Search results for "5'"

showing 10 items of 358 documents

Genomic structure and functional characterization of the human ADAM10 promoter

2005

The ADAM10 gene encodes a membrane-bound disintegrin-metalloproteinase, which, after overexpression in an Alzheimer disease (AD) mouse model, prevents amyloid pathology and improves long-term potentiation and memory. Because enhancing ADAM10 expression appears to be a reasonable approach for treatment of AD, we functionally analyzed the ADAM10 gene. Both human and mouse ADAM10 genes comprise approximately 160 kbp, are composed of 16 exons, and are evolutionarily highly conserved within 500 bp upstream of either translation initiation site. By using luciferase reporter assays, we demonstrate that nucleotides -2179 to -1 upstream of the human ADAM10 translation initiation site represent a fun…

5' Flanking Region5' flanking regionTretinoinBiologyPolymorphism Single NucleotideBiochemistryCell LineConserved sequenceADAM10 ProteinMiceOpen Reading FramesExonAlzheimer DiseaseGeneticsAnimalsHumansPromoter Regions GeneticMolecular BiologyTranscription factorGeneConserved SequenceExpressed Sequence TagsIntronMembrane ProteinsPromoterExonsMolecular biologyIntronsADAM ProteinsOpen reading frameMutagenesis Site-DirectedAmyloid Precursor Protein SecretasesBiotechnologyThe FASEB Journal
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Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29

2002

Abstract ERp29 is a soluble protein localized in the endoplasmic reticulum (ER) of eukaryotic cells, which is conserved in all mammalian species. The N-terminal domain of ERp29 displays sequence and structural similarity to the protein disulfide isomerase despite the lack of the characteristic double cysteine motif. Although the exact function of ERp29 is not yet known, it was hypothesized that it may facilitate folding and/or export of secretory proteins in/from the ER. ERp29 is induced by ER stress, i.e. accumulation of unfolded proteins in the ER. To gain an insight into the mechanisms regulating ERp29 expression we have cloned and characterized the rat ERp29 gene and studied in details …

5' Flanking RegionRecombinant Fusion ProteinsMolecular Sequence DataCHO CellsBiologyCell LineMiceCricetinaeSequence Homology Nucleic AcidGene expressionTumor Cells CulturedGeneticsAnimalsHumansRNA MessengerLuciferasesPromoter Regions GeneticProtein disulfide-isomeraseGeneHeat-Shock ProteinsPhylogenyBase SequenceGene Expression ProfilingEndoplasmic reticulumPromoter3T3 CellsDNAExonsSequence Analysis DNAGeneral MedicineMolecular biologyIntronsRatsHousekeeping geneSecretory proteinGenesUnfolded protein responseFemaleTranscription Initiation SiteSequence AlignmentHeLa CellsGene
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Sequence of a sea urchin hsp70 gene and its 5' flanking region.

1990

We report the nucleotide sequence of a 4470-bp fragment derived from a sea urchin genomic clone containing part of a heat-shock protein 70 (Hsp70)-encoding gene. This fragment, named hsp70 gene II, contains 1271 bp of the flanking region and 3299 bp of structural gene sequence interrupted by five introns and encoding the N-terminal 371 amino acids (aa) of the protein. The 5' flanking region contains a putative TATA element, two CCAAT boxes, four heat-shock consensus sequence elements (hse) and one consensus sequence for binding of Sp1. Remarkable homologies were observed for deduced aa sequence and intron-exon organization between hsp70 gene II and rat hsc73 gene.

5' flanking regionMolecular Sequence DataRestriction MappingBiologyExonSequence Homology Nucleic AcidConsensus SequenceGeneticsConsensus sequenceAnimalsAmino Acid SequencePromoter Regions GeneticGenePeptide sequenceHeat-Shock ProteinsGeneticsBase SequenceStructural geneNucleic acid sequenceGeneral MedicineExonsMolecular biologyIntronsGenesRegulatory sequenceSea UrchinsGene
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CCDC 1441505: Experimental Crystal Structure Determination

2018

Related Article: Michael G. S. Londesborough, Jiří Dolanský, Tomáš Jelínek, John D. Kennedy, Ivana Císařová, Robert D. Kennedy, Daniel Roca-Sanjuán, Antonio Francés-Monerris, Kamil Lang, William Clegg|2018|Dalton Trans.|47|1709|doi:10.1039/C7DT03823B

5'6':56-conjuncto-(10'-(pyridine-N)-6'7':8'9'-di-muH-nido-decaborane)-(67:89:910-tri-muH-nido-decaborane)Space GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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CCDC 2009112: Experimental Crystal Structure Determination

2020

Related Article: Jonathan Bould, Kamil Lang, Kaplan Kirakci, Luis Cerdán, Daniel Roca-Sanjuán, Antonio Francés-Monerris, William Clegg, Paul G. Waddell, Marcel Fuciman, Tomáš Polívka, Michael G. S. Londesborough|2020|Inorg.Chem.|59|17058|doi:10.1021/acs.inorgchem.0c02277

5'6':67-conjuncto-(22'-dichloro-11'33'44'-hexamethyl-6'7':8'9':9'10'-tri-muH-nido-decaborane)-(77'88'10'-pentamethyl-56:89:910-tri-muH-nido-decaborane) 5'6':67-conjuncto-(22'-dichloro-11'33'44'-hexamethyl-6'7':8'9':9'10'-tri-muH-nido-decaborane)-(77'88'1010'-hexamethyl-56:89:910-tri-muH-nido-decaborane)Space GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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CCDC 104990: Experimental Crystal Structure Determination

1999

Related Article: W.Wasikiewicz, G.Rokicki, J.Kielkiewicz, E.F.Paulus, V.Bohmer|1997|Monatsh.Chem.|128|863|doi:10.1007/BF00807096

55'11'1717'23'-Hexa-t-butyl-2525'262727'28-hexahydroxy-1124':2326'-dibutoxobis(calix(4)arene) acetonitrile chloroform solvateSpace GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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CCDC 689511: Experimental Crystal Structure Determination

2009

Related Article: A.Bogdan, M.Bolte, V.Bohmer|2008|Chem.-Eur.J.|14|8514|doi:10.1002/chem.200801268

55'-(33'-(Icosane-120-diyldioxy)-bis(3-phenylureido))-bis(1117-(33'-(decane-110-diyldioxy)-bis(3-phenylureido))-23-(3-(35-di-t-butylphenyl)ureido)-25262728-tetrakis(pentyloxy)calix(4)arene) bis(acetonitrile) clathrate acetonitrile chloroform solvateSpace GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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CCDC 1994473: Experimental Crystal Structure Determination

2020

Related Article: Justin J. Dressler, Joshua E. Barker, Lucas J. Karas, Hannah E. Hashimoto, Ryohei Kishi, Lev N. Zakharov, Samantha N. MacMillan, Carlos J. Gomez-Garcia, Masayoshi Nakano, Judy I. Wu, Michael M. Haley|2020|J.Org.Chem.|85|10846|doi:10.1021/acs.joc.0c01387

614-bis(4-t-butyl-26-dimethylphenyl)-513-[1]benzothieno[2''3'':2'3']indeno[5'6':56]indeno[21-b][1]benzothiophene-551313-tetrone acetonitrile solvateSpace GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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CCDC 2077067: Experimental Crystal Structure Determination

2021

Related Article: Joshua E. Barker, Tavis W. Price, Lucas J. Karas, Ryohei Kishi, Samantha N. MacMillan, Lev N. Zakharov, Carlos J. G��mez���Garc��a, Judy I. Wu, Masayoshi Nakano, Michael M. Haley|2021|Angew.Chem.,Int.Ed.|60|22385|doi:10.1002/anie.202107855

614-bis(4-t-butyl-26-dimethylphenyl)[1]benzofuro[2''3'':2'3']indeno[5'6':56]indeno[21-b][1]benzofuran chloroform solvateSpace GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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CCDC 1949404: Experimental Crystal Structure Determination

2020

Related Article: Joshua E. Barker, Justin J. Dressler, Abel Cárdenas Valdivia, Ryohei Kishi, Eric T. Strand, Lev N. Zakharov, Samantha N. MacMillan, Carlos J. Gómez-García, Masayoshi Nakano, Juan Casado, Michael M. Haley|2019|J.Am.Chem.Soc.|142|1548|doi:10.1021/jacs.9b11898

614-bis(4-t-butyl-26-dimethylphenyl)[1]benzothieno[2''3'':2'3']indeno[5'6':56]indeno[21-b][1]benzothiophene chloroform solvateSpace GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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