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Träfflista för sökning "WFRF:(MANNERVIK B) srt2:(2000-2004)"

Search: WFRF:(MANNERVIK B) > (2000-2004)

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1.	Dreij, K, et al. (author) Catalytic activities of human alpha class glutathione transferases toward carcinogenic dibenzo[a,l]pyrene diol epoxides 2002 In: Chemical research in toxicology. - : American Chemical Society (ACS). - 0893-228X .- 1520-5010. ; 15, s. 825-831 Journal article (peer-reviewed)
2.	Njalsson, R, et al. (author) Kinetic properties of missense mutations in patients with glutathione synthetase deficiency 2000 In: The Biochemical journal. - 0264-6021. ; 349:Pt 1, s. 275-279 Journal article (peer-reviewed)
3.	Cocco, R, et al. (author) The folding and stability of human alpha class glutathione transferase A1-1 depend on distinct roles of a conserved N-capping box and hydrophobic staple motif 2001 In: JOURNAL OF BIOLOGICAL CHEMISTRY. - : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC. - 0021-9258. ; 276:34, s. 32177-32183 Journal article (peer-reviewed)abstract An N-capping box and a hydrophobic staple motif are strictly conserved in the core of all known glutathione S-transferases (GST). In the present work, mutations of hGSTA1-1 enzyme residues forming these motifs have been generated. The analysis of S154A, D
4.	Dragani, B, et al. (author) Role of conserved local motifs in folding and stability of hGSTP1-1 2001 In: CHEMICO-BIOLOGICAL INTERACTIONS. - : ELSEVIER SCI IRELAND LTD. - 0009-2797. ; 133:1-3, s. 17-18 Journal article (peer-reviewed)abstract We investigated, by site directed mutagenesis, the role played by a conserved N-capping box and hydrophobic staple motif in the folding and stability of human GSTPl-1. The corresponding mutants, I149A, S150A, D153A and Y154A, in which these motifs have be
5.	Dreij, K, et al. (author) Inactivation of carcinogenic diol epoxides of dibenzo[a,l]pyrene (dibenzo[def,p]chrysene) by human alpha class glutathione transferases 2002 In: POLYCYCLIC AROMATIC COMPOUNDS. - : Informa UK Limited. - 1040-6638 .- 1563-5333. ; 22, s. 823-829 Journal article (other academic/artistic)
6.	Hamilton, DS, et al. (author) Mechanism of the glutathione transferase-catalyzed conversion of antitumor2-crotonyloxymethyl-2-cycloalkenones to GSH adducts. 2003 In: J Am Chem Soc. ; 125, s. 15049- Journal article (peer-reviewed)
7.	Jiang, FY, et al. (author) Examination of the transcription factor NtcA-binding motif by in vitro selection of DNA sequences from a random library 2000 In: Journal of Molecular Biology. - : Elsevier BV. - 0022-2836 .- 1089-8638. ; 301:4, s. 783-793 Journal article (peer-reviewed)abstract A recursive in vitro selection among random DNA sequences was used for analysis of the cyanobacterial transcription factor NtcA-binding motifs. An eight-base palindromic sequence, TGTA-(N-8)-TACA, was found to be the optimal NtcA-binding sequence. The mor
8.	Mannervik, B, et al. (author) Evolutionary design of glutathione-linked proteins in vivo and in vitro based on sampling of modules from pre-existing structures 2001 In: CHEMICO-BIOLOGICAL INTERACTIONS. - : ELSEVIER SCI IRELAND LTD. - 0009-2797. ; 133:1-3, s. 3-6 Journal article (peer-reviewed)abstract Structural studies suggest that naturally occurring proteins represent a limited number of folds. It would appear that the evolution of novel protein functions to a large extent involves redesign of stable peptide scaffolds by means of combinatorial prote
9.	Stenberg, G, et al. (author) A conserved "hydrophobic staple motif" plays a crucial role in the refolding of human glutathione transferase P1-1 2000 In: JOURNAL OF BIOLOGICAL CHEMISTRY. - : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC. - 0021-9258. ; 275:14, s. 10421-10428 Journal article (peer-reviewed)abstract The specific (i, i+5) hydrophobic staple interaction involving a helix residue and a second residue located in the turn preceding the helix is a recurrent motif at the N terminus of alpha-helices, This motif is strictly conserved in the core of all solubl
10.	Stenberg, G, et al. (author) A conserved 'hydrophobic staple motif' plays a crucial role in the refolding of human glutathione transferase Pl-l 2001 In: CHEMICO-BIOLOGICAL INTERACTIONS. - : ELSEVIER SCI IRELAND LTD. - 0009-2797. ; 133:1-3, s. 49-50 Journal article (peer-reviewed)abstract A hydrophobic staple motif is strictly conserved in the core of all soluble glutathione transferases (GSTs) as well as in other protein structures. The role of this local interaction in folding and stability of human GSTP1-1 has been analysed by site dire

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Result 1-10 of 32

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Type of publication: journal article (30); review (2)

Type of content: peer-reviewed (28); other academic/artistic (4)

Author/Editor: Mannervik, B. (32); Stenberg, G. (8); WIDERSTEN, M (6); Johansson, AS (5); Jemth, P (5); Gustafsson, A (4); show more...; Hubatsch, I (4); Cocco, R (4); Dragani, B (4); Aceto, A (4); Hansson, LO (3); Persson, MAA (2); Ridderstrom, M (2); Morgenstern, R (2); Dreij, K (2); Cameron, AD (2); Seidel, A (2); Jernstrom, B (2); Sundberg, K (2); Olin, B (2); Principe, DR (2); Edalat, M (2); Zhang, X. (1); Carlsson, K (1); Carlsson, B (1); Jiang, FY (1); Persson, B (1); Larsson, A (1); Bergman, B (1); Pettersson, S (1); Norgren, S (1); Andersson, AK (1); Svensson, R (1); Hasler, JA (1); Ding, Z. (1); Jones, TA (1); Lien, S. (1); Parker, MW (1); Njalsson, R (1); BOARD, PG (1); Nordling, E (1); Creighton, DJ (1); Paludi, D (1); Frickel, EM (1); Gardner, JL (1); Bammler, TK (1); Gallagher, EP (1); Hamilton, DS (1); Houk, KN (1); Ganem, B (1); show less...

University: Uppsala University (29); Karolinska Institutet (7)

Language: English (32)

Research subject (UKÄ/SCB): Natural sciences (2)

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