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  • 1
    Online Resource
    Online Resource
    ‘FAS’t inhibition of malaria
    Portland Press Ltd. ; 2004
    In:  Biochemical Journal Vol. 384, No. 3 ( 2004-12-15), p. 655-655
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 384, No. 3 ( 2004-12-15), p. 655-655
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/BJ3840655
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 2004
    detail.hit.zdb_id: 1473095-9
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  • 2
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    Effect of glycosylation on the structure of Erythrina corallodendron lectin
    Wiley ; 2004
    In:  Proteins: Structure, Function, and Bioinformatics Vol. 56, No. 4 ( 2004-05-14), p. 821-827
    Details
    In: Proteins: Structure, Function, and Bioinformatics, Wiley, Vol. 56, No. 4 ( 2004-05-14), p. 821-827
    Type of Medium: Online Resource
    ISSN: 0887-3585
    URL: Article
    DOI: 10.1002/prot.20168
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 2004
    detail.hit.zdb_id: 1475032-6
    SSG: 12
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  • 3
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    Napin from Brassica juncea: Thermodynamic and structural analysis of stability
    Elsevier BV ; 2007
    In:  Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics Vol. 1774, No. 7 ( 2007-7), p. 907-919
    Details
    In: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Elsevier BV, Vol. 1774, No. 7 ( 2007-7), p. 907-919
    Type of Medium: Online Resource
    ISSN: 1570-9639
    URL: Article
    DOI: 10.1016/j.bbapap.2007.04.008
    RVK:
    WA 15000
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2007
    detail.hit.zdb_id: 2209540-8
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  • 4
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    A model for the transcriptional regulation of the CYP2B1/B2 gene in rat liver.
    Proceedings of the National Academy of Sciences ; 1995
    In:  Proceedings of the National Academy of Sciences Vol. 92, No. 21 ( 1995-10-10), p. 9628-9632
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 92, No. 21 ( 1995-10-10), p. 9628-9632
    Abstract: The phenobarbitone-responsive minimal promoter has been shown to lie between nt -179 and nt + 1 in the 5' (upstream) region of the CYP2B1/B2 gene in rat liver, on the basis of the drug responsiveness of the sequence linked to human growth hormone gene as reporter and targeted to liver as an asialoglycoprotein-DNA complex in vivo. Competition analyses of the nuclear protein-DNA complexes formed in gel shift assays with the positive (nt -69 to -98) and negative (nt -126 to -160) cis elements (PE and NE, respectively) identified within this region earlier indicate that the same protein may be binding to both the elements. The protein species purified on PE and NE affinity columns appear to be identical based on SDS/PAGE analysis, where it migrates as a protein of 26-28 kDa. Traces of a high molecular weight protein (94-100 kDa) are also seen in the preparation obtained after one round of affinity chromatography. The purified protein stimulates transcription of a minigene construct containing the 179 nt on the 5' side of the CYP2B1/B2 gene linked to the I exon in a cell-free system from liver nuclei. The purified protein can give rise to all the three complexes (I, II, and III) with the PE, just as the crude nuclear extract, under appropriate conditions. Manipulations in vitro indicate that the NE has a significantly higher affinity for the dephosphorylated form than for the phosphorylated form of the protein. The PE binds both forms. Phenobarbitone treatment of the animal leads to a significant increase in the phosphorylation of the 26- to 28-kDa and 94-kDa proteins in nuclear labeling experiments followed by isolation on a PE affinity column. We propose that the protein binding predominantly to the NE in the dephosphorylated state characterizes the basal level of transcription of the CYP2B1/B2 gene. Phenobarbitone treatment leads to phosphorylation of the protein, shifting the equilibrium toward binding to the PE. This can promote interaction with an upstream enhancer through other proteins such as the 94-kDa protein and leads to a significant activation of transcription.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.92.21.9628
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1995
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
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  • 5
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    Primary structure of a Thomsen-Friedenreich-antigen-specific lectin, jacalin [ Artocarpus integrifolia (jack fruit) agglutinin]. Evidence for the presence of an internal repeat
    Portland Press Ltd. ; 1992
    In:  Biochemical Journal Vol. 284, No. 1 ( 1992-05-15), p. 95-101
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 284, No. 1 ( 1992-05-15), p. 95-101
    Abstract: Jacalin [Artocarpus integrifolia (jack fruit) agglutinin] is made up of two types of chains, heavy and light, with M(r) values of 16,200 +/- 1200 and 2090 +/- 300 respectively (on the basis of gel-permeation chromatography under denaturing conditions). Its complete amino acid sequence was determined by manual degradation using a 4-dimethylaminoazobenzene 4′-isothiocyanate double-coupling method. Peptide fragments for sequence analysis were obtained by chemical cleavages of the heavy chain with CNBr, hydroxylamine hydrochloride and iodosobenzoic acid and enzymic cleavage with Staphylococcus aureus proteinase. The peptides were purified by a combination gel-permeation and reverse-phase chromatography. The light chains, being only 20 residues long, could be sequenced without fragmentation. Amino acid analyses and carboxypeptidase-Y-digestion C-terminal analyses of the subunits provided supportive evidence for their sequence. Computer-assisted alignment of the jacalin heavy-chain sequence failed to show sequence similarity to that of any lectin for which the complete sequence is known. Analyses of the sequence showed the presence of an internal repeat spanning residues 7-64 and 76-130. The internal repeat was found to be statistically significant.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/bj2840095
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 1992
    detail.hit.zdb_id: 1473095-9
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  • 6
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    Induction of a spectroscopically defined transition by guanidinium hydrochloride on a recombinant calcium binding protein from Entamoeba histolytica
    Wiley ; 1998
    In:  FEBS Letters Vol. 441, No. 1 ( 1998-12-11), p. 71-76
    Details
    In: FEBS Letters, Wiley, Vol. 441, No. 1 ( 1998-12-11), p. 71-76
    Abstract: Sequence analysis and metal ion binding studies reported earlier have established that the calcium binding protein (CaBP) from the parasitic ameboid Entamoeba histolytica protein has four canonical EF hand motifs which bind calcium. Equilibrium denaturation studies on both the apo and the holo forms of this protein indicate the presence of stable transition intermediates at low denaturant concentrations as revealed by the binding of the non‐specific hydrophobic dye ANS. Fast reaction kinetics shows that the binding of the Gdn + ions at or near the Ca 2+ sites in the N‐terminal domain influences metal ion binding to the sites in the C‐terminal domain. Isothermal calorimetric titrations performed using low GdnHCl concentrations reveal the presence of two binding sites of low affinity, both being endothermic in nature. Thus the stabilization of CaBP observed at low GdnHCl concentration represents a native‐like intermediate, with the Gdn + ions mimicking Ca 2+ binding at the N‐terminal domain of this protein.
    Type of Medium: Online Resource
    ISSN: 0014-5793 , 1873-3468
    URL: Article
    DOI: 10.1016/S0014-5793(98)01513-0
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1998
    detail.hit.zdb_id: 1460391-3
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  • 7
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    Topography of the combining region of a Thomsen-Friedenreich-antigen-specific lectin jacalin ( Artocarpus integrifolia agglutinin). A thermodynamic and circular-dichroism spectroscopic study
    Portland Press Ltd. ; 1990
    In:  Biochemical Journal Vol. 265, No. 3 ( 1990-02-01), p. 831-840
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 265, No. 3 ( 1990-02-01), p. 831-840
    Abstract: Thermodynamic analysis of carbohydrate binding by Artocarpus integrifolia (jackfruit) agglutinin (jacalin) shows that, among monosaccharides, Me alpha GalNAc (methyl-alpha-N-acetylgalactosamine) is the strongest binding ligand. Despite its strong affinity for Me alpha GalNAc and Me alpha Gal, the lectin binds very poorly when Gal and GalNAc are in alpha-linkage with other sugars such as in A- and B-blood-group trisaccharides, Gal alpha 1-3Gal and Gal alpha 1-4Gal. These binding properties are explained by considering the thermodynamic parameters in conjunction with the minimum energy conformations of these sugars. It binds to Gal beta 1-3GalNAc alpha Me with 2800-fold stronger affinity over Gal beta 1-3GalNAc beta Me. It does not bind to asialo-GM1 (monosialoganglioside) oligosaccharide. Moreover, it binds to Gal beta 1-3GalNAc alpha Ser, the authentic T (Thomsen-Friedenreich)-antigen, with about 2.5-fold greater affinity as compared with Gal beta 1-3GalNAc. Asialoglycophorin A was found to be about 169,333 times stronger an inhibitor than Gal beta 1-3GalNAc. The present study thus reveals the exquisite specificity of A. integrifolia lectin for the T-antigen. Appreciable binding of disaccharides Glc beta 1-3GalNAc and GlcNAc beta 1-3Gal and the very poor binding of beta-linked disaccharides, which instead of Gal and GalNAc contain other sugars at the reducing end, underscore the important contribution made by Gal and GalNAc at the reducing end for recognition by the lectin. The ligand-structure-dependent alterations of the c.d. spectrum in the tertiary structural region of the protein allows the placement of various sugar units in the combining region of the lectin. These studies suggest that the primary subsite (subsite A) can accommodate only Gal or GalNAc or alpha-linked Gal or GalNAc, whereas the secondary subsite (subsite B) can associate either with GalNAc beta Me or Gal beta Me. Considering these factors a likely arrangement for various disaccharides in the binding site of the lectin is proposed. Its exquisite specificity for the authentic T-antigen, Gal beta 1-3GalNAc alpha Ser, together with its virtual non-binding to A- and B-blood-group antigens, Gal beta 1-3GalNAc beta Me and asialo-GM1 should make A. integrifolia lectin a valuable probe for monitoring the expression of T-antigen on cell surfaces.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/bj2650831
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 1990
    detail.hit.zdb_id: 1473095-9
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  • 8
    Online Resource
    Online Resource
    Ribosome-inactivating protein and apoptosis: abrin causes cell death via mitochondrial pathway in Jurkat cells
    Portland Press Ltd. ; 2004
    In:  Biochemical Journal Vol. 377, No. 1 ( 2004-01-01), p. 233-240
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 377, No. 1 ( 2004-01-01), p. 233-240
    Abstract: Abrin belongs to the type II family of ribosome-inactivating proteins comprising a galactose-binding B chain coupled with a toxic A chain through a single disulphide linkage. Apart from its RNA-N-glycosidase activity, another role that has been recently ascribed to abrin was the induction of apoptosis. Studies were undertaken to determine the kinetics of these two activities. In the present study, we report that the signal for apoptosis is triggered at a time point later than the inhibition of protein synthesis. This apoptotic pathway induced by abrin is caspase 3-dependent but caspase 8-independent and involves mitochondrial membrane potential damage and reactive oxygen species production. Overexpression of B-cell lymphocytic-leukaemia proto-oncogene 2 was found to block this apoptotic pathway.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/bj20030797
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 2004
    detail.hit.zdb_id: 1473095-9
    SSG: 12
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  • 9
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    Online Resource
    Thermodynamics of target peptide recognition by calmodulin and a calmodulin analogue: implications for the role of the central linker
    Wiley ; 1999
    In:  FEBS Letters Vol. 461, No. 1-2 ( 1999-11-12), p. 19-24
    Details
    In: FEBS Letters, Wiley, Vol. 461, No. 1-2 ( 1999-11-12), p. 19-24
    Abstract: The thermodynamics of interaction of two model peptides melittin and mastoparan with bovine brain calmodulin (CAM) and a smaller CAM analogue, a calcium binding protein from Entamoeba histolytica (CaBP) in 10 mM MOPS buffer (pH 7.0) was examined using isothermal titration calorimetry (ITC). These data show that CAM binds to both the peptides and the enthalpy of binding is endothermic for melittin and exothermic for mastoparan at 25°C. CaBP binds to the longer peptide melittin, but does not bind to mastoparan, the binding enthalpy being endothermic in nature. Concurrently, we also observe a larger increase in α‐helicity upon the binding of melittin to CAM when compared to CaBP. The role of hydrophobic interactions in the binding process has also been examined using 8‐anilino‐1‐naphthalene‐sulphonic acid (ANS) binding monitored by ITC. These results have been employed to rationalize the energetic consequences of the binding reaction.
    Type of Medium: Online Resource
    ISSN: 0014-5793 , 1873-3468
    URL: Article
    DOI: 10.1016/S0014-5793(99)01380-0
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1999
    detail.hit.zdb_id: 1460391-3
    SSG: 12
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  • 10
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    Crystallization of a scRIP—gelonin isolated from plant seedsGelonium multiforum
    Wiley ; 1994
    In:  Proteins: Structure, Function, and Genetics Vol. 19, No. 4 ( 1994-08), p. 340-342
    Details
    In: Proteins: Structure, Function, and Genetics, Wiley, Vol. 19, No. 4 ( 1994-08), p. 340-342
    Type of Medium: Online Resource
    ISSN: 0887-3585 , 1097-0134
    URL: Issue
    URL: Journal
    URL: Article
    DOI: 10.1002/prot.v19:4
    DOI: 10.1002/(ISSN)1097-0134
    DOI: 10.1002/prot.340190409
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1994
    detail.hit.zdb_id: 1475032-6
    SSG: 12
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