SwePub
Sök i SwePub databas

  Utökad sökning

Träfflista för sökning "WFRF:(Grubb Anders) "

Sökning: WFRF:(Grubb Anders)

  • Resultat 21-30 av 257
Sortera/gruppera träfflistan
   
NumreringReferensOmslagsbildHitta
21.
  • Grubb, R, et al. (författare)
  • Assignment of allotypes G1m(a+) and G1m(a-) at the genomic level by polymerase chain reaction analysis
  • 1990
  • Ingår i: Experimental and Clinical Immunogenetics. - 0254-9670. ; 7:4, s. 205-212
  • Tidskriftsartikel (refereegranskat)abstract
    • A method of assignment of the human immunoglobulin allotypes G1m(a+) and G1m(a-) without the use of serological reagents is described. It is based upon oligonucleotide-directed enzymatic amplification of genomic segments encoding CH3 of gamma chains, followed by dot-blot hybridization of radioactively labelled oligonucleotides to the amplified DNA. The method was used to classify the immunoglobulin allotypes of 11 persons, six G1m(a+) and five G1m(a-), and the resultant classification agreed completely with that of classical serological typing.
  •  
22.
  • Hall, Anders, et al. (författare)
  • Cystatin C based peptidyl diazomethanes as cysteine proteinase inhibitors: Influence of the peptidyl chain length
  • 1992
  • Ingår i: Journal of Enzyme Inhibition and Medicinal Chemistry. - : Informa UK Limited. - 1475-6374. ; 6:2, s. 113-123
  • Tidskriftsartikel (refereegranskat)abstract
    • The peptidyl diazomethanes Cbz-Gly-CHN2, Boc-Val-Gly-CHN2, H-Leu-Val-Gly-CHN2, Cbz-Leu-Val-Gly-CHN2 and Cbz-Arg-Leu-Val-Gly-CHN2, with peptidyl portions modelled after the proposed cysteine proteinase interacting N-terminal segment of human cystatin C, were synthesized. Their efficiency as cysteine proteinase inhibitors was tested against papain, human cathepsin B and bovine cathepsin B. All, except Cbz-Gly-CHN2, were found to be irreversible inhibitors of the tested enzymes. Each addition of an amino acid residue to their peptidyl portions resulted in an increased inhibition rate of all three enzymes. These data suggest that the arginyl residue of the tetrapeptidyl diazomethane, and also the corresponding arginyl residue in native cystatin C, interact with a S4 substrate pocket subsite of both papain and cathepsin B. The most efficient inhibitor, Cbz-Arg-Leu-Val-Gly-CHN2, inhibited papain and cathepsin B with rate constants of the same order of magnitude as those for L-3-carboxy-trans-2.3-epoxypropionyl-leucylamido-(4-guanidino)butane (E-64). The high water-solubility of Cbz-Arg-Leu-Val-Gly-CHN2 allowing it to be dissolved to molar concentrations without use of non-physiological additives, makes it suitable for in vitro and in vivo cysteine proteinase inhibition studies.
  •  
23.
  • Hall, Anders, et al. (författare)
  • Importance of the evolutionarily conserved glycine residue in the N-terminal region of cystatin C (Gly-11) for cysteine endopeptidase inhibition
  • 1993
  • Ingår i: Biochemical Journal. - 0264-6021. ; 291:1, s. 123-129
  • Tidskriftsartikel (refereegranskat)abstract
    • Human cystatin C variants in which the evolutionarily conserved Gly-11 residue has been replaced by residues with positively charged (Arg), negatively charged (Glu), bulky hydrophobic (Trp), or small (Ser or Ala) side-chains have been produced by site-directed mutagenesis and expression in Escherichia coli. The five variants were isolated and structurally verified. Their inhibitory properties were compared with those of wild-type recombinant cystatin C by determination of the equilibrium constants for dissociation (Ki) of their complexes with the cysteine endopeptidases papain and human cathepsin B and with the cysteine exopeptidase dipeptidyl peptidase I. The Ser-11 and Ala-11 cystatin C variants displayed Ki values for the two endopeptidases that were approx. 20-fold higher than those of wild-type cystatin C, while the corresponding values for the Trp-11. Arg-11 and Glu-11 variants were increased by a factor of about 2000. In contrast, the Ki values for the interactions of all five variants with the exopeptidase differed from that of wild-type cystatin C by a factor of less than 10. Wild-type cystatin C and the Ser-11, Ala-11 and Glu-11 variants were incubated with neutrophil elastase, which in all cases resulted in the rapid hydrolysis of a single peptide bond, between amino acid residues 10 and 11. The Ki values for the interactions with papain of these three N-terminal-decapeptide-lacking cystatin C variants were 20-50 nM, just one order of magnitude higher than the value for N-terminally truncated wild-type cystatin C, which in turn was similar to the corresponding values for the full-length Glu-11, Arg-11 and Trp-11 variants. These data indicate that the crucial feature of the conserved Gly residue in position 11 of wild-type cystatin C is that this residue, devoid of a side-chain, will allow the N-terminal segment of cystatin C to adopt a conformation suitable for interaction with the substrate-binding pockets of cysteine endopeptidases, resulting in high-affinity binding and efficient inhibition. The functional properties of the remaining part of the proteinase contact area, which is built from more C-terminal inhibitor segments, are not significantly affected even when amino acids with bulky or charged side-chains replace the Gly-11 residue of the N-terminal segment.
  •  
24.
  • Hall, Anders, et al. (författare)
  • Structural basis for different inhibitory specificities of human cystatins C and D
  • 1998
  • Ingår i: Biochemistry. - 0006-2960. ; 37:12, s. 4071-4079
  • Tidskriftsartikel (refereegranskat)abstract
    • Human cystatins C and D share almost identical primary structures of two out of the three segments proposed to be of importance for enzyme interactions but have markedly different profiles for inhibition of the target cysteine peptidases, cathepsins B, H, L, and S. To investigate if the N-terminal binding regions of the inhibitors are responsible for the different inhibition profiles, and thereby confer biological selectivity, two hybrid cystatins were produced in Escherichia coli expression systems. In one hybrid, the N-terminal segment of cystatin C was placed on the framework of cystatin D, and the second was engineered with the N-terminal segment of cystatin D on the cystatin C scaffold. Truncated cystatin C and D variants, devoid of their N-terminal segments, were obtained by incubation with glycyl endopeptidase and isolated, in a second approach to assess the importance of the N-terminal binding regions for cystatin function and specificity. The affinities of the four cystatin variants for cathepsins B, H, L, and S were measured. By comparison with corresponding results for wild-type cystatins C and D, it was concluded (1) that both the N-terminal and framework part of the molecules significantly contribute to the observed differences in inhibitory activities of cystatins C and D and (2) that the N-terminal segment of cystatin C increases the inhibitory activity of cystatin D against cathepsin S and cathepsin L but results in decreased activity against cathepsin H. These differences in specificity were explained by the residues interacting with the S2 subsite of peptidases (Val- and Ala-10 in cystatin C and D, respectively). Also, removal of the N-terminal segment results in total loss of enzyme affinity for cystatin D but not for cystatin C. Therefore, structural differences in the framework parts, as well as in the N-terminal segments, are critical for both inhibitory specificity and potency. Homology modeling was used to identify residues likely responsible for the generally reduced inhibitory potency of cystatin D.
  •  
25.
  • Hall, Anders, et al. (författare)
  • Structural basis for the biological specificity of cystatin C. Identification of leucine 9 in the N-terminal binding region as a selectivity-conferring residue in the inhibition of mammalian cysteine peptidases
  • 1995
  • Ingår i: Journal of Biological Chemistry. - 1083-351X. ; 270:10, s. 5115-5121
  • Tidskriftsartikel (refereegranskat)abstract
    • The structural basis for the biological specificity of human cystatin C has been investigated. Cystatin C and other inhibitors belonging to family 2 of the cystatin superfamily interact reversibly with target peptidases, seemingly by independent affinity contributions from a wedge-shaped binding region built from two loop-forming inhibitor segments and a binding region corresponding to the N-terminal segment of the inhibitor. Human cystatin C variants with Gly substitutions for residues Arg-8, Leu-9, and/or Val-10 of the N-terminal binding region, and/or the evolutionarily conserved Trp-106 in the wedge-shaped binding region, were produced by site-directed mutagenesis and Escherichia coli expression. A total of 10 variants were isolated, structurally verified, and compared to wild-type cystatin C with respect to inhibition of the mammalian cysteine peptidases, cathepsins B, H, L, and S. Varying contributions from the N-terminal binding region and the wedge-shaped binding region to cystatin C affinity for the four target peptidases were observed. Interactions from the side chains of residues in the N-terminal binding region and Trp-106 are jointly responsible for the major part of cystatin C affinity for cathepsin L and are also of considerable importance for cathepsin B and H affinity. In contrast, for cathepsin S inhibition these interactions are of lesser significance, as reflected by a Ki value of 10(-8) M for the cystatin C variant devoid of Arg-8, Leu-9, Val-10, and Trp-106 side chains. The side chain of Val-10 is responsible for most of the affinity contribution from the N-terminal binding region, for all four enzymes. The contribution of the Arg-8 side chain is minor, but significant for cystatin C interaction with cathepsin B. The Leu-9 side chain confers selectivity to the inhibition of the target peptidases; it contributes to cathepsin B and L affinity by factors of 200 and 50, respectively, to cathepsin S binding by a factor of 5 only, and results in a 10-fold decreased affinity between cystatin C and cathepsin H.
  •  
26.
  • Hansson, Lars-Olof, et al. (författare)
  • Performance evaluation of a turbidimetric cystatin C assay on different high-throughput platforms
  • 2010
  • Ingår i: Scandinavian Journal of Clinical & Laboratory Investigation. - : Informa UK Limited. - 1502-7686 .- 0036-5513. ; 70:5, s. 347-353
  • Tidskriftsartikel (refereegranskat)abstract
    • Objective. The goal with this study was to evaluate the analytical performance of a new cystatin C immunoassay (Tina-quant (R) a Cystatin C, Roche Diagnostics GmbH). The evaluation was carried out at four centers according to a standardized protocol. Material and methods. The Tina-quant (R) a Cystatin C is a latex particle-enhanced immunoturbidimetric assay. Roche cobas (R) 6000, MODULAR ANALYTICS SWA and COBAS INTEGRA (R) instruments were included in the study. Method comparison studies were carried out against two turbidimetric methods (Dako Cystatin C, Gentian Cystatin C), and one nephelometric method (Siemens N-Latex Cystatin C). Results. Linearity was proven throughout the measuring range from 0.4 to 8 mg/L. Within-run CVs ranged from 0.7-2.8%, and total CVs from 1.4-4.7 % (concentration range 0.6-3.9 mg/L). Comparable results were obtained with paired serum and Li-heparinate plasma samples. Good agreement was achieved in the comparisons between the Tina-quant (R) a Cystatin C assay and the other commercially available cystatin C assays, two different turbidimetric methods (slope range 0.88-1.04, intercept < 0.17 mg/L, r >= 0.993) and one nephelometric assay (slope range 0.90-1.05, intercept < 0.21 mg/L, r >= 0.986). Conclusions. The Tina-quant (R) a Cystatin C assay was shown to be precise and accurate with proven linearity over the measuring range. Good comparability was obtained with other commercially available assays for the determination of cystatin C. The Tina-quant (R) a Cystatin C assay is very well suited for clinical use on routine clinical chemistry analysers to detect renal dysfunction with a 24 h availability.
  •  
27.
  •  
28.
  • Johansson, Anders, et al. (författare)
  • Cisplatin pharmacokinetics and pharmacodynamics in patients with squamous-cell carcinoma of the head/neck or esophagus
  • 1996
  • Ingår i: Cancer Chemotherapy and Pharmacology. - : Springer Science and Business Media LLC. - 0344-5704 .- 1432-0843. ; 39, s. 25-33
  • Tidskriftsartikel (refereegranskat)abstract
    • The pharmacokinetics of total platinum (Pt) in plasma and cisplatin (CDDP)-DNA adducts in different cell types were described in ten patients with squamous-cell carcinoma of the head/neck or esophagus after their first cycle of chemotherapy containing a CDDP dose of 100 mg/m2. Nephrotoxicity was studied in terms of urinary excretion of marker proteins (protein HC, IgG, and albumin). Pharmacodynamic relationships between pharmacokinetic parameters and toxicity were investigated. A population-based model with limited sampling was found feasible for producing pharmacokinetic information, in accordance with literature data. The kinetics of two normal cell types with different turnover (lymphocytes and buccal cells) appeared to have different kinetic profiles of CDDP-DNA adducts. Analysis of urinary excretion of marker proteins (protein HC, albumin, and IgG) showed that the nephrotoxicity was displayed first as tubular damage and later as impaired glomerular barrier function. There were indications that tubular nephrotoxicity may be predicted by pharmacokinetic parameters of plasma Pt. We found older patients to have a lower Pt clearance and more extensive early tubular damage. There was no correlation between CDDP-DNA adducts in normal cells and nephrotoxicity. Larger studies are warranted to define the pharmacokinetic window of CDDP. Limited sampling for analysis of CDDP pharmacokinetics may then be a possible avenue for individualizing the dose and, thus, improving the clinical use of the drug.
  •  
29.
  • Jonsson, M, et al. (författare)
  • Plasmaproteiner, inflammation och amyloidos
  • 2018. - 10
  • Ingår i: Laurells klinisk kemi i praktisk medicin.. - Lund : Studentlitteratur AB. - 9789144119748 ; , s. 87-130
  • Bokkapitel (refereegranskat)
  •  
30.
  •  
Skapa referenser, mejla, bekava och länka
  • Resultat 21-30 av 257
Typ av publikation
tidskriftsartikel (238)
konferensbidrag (8)
forskningsöversikt (7)
bokkapitel (4)
Typ av innehåll
refereegranskat (253)
övrigt vetenskapligt/konstnärligt (4)
Författare/redaktör
Grubb, Anders (251)
Abrahamson, Magnus (65)
Björk, Jonas (41)
Lindström, Veronica (39)
Nyman, Ulf (37)
Larsson, Anders (19)
visa fler...
Christensson, Anders (19)
Sterner, Gunnar (15)
Hansson, Magnus (14)
Åkesson, Anna (13)
Pottel, Hans (13)
Littmann, Karin (12)
Delanaye, Pierre (12)
Bökenkamp, Arend (11)
Olafsson, I (10)
Dubourg, Laurence (10)
Jensson, O (9)
Håkansson, Katarina (9)
Strevens, Helena (9)
Kasprzykowski, F (9)
Schaeffner, Elke (9)
Magnusson, Martin (8)
Olafsson, Isleifur (8)
Wide-Swensson, Dag (8)
Ebert, Natalie (8)
Mariat, Christophe (8)
Melsom, Toralf (8)
Åsling-Monemi, Kajsa (8)
Lamb, Edmund J. (7)
Rule, Andrew D. (7)
Berg, Ulla (7)
Wang, Xin (6)
Lerner, Ulf H (6)
Thysell, Hans (6)
Bäck, Sten Erik (6)
Hansson, Lars-Olof (6)
Kasprzykowski, Franc ... (6)
Jovinge, Stefan (5)
Hall, Anders (5)
Rippe, Bengt (5)
Bakoush, Omran (5)
Balbin, Milagros (5)
Jaskolski, M (5)
Rodziewicz-Motowidlo ... (5)
Kozak, Maciej (5)
Flodin, Mats (5)
Levey, Andrew S. (5)
Nordin, Gunnar (5)
Gaillard, Francois (5)
Cavalier, Etienne (5)
visa färre...
Lärosäte
Lunds universitet (236)
Uppsala universitet (23)
Karolinska Institutet (9)
Göteborgs universitet (8)
Umeå universitet (6)
Örebro universitet (6)
visa fler...
Linköpings universitet (4)
Högskolan i Halmstad (1)
Malmö universitet (1)
Högskolan Dalarna (1)
visa färre...
Språk
Engelska (251)
Svenska (6)
Forskningsämne (UKÄ/SCB)
Medicin och hälsovetenskap (229)
Naturvetenskap (25)
Teknik (1)

År

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Stäng

Kopiera och spara länken för att återkomma till aktuell vy