated by the UPS. The BRI1 SUPPRESSOR 1 (BRS1), a secreted [http://armor-team.com/activities/p/658584/ Salt/drought anxiety tolerance in Arabidopsis. Planta. 2010;231(6):1251?0. 69. Munemasa S, Hossain MA] SERINE carboxypeptidase, is involved in brassinosteroid signaling possibly by processing some proteins [80]. Other peptidases are largely unknown exceptTable 6 Kinases enriched in ask1-only and ask1-higher proteinsKinases Enriched in ask1-only proteins AT2G17290 CALCIUM-DEPENDENT PROTEIN KINASE six (CPK6) AT4G21940 CALCIUM-DEPENDENT PROTEIN KINASE 15 (CPK15) AT5G45190 Cyclin T companion CYCT1;five AT3G48750 Cyclin-dependent kinase CELL DIVISION Manage 2 (CDC2) AT4G29810 MAP KINASE KINASE 2 (MKK2) AT3G29160 SNF1-RELATED PROTEIN KINASE 1.two (SnRK1.2) AT5G63650 SNF1-RELATED PROTEIN KINASE 2.5 (SNRK2.five) AT4G26100 CASEIN KINASE 1 (CK1) AT4G35780 ACT-like protein tyrosine kinase AT5G49470 PAS domain-containing protein tyrosine kinase AT5G11020 Protein kinase superfamily protein AT5G24010 Protein kinase superfamily protein AT5G57610 Protein kinase superfamily protein AT5G43020 Leucine-rich repeat protein kinase family protein AT3G21630 LYSM DOMAIN RECEPTOR-LIKE KINASE 1 (LYSM RLK1) AT3G14350 STRUBBELIG-RECEPTOR Family members 7 (SRF7) AT4G33240 1-phosphatidylinositol-3-phosphate (PtdIns3P) 5-kinase Enriched in ask1-higher proteins AT1G31910 GHMP kinase family protein AT2G18170 MAP KINASE 7 (ATMPK7) AT2G27970 CDK-SUBUNIT two (CKS2) [https://dx.doi.org/10.1136/bmjopen-2015-010112 title= bmjopen-2015-010112] AT3G02880 Leucine-rich repeat protein kinase family members protein AT4G21210 PPDK REGULATORY PROTEIN (RP1) AT4G35230 BR-SIGNALING KINASE 1 (BSK1)Lu et al. BMC Plant Biology (2016) 16:Web page 12 ofTable 7 Peptidases enriched in ask1-higher proteinsPeptidases AT1G01300 AT1G79720 AT1G02305 AT3G62940 AT5G43060 AT4G30610 AT4G30810 AT1G13270 AT3G14067 AT5G04710 AT5G05740 Eukaryotic aspartyl protease household protein Eukaryotic aspartyl protease family members protein Cysteine proteinases superfamily protein Cysteine proteinases superfamily protein Granulin repeat cysteine protease household protein, ESPONSIVE TO DEHYDRATION 21B (RD21B) SERINE CARBOXYPEPTIDASE 24 PRECURSOR (SCPL24); BRI1 SUPPRESSOR 1 (BRS1) SERINE CARBOXYPEPTIDASE-LIKE 29 (SCPL29) METHIONINE AMINOPEPTIDASE 1B (MAP1C) Subtilase family members protein Zn-dependent exopeptidases superfamily protein S2P-like putative metalloprotease, E.Ribosomal protein L16p/L10e household protein Ribosomal protein L22p/L17e family members protein Ribosomal protein L35Ae household protein Ribosomal protein L22p/L17e family protein RIBOSOMAL PROTEIN L34 (RPL34) Ribosomal protein L13 family protein, EMBRYO DEFECTIVE 1473 (EMB1473) Ribosomal protein L10aP, PIGGYBACK1 (PGY1) Ribosomal protein L13 family members protein Ribosomal protein L17 family members protein Ribosomal L38e protein household Ribosomal protein L13e family protein Ribosomal protein L18e/L15 superfamily protein RIBOSOMAL PROTEIN L5B (RPL5B); OLIGOCELLULA 7 (OLI7) PLANT U-BOX 12 (PUB12) with ribosomal protein L10e/L16 domain RIBOSOMAL PROTEIN S9 (RPS9) Ribosomal protein S26e loved ones protein Ribosomal protein S26e loved ones protein Ribosomal protein S24e family members protein Ribosomal protein S10p/S20e loved ones protein Ribosomal protein S26e household protein RIBOSOMAL PROTEIN S13A (RPS13A); POINTED Initial LEAF two (PFL2) Ribosomal [https://dx.doi.org/10.1038/srep43317 title= srep43317] protein S14p/S29e family members protein Ribosomal protein S14p/S29e loved ones protein Ribosomal S17 family protein Ribosomal protein S4 Ribosomal protein S24e household proteinproteasome core complicated may possibly also be regulated by UPS. Two ubiquitin-specific proteases UBIQUITIN-SPECIFIC PROTEASE5 (UBP5) and UBP6 were also detected in ask1-higher proteins, suggesting that deubiquitinases, which antagonize protein ubiquitination, may possibly also be regulated by the UPS. The BRI1 SUPPRESSOR 1 (BRS1), a secreted serine carboxypeptidase, is involved in brassinosteroid signaling possibly by processing some proteins [80].&lt;/div&gt;</summary>
		<author><name>Plowjoke0</name></author>	</entry>

	<entry>
		<id>http://istoriya.soippo.edu.ua/index.php?title=Analyzer_(Agilent_Technologies,_Santa_Clara,_CA),_controlled_by_the_Agilent_2100_Professional&amp;diff=279496</id>
		<title>Analyzer (Agilent Technologies, Santa Clara, CA), controlled by the Agilent 2100 Professional</title>
		<link rel="alternate" type="text/html" href="http://istoriya.soippo.edu.ua/index.php?title=Analyzer_(Agilent_Technologies,_Santa_Clara,_CA),_controlled_by_the_Agilent_2100_Professional&amp;diff=279496"/>
				<updated>2018-01-23T09:47:38Z</updated>
		
		<summary type="html">&lt;p&gt;Plowjoke0: Створена сторінка: The ProteinPilot computer software [http://hot-not.com/members/health2felony/activity/164932/ Ew stomatal signaling pathways. Plant Cell. 2008;20(12):3210?6. 87...&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;The ProteinPilot computer software [http://hot-not.com/members/health2felony/activity/164932/ Ew stomatal signaling pathways. Plant Cell. 2008;20(12):3210?6. 87. Zhu W, Smith JW, Huang] version four.two was applied to perform protein identification by searching MS spectra against the protein database which integrated the Arabidopsis thaliana protein list TAIR10_pep_20101214, 156 prevalent human and lab contaminants (ABSciex_ContaminantDB_20070711), and also a reverse &amp;quot;decoy&amp;quot; version of your protein database itself (concatenated Reverse Decoy.Analyzer (Agilent Technologies, Santa Clara, CA), controlled by the Agilent 2100 Professional software, using the Plant RNA Nano assay following the RNA 6000 Nano kit protocol. Microarray signal values had been averaged from biological replicates of each and every genotype and compared amongst ask1 and Ler to find differentially expressed genes which show at the very least 2-fold variations in RNA levels and p-value [https://dx.doi.org/10.1089/jir.2013.0113 title= jir.2013.0113] the Proteomics and Mass Spec Core Facility, College of Medicine, Pennsylvania State University, Hershey, PA.Mass spectrometry analysis/MudPITThe protein extraction system was modified from a earlier study [85]. Floral buds have been ground completely in liquid nitrogen with mortars and pestles plus the powder [https://dx.doi.org/10.1136/bmjopen-2015-010112 title= bmjopen-2015-010112] was suspended in -20   Acetone with ten   w/v Trichloroacetic Acid (TCA) and 0.07   (v/v) Mercaptoethanol (1 ml for 0.3 g of tissue powder). AfterTrypsin-digested peptide samples were analyzed by MudPIT in line with the 2D LC-MALDI separation and evaluation procedures published previously applying a 4800 proteomic analyzer MALDI TOF/TOF tandem program (Applied Biosysems) [86] except many modifications. The ProteinPilot application version 4.two was applied to carry out protein identification by looking MS spectra against the protein database which incorporated the Arabidopsis thaliana protein list TAIR10_pep_20101214, 156 common human and lab contaminants (ABSciex_ContaminantDB_20070711), as well as a reverse &amp;quot;decoy&amp;quot; version of your protein database itself (concatenated Reverse Decoy.&lt;/div&gt;</summary>
		<author><name>Plowjoke0</name></author>	</entry>

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