Search

Your search keyword '"Mannervik B"' showing total 690 results
Start Over Author "Mannervik B"
690 results on '"Mannervik B"'

8. Inhibitory effects of ethacrynic acid on glutathione S-transferase A1-1 from Callithrix jacchus

Author

Aksoy, N. H., Mannervik, B., and [Aksoy, N. H.] Aksaray Univ, Dept Biochem, Aksaray, Turkey -- [Aksoy, N. H. -- Mannervik, B.] Uppsala Univ, Dept Biochem & Organ Chem, BMC, Uppsala, Sweden

Abstract

40th Congress of the Federation-of-European-Biochemical-Societies (FEBS) - The Biochemical Basis of Life -- JUL 04-09, 2015 -- Berlin, GERMANY, WOS: 000362570606120, Federat European Biochemical Soc

Published
2015

12. Molecular cloning, expression, purification and characterization of wild type and mutant marmoset alpha class glutathione transferase

Author

Aksoy, N. H., Mannervik, B., Raffalli-Mathieu, F., Veteriner Fakültesi, and [Aksoy, N. H. -- Mannervik, B. -- Raffalli-Mathieu, F.] Uppsala Univ, Dept Biochem & Organ Chem, Bmc, Sweden -- [Aksoy, N. H.] Aksaray Univ Sc Hlth, Aksaray, Turkey

Subjects
Enzyme Activity, Identification, Alpha Class GST, Marmoset
Abstract

22nd IUBMB Congress/37th FEBS Congress -- SEP 04-09, 2012 -- Seville, SPAIN, WOS: 000308128602632, IUBMB, FEBS

Published
2012

23. Yeast glyoxalase I is a monomeric enzyme with two active sites

Author

Frickel, EM, Jemth, P, Widersten, M, Mannervik, B, Frickel, EM, Jemth, P, Widersten, M, and Mannervik, B

Abstract

The tertiary structure of the monomeric yeast glyoxalase I has been modeled based on the crystal structure of the dimeric human glyoxalase I and a sequence alignment of the two enzymes, The model suggests that yeast glyoxalase I has two active sites conta, Addresses: Mannervik B, Uppsala Univ, Ctr Biomed, Dept Biochem, Box 576, SE-75123 Uppsala, Sweden. Uppsala Univ, Ctr Biomed, Dept Biochem, SE-75123 Uppsala, Sweden.

Published
2001

24. Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones

Author

Johansson, AS, Mannervik, B, Johansson, AS, and Mannervik, B

Abstract

The cDNA of a novel human glutathione transferase (GST) of the Alpha class was cloned, and the corresponding protein, denoted GST A3-3, was heterologously expressed and characterized. GST A3-3 was found to efficiently catalyze obligatory double-bond isome, Addresses: Mannervik B, Uppsala Univ, Dept Biochem, Biomed Ctr, Box 576, SE-75123 Uppsala, Sweden. Uppsala Univ, Dept Biochem, Biomed Ctr, SE-75123 Uppsala, Sweden.

Published
2001

25. Ser11 plays several roles in the catalytic mechanism of rat glutathione transferase T2-2

Author

Jemth, P, Mannervik, B, Jemth, P, and Mannervik, B

Abstract

Ser11 in rat glutathione transferase T2-2 promotes several steps in the catalyzed reaction pathway of the enzyme. First, the residue lowers the pK(a) value of the enzyme-bound glutathione thiol by 2.2 pH units, from 7.9 to 5.7. Secondly, the presence of S, Addresses: Mannervik B, Uppsala Univ, Dept Biochem, Biomed Ctr, Box 576, SE-75123 Uppsala, Sweden. Uppsala Univ, Dept Biochem, Biomed Ctr, SE-75123 Uppsala, Sweden.

Published
2001

26. Evolutionary design of glutathione-linked proteins in vivo and in vitro based on sampling of modules from pre-existing structures

Author

Mannervik, B, Bolton-Grob, R, Cameron, AD, Etahadieh, M, Gustafsson, A, Hansson, LO, Hubatsch, I, Jemth, P, Johansson, AS, Jones, TA, Larsson, AK, Nilsson, LO, Olin, B, Pettersson, PL, Ridderstrom, M, Stenberg, G, Widersten, M, Wisen, S, Mannervik, B, Bolton-Grob, R, Cameron, AD, Etahadieh, M, Gustafsson, A, Hansson, LO, Hubatsch, I, Jemth, P, Johansson, AS, Jones, TA, Larsson, AK, Nilsson, LO, Olin, B, Pettersson, PL, Ridderstrom, M, Stenberg, G, Widersten, M, and Wisen, S

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, Addresses: Mannervik B, Uppsala Univ, Dept Biochem, Ctr Biomed, Box 576, SE-75123 Uppsala, Sweden. Uppsala Univ, Dept Biochem, Ctr Biomed, SE-75123 Uppsala, Sweden. Uppsala Univ, Dept Mol Biol, SE-75123 Uppsala, Sweden.

Published
2001

27. The dimeric state of glutathione transferases; role of a key residue at the subunit interface in human GSTP1-1

Author

Stenberg, G, Abdallah, AM, Mannervik, B, Stenberg, G, Abdallah, AM, and Mannervik, B

Abstract

The dimer interface has been modified in human GSTP1-1 by site-directed mutagenesis. Five single-point mutants were generated by the exchange of Tyr50, the key residue in the lock-and-key motif, for Ala, Arg, Phe, Leu and Thr. Both structural stabilities, Addresses: Stenberg G, Uppsala Univ, Biomed Ctr, Dept Biochem, Box 576, SE-75123 Uppsala, Sweden. Uppsala Univ, Biomed Ctr, Dept Biochem, SE-75123 Uppsala, Sweden.

Published
2001

28. Characterization of a peptide antibody toward hGSTA4-4

Author

Gardner, JL, Bammler, TK, Mannervik, B, Gallagher, EP, Gardner, JL, Bammler, TK, Mannervik, B, and Gallagher, EP

Abstract

A polyclonal antibody was developed that can discriminate human alpha class glutathionetransferase 4-4 (hGSTA4-4). This was accomplished by first determining candidate peptide sequences of the hGSTA4 subunit, which exhibited low homology to other human GS, Addresses: Gallagher EP, Univ Florida, Dept Physiol Sci, Bldg 471, Mowry Rd, Gainesville, FL 32611 USA. Univ Florida, Dept Physiol Sci, Gainesville, FL 32611 USA. Univ Washington, Dept Environm Hlth, Seattle, WA 98195 USA. Uppsala Univ, Dept Biochem, Upps

Published
2001

29. Improved heterologous expression of human glutathione transferase A4-4 by random silent mutagenesis of codons in the 5 ' region

Author

Nilsson, LO, Mannervik, B, Nilsson, LO, and Mannervik, B

Abstract

Glutathione transferase A4-4 (GST A4-4) is involved in the detoxication of lipid peroxidation products such as alkenals. The human enzyme has been heterologously expressed in Escherichia coli, but for more extensive characterization of the enzyme the expr, Addresses: Mannervik B, Univ Uppsala, Ctr Biomed, Dept Biochem, Box 576, SE-75123 Uppsala, Sweden. Univ Uppsala, Ctr Biomed, Dept Biochem, SE-75123 Uppsala, Sweden.

Published
2001

30. Human glutathione transferase Al-1 demonstrates both half-of-the-sites and all-of-the-sites reactivity

Author

Lien, S, Gustafsson, A, Andersson, AK, Mannervik, B, Lien, S, Gustafsson, A, Andersson, AK, and Mannervik, B

Abstract

A study of the kinetics of a heterodimeric variant of glutathione transferase (GST) A1-1 has led to the conclusion that, although the wild-type enzyme displays all-of-the-sites reactivity in nucleophilic aromatic substitution reactions, it demonstrates ha, Addresses: Mannervik B, Uppsala Univ, Dept Biochem, Biomed Ctr, Box 576, SE-75123 Uppsala, Sweden. Uppsala Univ, Dept Biochem, Biomed Ctr, SE-75123 Uppsala, Sweden.

Published
2001

31. Structural basis for 4-hydroxyalkenal activity in human glutathione transferase A4-4

Author

Nilsson, LO, Gustafsson, A, Hubatsch, I, Mannervik, B, Nilsson, LO, Gustafsson, A, Hubatsch, I, and Mannervik, B

Abstract

The Alpha class glutathione transferase A4-4 (GST A4-4) detoxifies products of lipid peroxidation, e.g.4-hydroxynonenal, by a Michael-addition to glutathione. Another Alpha class enzyme, GST A1-1, is not as efficient although the structures of the enzymes, Addresses: Mamervik B, Uppsala Univ, Dept Biochem, Ctr Biomed, Box 576, SE-75123 Uppsala, Sweden. Uppsala Univ, Dept Biochem, Ctr Biomed, SE-75123 Uppsala, Sweden.

Published
2001

32. Proposed reductive metabolism of artemisinin by glutathione transferases in vitro

Author

Mukanganyama, S, Naik, YS, Widersten, M, Mannervik, B, Hasler, JA, Mukanganyama, S, Naik, YS, Widersten, M, Mannervik, B, and Hasler, JA

Abstract

Artemisinin is a sesquiterpene lactone containing an endoperoxide bridge. It is a promising new antimalarial and is particularly useful against the drug resistant strains of Plasmodium falciparum. It has unique antimalarial properties since it acts throug, Addresses: Hasler JA, Univ Zimbabwe, Dept Biochem, Box MP 167, Harare, Zimbabwe. Univ Zimbabwe, Dept Biochem, Harare, Zimbabwe. Univ Uppsala, Ctr Biomed, Dept Biochem, S-75123 Uppsala, Sweden.

Published
2001

33. Role of conserved local motifs in folding and stability of hGSTP1-1

Author

Dragani, B, Stenberg, G, Cocco, R, Mannervik, B, Aceto, A, Dragani, B, Stenberg, G, Cocco, R, Mannervik, B, and Aceto, A

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, Addresses: Aceto A, Univ G DAnnunzio, Dipartimento Sci Biomed, Via Vestini 31, I-66100 Chieti, Italy. Univ G DAnnunzio, Dipartimento Sci Biomed, I-66100 Chieti, Italy. Uppsala Univ, Biomed Ctr, Dept Biochem, SE-75123 Uppsala, Sweden.

Published
2001

34. 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

Author

Cocco, R, Stenberg, G, Dragani, B, Principe, DR, Paludi, D, Mannervik, B, Aceto, A, Cocco, R, Stenberg, G, Dragani, B, Principe, DR, Paludi, D, Mannervik, B, and Aceto, A

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, Addresses: Aceto A, Univ G DAnnunzio, Dipartimento Sci Biochim, Via Vestini 31, I-66100 Chieti, Italy. Univ G DAnnunzio, Dipartimento Sci Biochim, I-66100 Chieti, Italy. Univ G DAnnunzio, Dipartimento Sci Farmaco, I-66100 Chieti, Italy. Uppsala Univ, Dept

Published
2001

35. Disorder-to-order transition of the active site of human class Pi glutathione transferase, GST P1-1

Author

Hitchens, TK, Mannervik, B, Rule, GS, Hitchens, TK, Mannervik, B, and Rule, GS

Abstract

Glutathione transferases comprise a large family of cellular detoxification enzymes that function by catalyzing the conjugation of glutathione (GSH) to electron-deficient centers on carcinogens and other toxins. NMR methods have been used to characterize, Addresses: Rule GS, Carnegie Mellon Univ, Dept Biol Sci, 4400 5th Ave, Pittsburgh, PA 15213 USA. Carnegie Mellon Univ, Dept Biol Sci, Pittsburgh, PA 15213 USA. Univ Uppsala, Biomed Ctr, Dept Biochem, SE-75123 Uppsala, Sweden.

Published
2001

36. The isomerization of Delta(5)-androstene-3,17-dione catalyzed by human glutathione transferase A1-1

Author

Pettersson, PL, Mannervik, B, Pettersson, PL, and Mannervik, B

Abstract

Human glutathione transferase A1-1 can catalyze the isomerization of Delta (5)-androstene-3,17-dione to its isomer in the absence of glutathione. The presence of glutathione, however, significantly increases the rate of product formation. Substitution of, Addresses: Mannervik B, Uppsala Univ, Dept Biochem, Biomed Ctr, POB 576, SE-75123 Uppsala, Sweden. Uppsala Univ, Dept Biochem, Biomed Ctr, SE-75123 Uppsala, Sweden.

Published
2001

37. A conserved 'hydrophobic staple motif' plays a crucial role in the refolding of human glutathione transferase Pl-l

Author

Stenberg, G, Dragani, B, Cocco, R, Principe, DR, Mannervik, B, Aceto, A, Stenberg, G, Dragani, B, Cocco, R, Principe, DR, Mannervik, B, and Aceto, A

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, Addresses: Aceto A, Univ G DAnnunzio, Dipartimento Sci Biomed, Via Vestini 31, I-66100 Chieti, Italy. Univ G DAnnunzio, Dipartimento Sci Biomed, I-66100 Chieti, Italy. Univ Uppsala, Ctr Biomed, Dept Biochem, S-75123 Uppsala, Sweden.

Published
2001

38. A highly acidic tyrosine 9 and a normally titrating tyrosine 212 contribute to the catalytic mechanism of human glutathione transferase A4-4

Author

Hubatsch, I, Mannervik, B, Hubatsch, I, and Mannervik, B

Abstract

Human glutathione transferase A4-4 is an enzyme catalyzing the detoxication of intracellularly produced electrophiles such as 4-hydroxynonenal and other alkenal products of lipid peroxidation. Two tyrosines in the active site of the enzyme have been studi, Addresses: Hubatsch I, Uppsala Univ, Biomed Ctr, Dept Biochem, Box 576, SE-75123 Uppsala, Sweden. Uppsala Univ, Biomed Ctr, Dept Biochem, SE-75123 Uppsala, Sweden.

Published
2001

42. Examination of the transcription factor NtcA-binding motif by in vitro selection of DNA sequences from a random library

Author

Jiang, FY, Wisen, S, Widersten, M, Bergman, B, Mannervik, B, Jiang, FY, Wisen, S, Widersten, M, Bergman, B, and Mannervik, B

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, Addresses: Mannervik B, Univ Uppsala, Biomed Ctr, Dept Biochem, Box 576, S-75123 Uppsala, Sweden. Univ Uppsala, Biomed Ctr, Dept Biochem, S-75123 Uppsala, Sweden. Univ Stockholm, Dept Bot, S-10691 Stockholm, Sweden.

Published
2000
Full Text
View/download PDF

43. Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation

Author

Nilsson, LO, Gustafsson, A, Mannervik, B, Nilsson, LO, Gustafsson, A, and Mannervik, B

Abstract

The evolution of proteins for novel functions involves point mutations and recombinations of domains or structural segments. Mimicking this process by rational design in vitro is still a major challenge. The present report demonstrates that the active sit, Addresses: Mannervik B, Univ Uppsala, Biomed Ctr, Dept Biochem, Box 576, SE-75123 Uppsala, Sweden. Univ Uppsala, Biomed Ctr, Dept Biochem, SE-75123 Uppsala, Sweden.

Published
2000

45. Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2 - Evidence against proposed sulfatase activity of the corresponding human enzyme

Author

Jemth, P, Mannervik, B, Jemth, P, and Mannervik, B

Abstract

Ser(11) in rat glutathione transferase T2-2 is important for stabilization of the reactive enzyme-bound glutathione thiolate in the reaction with 1-menaphthyl sulfate. The S11A mutation increased the pK(a) value for the pH dependence of the rate constant, Addresses: Mannervik B, Univ Uppsala, Ctr Biomed, Dept Biochem, Box 576, S-75123 Uppsala, Sweden. Univ Uppsala, Ctr Biomed, Dept Biochem, S-75123 Uppsala, Sweden.

Published
2000

47. Tyrosine 50 at the subunit interface of dimeric human glutathione transferase P1-1 is a structural key residue for modulating protein stability and catalytic function

Author

Stenberg, G, Abdalla, AM, Mannervik, B, Stenberg, G, Abdalla, AM, and Mannervik, B

Abstract

The dimer interface in human GSTP1-1 has been altered by site-directed mutagenesis of Tyr50. It is shown that the effects of some mutations of this single amino acid residue are as detrimental for enzyme function as mutations of Tyr8 in the active site. T, Addresses: Stenberg G, Uppsala Univ, Biomed Ctr, Dept Biochem, Box 576, SE-75123 Uppsala, Sweden. Uppsala Univ, Biomed Ctr, Dept Biochem, SE-75123 Uppsala, Sweden.

Published
2000

48. A conserved 'hydrophobic staple motif' plays a crucial role in the refolding of human glutathione transferase P1-1

Author

Stenberg, G, Dragani, B, Cocco, R, Mannervik, B, Aceto, A, Stenberg, G, Dragani, B, Cocco, R, Mannervik, B, and Aceto, A

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, Addresses: Aceto A, Univ Chieti, Dipartimento Sci Biomed, Via Vestini 31, I-66100 Chieti, Italy. Univ Chieti, Dipartimento Sci Biomed, I-66100 Chieti, Italy. Univ Uppsala, Ctr Biomed, Dept Biochem, S-75123 Uppsala, Sweden.

Published
2000

49. The active-site residue Tyr-175 in human glyoxalase II contributes to binding of glutathione derivatives

Author

Ridderstrom, M, Jemth, P, Cameron, AD, Mannervik, B, Ridderstrom, M, Jemth, P, Cameron, AD, and Mannervik, B

Abstract

Tyrosine-175 located in the active site of human glyoxalase II was replaced by phenylalanine in order to study the contribution of this residue to catalysis. The mutation had a marginal effect on the k(cat) value determined using S-D-lactoylglutathione as, Addresses: Mannervik B, Univ Uppsala, Ctr Biomed, Dept Biochem, Box 576, S-75123 Uppsala, Sweden. Univ Uppsala, Ctr Biomed, Dept Biochem, S-75123 Uppsala, Sweden. Uppsala Univ, Biomed Ctr, Dept Mol Biol, S-75124 Uppsala, Sweden.

Published
2000

Catalog

Books, media, physical & digital resources
See catalog results