Relevant bibliographies by topics / Chlorophyll a/b binding proteins

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Chlorophyll a/b binding proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 15 February 2022

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Journal articles on the topic "Chlorophyll a/b binding proteins"

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Paulsen, Harald. "CHLOROPHYLL a/b-BINDING PROTEINS." Photochemistry and Photobiology 62, no. 3 (September 1995): 367–82. http://dx.doi.org/10.1111/j.1751-1097.1995.tb02357.x.

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Bassi, Roberto, Dorianna Sandona, and Roberta Croce. "Novel aspects of chlorophyll a/b-binding proteins." Physiologia Plantarum 100, no. 4 (August 1997): 769–79. http://dx.doi.org/10.1034/j.1399-3054.1997.1000404.x.

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Bassi, Roberto, Dorianna Sandona, and Roberta Croce. "Novel aspects of chlorophyll a/b-binding proteins." Physiologia Plantarum 100, no. 4 (August 1997): 769–79. http://dx.doi.org/10.1111/j.1399-3054.1997.tb00004.x.

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Green, Beverly R., Eran Pichersky, and Klaus Kloppstech. "Chlorophyll a/b-binding proteins: an extended family." Trends in Biochemical Sciences 16 (January 1991): 181–86. http://dx.doi.org/10.1016/0968-0004(91)90072-4.

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Krol, M., M. D. Spangfort, NPA Huner, G. Oquist, P. Gustafsson, and S. Jansson. "Chlorophyll a/b-Binding Proteins, Pigment Conversions, and Early Light-Induced Proteins in a Chlorophyll b-less Barley Mutant." Plant Physiology 107, no. 3 (March 1, 1995): 873–83. http://dx.doi.org/10.1104/pp.107.3.873.

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Van Buren, Jerome P. "Extraction of chlorophylls a and b from different binding sites on thylakoid chlorophyll-proteins." Journal of Agricultural and Food Chemistry 33, no. 2 (March 1985): 204–8. http://dx.doi.org/10.1021/jf00062a011.

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Babiychuk, Elena, Rodolphe Schantz, Nicolai Cherep, Jacques-Henry Weil, Yuri Gleba, and Sergei Kushnir. "Alterations in chlorophyll a/b binding proteins in Solanaceae cybrids." Molecular and General Genetics MGG 249, no. 6 (November 1995): 648–54. http://dx.doi.org/10.1007/bf00418034.

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H�yer-Hansen, G., R. Bassi, L. S. H�nberg, and D. J. Simpson. "Immunological characterization of chlorophyll a/b-binding proteins of barley thylakoids." Planta 173, no. 1 (January 1988): 12–21. http://dx.doi.org/10.1007/bf00394481.

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Darr, S. C., S. C. Somerville, and C. J. Arntzen. "Monoclonal antibodies to the light-harvesting chlorophyll a/b protein complex of photosystem II." Journal of Cell Biology 103, no. 3 (September 1, 1986): 733–40. http://dx.doi.org/10.1083/jcb.103.3.733.

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A collection of 17 monoclonal antibodies elicited against the light-harvesting chlorophyll a/b protein complex which serves photosystem II (LHC-II) of Pisum sativum shows six classes of binding specificity. Antibodies of two of the classes recognize a single polypeptide (the 28- or the 26- kD polypeptides), thereby suggesting that the two proteins are not derived from a common precursor. Other classes of antibodies cross-react with several polypeptides of LHC-II or with polypeptides of both LHC-II and the light-harvesting chlorophyll a/b polypeptides of photosystem I (LHC-I), indicating that there are structural similarities among the polypeptides of LHC-II and LHC-I. The evidence for protein processing by which the 26-, 25.5-, and 24.5-kD polypeptides are derived from a common precursor polypeptide is discussed. Binding studies using antibodies specific for individual LHC-II polypeptides were used to quantify the number of antigenic polypeptides in the thylakoid membrane. 27 copies of the 26-kD polypeptide and two copies of the 28-kD polypeptide were found per 400 chlorophylls. In the chlorina f2 mutant of barley, and in intermittent light-treated barley seedlings, the amount of the 26-kD polypeptide in the thylakoid membranes was greatly reduced, while the amount of 28-kD polypeptide was apparently not affected. We propose that stable insertion and assembly of the 28-kD polypeptide, unlike the 26-kD polypeptide, is not regulated by the presence of chlorophyll b.
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Allen, K. D., M. E. Duysen, and L. A. Staehelin. "Biogenesis of thylakoid membranes is controlled by light intensity in the conditional chlorophyll b-deficient CD3 mutant of wheat." Journal of Cell Biology 107, no. 3 (September 1, 1988): 907–19. http://dx.doi.org/10.1083/jcb.107.3.907.

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Biogenesis of thylakoid membranes in the conditional chlorophyll b-deficient CD3 mutant of wheat is dramatically altered by relatively small differences in the light intensity under which seedlings are grown. When the CD3 mutant is grown at 400 microE/m2 S (high light, about one-fifth full sunlight) plants are deficient in chlorophyll b (chlorophyll a/b ratio greater than 6.0) and lack or contain greatly reduced amounts of the chlorophyll a/b-binding complexes CPII/CPII (mobile or peripheral LHCII), CP29, CP24 and LHCI, as shown by mildly denaturing 'green gel' electrophoresis, by fully denaturing SDS-PAGE, and by Western blot analysis. High light CD3 chloroplasts display an unusual morphology characterized by large, sheet-like stromal thylakoids formed into parallel unstacked arrays and a limited number of small grana stacks displaced toward the edges of the arrays. Changes in the supramolecular organization of CD3 thylakoids, seen with freeze-fracture electron microscopy, include a reduction in the size of EFs particles, which correspond to photosystem II centers with variable amounts of attached LHCII, and a redistribution of EF particles from the stacked to the unstacked regions. When CD3 seedlings are grown at 150 microE/m2 S (low light) there is a substantial reversal of all of these effects. Thus, chlorophyll b and the chlorophyll a/b-binding proteins accumulate to near wild-type levels (chlorophyll a/b ratio = 3.5-4.5) and thylakoid morphology is more nearly wild type in appearance. Growth of the CD3 mutant in the presence of chloramphenicol stimulates the accumulation of chlorophyll b and its binding proteins (Duysen, M. E., T. P. Freeman, N. D. Williams, and L. L. Huckle. 1985. Plant Physiol. 78:531-536). We show that this partial rescue of the CD3 high light phenotype is accompanied by large changes in thylakoid structure. The CD3 mutant, which defines a new class of chlorophyll b-deficient phenotype, is discussed in the more general context of chlorophyll b deficiency.
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Dissertations / Theses on the topic "Chlorophyll a/b binding proteins"

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Szekeres, Ferenc. "Bioinformatics applied to chlorophyll a/b binding proteins in Avena sativa (oat)." Thesis, University of Skövde, Department of Computer Science, 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:his:diva-820.

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The chlorophyll a/b binding (CAB) genes play a very central role in all photosynthetic systems and are for Avena sativa (oat) totally unexplored. This dissertation investigates a large number of EST sequences and this investigation characterises the CAB genes in oat, with help from the evolutionary background of oat and the comparison to a reference organism and similar species.

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Schmidt, Kristin. "Pigmentbindung verschiedener Mitglieder der erweiterten Chlorophyll-a-b-Proteinfamilie und des wasserlöslichen Chlorophyll-Proteins WSCP." [S.l. : s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=968710921.

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Wang, Hui. "Immunoglobulin binding proteins in ticks." Thesis, University of Oxford, 1995. http://ora.ox.ac.uk/objects/uuid:7c09068b-82fb-4434-9e84-4663cbab7795.

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Jones, Gareth. "NMR studies of the DNA-binding domain of B-Myb." Thesis, University of Kent, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.270703.

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Sarma, Ranjana. "Investigations of nucleotide-dependent electron transfer and substrate binding in nitrogen fixation and chlorophyll biosynthesis." Thesis, Montana State University, 2009. http://etd.lib.montana.edu/etd/2009/sarma/SarmaR1209.pdf.

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The studies presented in this thesis include studies of nucleotide-dependent conformations of the electron donor protein in nitrogenase and dark-operative protochlorophyllide reductase (DPOR) characterized using small-angle x-ray scattering and x-ray diffraction methods. Nitrogen fixation and chlorophyll synthesis are involved in the reduction of high energy bonds under physiological conditions. Both make use of elegant reaction mechanisms made possible by complex enzyme systems which are evolutionarily related. Nitrogenase reduces nitrogen to ammonia and is a two-component metalloenzyme composed of Fe protein and MoFe protein. For nitrogen reduction, the Fe protein and MoFe protein associate and dissociate in a manner concomitant with hydrolysis of at least two MgATP molecules and enables the concomitant transfer of at least one electron from Fe protein to MoFe protein. During chlorophyll biosysnthesis, the rate limiting step is catalyzed by a two-component metalloenzyme called DPOR. The two components of DPOR are BchL and BchNB proteins and these share high level of sequence similarity with the Fe protein and the MoFe protein, respectively. Based on this sequence similarity and biochemical data available, it is proposed that the reaction mechanism is similar to nitrogenase mechanism in which the components of DPOR associate and dissociate in a nucleotide dependent manner, to enable intercomponent electron transfer. Fe protein and BchL present as unique examples of proteins that couple nucleotide dependent conformational change to enable electron transfer for high energy bond reduction. The present studies have been directed at studying the low resolution studies of MgATP-bound wild-type Fe protein and its comparison to the structure of the proposed mimic, i.e, L127 Delta Fe protein. The studies presented show evidence of the MgATP-bound wild-type Fe protein having a conformation very different from the L127 Delta Fe protein. The chapters also include detailed characterization of the structure of BchL in both MgADP bound and nucleotide-free states which offer detailed insights in the structure based mechanism of BchL, with primary focus on identifying key residues involved in componenet docking and in electron transfer. Together, the studies on the Fe protein and BchL have furthered our understanding of mechanism of electron transfer in these complex enzyme systems.
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Taylor, John Philip. "Sub-cellular localisation and function of calcineurin B-like proteins in plant cells." Thesis, University of East Anglia, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.268512.

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Price, Gregory A. "Immunogenicity of the Gonococcal Transferrin Binding Proteins." VCU Scholars Compass, 2005. http://scholarscompass.vcu.edu/etd_retro/76.

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The gonococcal transferrin binding proteins (Tbps) are two surface-exposed outer membrane proteins, TbpA and TbpB, which together function to remove and internalized iron from human transferrin. Iron is an essential nutrient to the gonococcus, without which it cannot survive. The Tbps have been established as virulence factors, demonstrating their importance in establishing infection. Both TbpA and TbpB are well conserved among gonococcal isolates, and have been considered potential vaccine targets. Vaccine studies with the closely related species Neisseria meningitidis, have demonstrated these proteins to be protective in murine challenge studies. Though the meningococcal Tbps have demonstrated promise, no similar gonococcal vaccine experiments have been conducted prior to the current studies. Here we demonstrate purification of recombinant TbpA and TbpB. These recombinant proteins were utilized to evaluate the human immune response to these proteins during natural infections, and their immunogenicity in murine vaccine studies. Our results demonstrate a paucity of antibodies elicited to these proteins during natural infections in serum and mucosal secretions from infected individuals. From this study we hypothesized the induction of both serum and genital antibodies to these proteins could serve to protect an individual from infection. To begin testing this hypothesis, we immunized mice both intranasally (IN) and subcutaneously (s.c.) with full-length Tbps in conjunction with the B subunit of cholera toxin (Ctb) as an adjuvant. We also performed another vaccine study using domains from both proteins in genetic fusions with Ctb and E. coli heat labile toxin IIb (LtbIIb). Both studies demonstrated that these antigens were immunogenic, as Tbp-specific antibodies were elicited in the serum and vaginal washes of female Balb/C mice. Intranasal immunization however was the only route with which we were able to elicit vaginal Tbp-specific IgA, and IgG, whereas subcutaneous immunization only elicited vaginal IgG. Furthermore, we found the full-length Tbps and the Ctb/LtbIIb chimeras were able to elicit bactericidal antibodies, which were also effective in killing heterologous gonococcal strains. This body of work comprises the first published study using the gonococcal transferrin binding proteins as vaccine antigens, and highlights their potential as vaccine antigens in the development of an efficacious gonococcal vaccine.
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Fernandez, D. S. "Signalling in Trypanosoma b. brucei mediated by GTP-binding proteins and phosphorylation." Thesis, University of Cambridge, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.598993.

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Antisera raised against the C-terminal decapeptide of Gsα, (RMHLRQYELL or RM), immunodetected polypeptides of 52, 45 and 42 kDa species consistent with identified mammalian species. The specificity of the immunoreactivity was demonstrated by competition with preincubations utilising the decapeptide RM against which the antiserum was raised. Antibodies to Gi and Gq and their respective competing peptides were also utilised. These indicated the presence of a 41 kDa polypeptide cross-reactive with anti-Gi and two polypeptides of 43 and 42 kDa cross-reactive with anti-Gq in trypanosome extracts. GTP binding proteins of T. b. brucei were additionally identified by [α32P]-GTP binding. This method elucidated polypeptides of 65, 52, 45 and 41 kDa as well as low molecular weight polypeptides (less than 30 kDa) typical in size and abundance of members of the ras superfamily. GTP-binding proteins were also labelled by a photoaffinity reaction by UV irradiation in the presence of [α32P]-GTP, identifying polypeptides of 160, 140, 65, 52 and 45 kDa in trypanosomes which co-localised with CS1-immunoreactive species. Cholera toxin catalysed ADP-ribosylations of 52 and 45 kDa polypeptides while pertussis toxin mediated the ADP-ribosylation of 41-43 kDa polypeptides; consistent with observations for mammalian species and the immoreactivity data presented. The role of tyrosine kinase signalling pathways was also studied. By stimulating conditions required for transformation of the bloodstream form to the procyclic, increases in autophosphorylating kinase activity and tyrosine phosphorylation were observed. Phosphorylations on polypeptides of 138, 87, 66, 60 and 46 kDa were found to be alkaline stable, identifying them as possible tyrosine kinases. Phosphoamino acid analysis confirmed phosphorylation of tyrosine of polypeptides of 138, 66 and 46 kDa. The autophosphorylating kinase activity of a 138 kDa polypeptide was found to be 1) stimulated by EGF; 2) shown to be alkaline resistance and; 3) to be phosphorylated on tyrosine which indicate it might be the putative EGF receptor tyrosine kinase of T. brucei while a 98 kDa polypeptide was identified by immunoblotting as a possible insulin receptor kinase.
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Joshi, Jidnyasa [Verfasser], and Claudia [Akademischer Betreuer] Büchel. "Biochemical characterization of Fucoxanthin Chlorophyll a/c binding proteins in the diatom Phaeodactylum tricornutum / Jidnyasa Joshi. Gutachter: Claudia Büchel." Frankfurt am Main : Univ.-Bibliothek Frankfurt am Main, 2012. http://d-nb.info/1044772700/34.

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Galloway, Alison. "The RNA binding proteins ZFP36L1 and ZFP36L2 are essential for B lymphocyte development." Thesis, University of Cambridge, 2014. https://www.repository.cam.ac.uk/handle/1810/283950.

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Books on the topic "Chlorophyll a/b binding proteins"

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Green, Beverly R. Chlorophyll a/b/-binding proteins: An extended family. Amsterdam: Elsevier, 1991.

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Clark, Steven Edward. Determinants for chloroplast import and processing of the light-harvesting chlorophyll a/b-binding protein precursor. 1991.

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Metabolism, Structure and Function of Plant Tetrapyrroles: Control Mechanisms of Chlorophyll Biosynthesis and Analysis of Chlorophyll-Binding Proteins. Elsevier, 2019. http://dx.doi.org/10.1016/s0065-2296(19)x0003-8.

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(Editor), Ravi Iyengar, and John D. Hildebrandt (Editor), eds. Methods in Enzymology, Volume 344: G Protein Pathways, Part B: G Proteins and Their Regulators (Methods in Enzymology). Academic Press, 2001.

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Recognition of Carbohydrates in Biological Systems, Part B: Specific Applications, Volume 363 (Methods in Enzymology). Academic Press, 2003.

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(Editor), John N. Abelson, Melvin I. Simon (Editor), and Krzysztof Palczewski (Editor), eds. Vertebrae Phototransduction and the Visual Cycle, Part B, Volume 316 (Methods in Enzymology). Academic Press, 2000.

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Ferran, Christiane. The Multiple Therapeutic Targets of A20. Springer, 2014.

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Ferran, Christiane. The Multiple Therapeutic Targets of A20. Springer, 2016.

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Book chapters on the topic "Chlorophyll a/b binding proteins"

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Ruban, A. V., A. J. Young, and P. Horton. "Quenching of Chlorophyll Fluorescence in the Minor Chlorophyll A/B Binding Proteins of Photosystem II." In Photosynthesis: from Light to Biosphere, 295–98. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_69.

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Funk, C., V. Lindström, and W. Vermaas. "Small Cab-Like Proteins: Relatives to the Chlorophyll A/B Binding Proteins in Cyanobacteria." In The Chloroplast: From Molecular Biology to Biotechnology, 103–6. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4788-0_15.

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Pichersky, Eran, and Beverley R. Green. "The Extended Family of Chlorophyll A/B-Binding Proteins of PSI and PSII." In Current Research in Photosynthesis, 2459–62. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_554.

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Kilian, R., and C. Schäfer. "Features and Functions of Chlorophyll A/B-Binding Proteins in Liverwort (Marchantia Polymorpha)." In Photosynthesis: from Light to Biosphere, 331–34. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_78.

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Färber, Andreas, and Peter Jahns. "The Xanthophyll Cycle of Higher Plants: Function of Chlorophyll a/b Binding Proteins and Membrane Stacking." In Photosynthesis: from Light to Biosphere, 3019–22. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_707.

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Ko, K., Z. W. Ko, D. H. Turpin, C. Labates, N. Mohanty, and A. Granell. "Overproduction of Chlorophyll A/B Binding Protein Enhances Photosynthetic Activity in Transgenic Tobacco." In Research in Photosynthesis, 445–48. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-009-0383-8_100.

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Paulsen, Harald, Christoph Dockter, Aleksei Volkov, and Gunnar Jeschke. "Chapter 16 Folding and Pigment Binding of Light-Harvesting Chlorophyll a/b Protein (LHCIIb)." In The Chloroplast, 231–44. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-8531-3_16.

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Buetow, Dennis E., Houqi Chen, Géza Erdős, and Lee S. H. Yi. "Regulation and expression of the multigene family coding light-harvesting chlorophyll a/b-binding proteins of photosystem II." In Molecular Biology of Photosynthesis, 283–319. Dordrecht: Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-009-2269-3_13.

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Abad, Mark, Steven Clark, and Gayle Lamppa. "Optimization of an Organelle-Free Processing Reaction for the Chlorophyll A/B Binding Protein Precursor." In Current Research in Photosynthesis, 2637–40. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_596.

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Lamppa, Gayle, Mark Abad, Steven Clark, and John Oblong. "Import and Processing of the Major Light-Harvesting Chlorophyll A/B Binding Protein of PSII." In Regulation of Chloroplast Biogenesis, 143–49. Boston, MA: Springer US, 1992. http://dx.doi.org/10.1007/978-1-4615-3366-5_20.

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Conference papers on the topic "Chlorophyll a/b binding proteins"

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Gao, Lan, and Hao-Ming Li. "Identification of a Light-Harvesting Chlorophyll a/b-Binding Protein Gene in Gardenia jasminoides." In International Conference on Chemical,Material and Food Engineering. Paris, France: Atlantis Press, 2015. http://dx.doi.org/10.2991/cmfe-15.2015.34.

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Obukhov, Yu N., K. V. Neverov, Yu V. Maleeva, and M. S. Kritsky. "Obtaining and properties of water-soluble chlorophyll-binding proteins (WSCP) from Brassica oleracea and Lepidiumvirginicum." In IX Congress of society physiologists of plants of Russia "Plant physiology is the basis for creating plants of the future". Kazan University Press, 2019. http://dx.doi.org/10.26907/978-5-00130-204-9-2019-319.

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Timmer, Marco, Efthymios Papazacharias, and Roland Goldbrunner. "Abstract 2164: Overexpression of the TERT binding proteins GABPA/B in Glioblastoma." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-2164.

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Lapetina, Eduardo G. "THE ROLE OF INOSITIDES, PHOSPHOLIPASE C AND G-PROTEINS IN RECEPTOR TRANSDUCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644775.

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It is now widely recognized that the activation of phospholipase C by specific agonists leads to the formation of two second messengers: (1) inositol trisphosphate, which releases Ca2+ from the endoplasmic reticulum to the cytosol and (2) 1,2- diacylglycerol, which stimulates protein kinase C. In the past few years, GTP-binding proteins have been associated with the regulation of phospholipase C. However, the identity of the GTP-binding protein involved and the type of association with phospholipase C is not yet known. It is now recognized that there are two types of phospholipase C enzymes: (a) a soluble enzyme that has been characterized in several tissues and does not preferentially hydrolyze polyphospholinositides and (b) membrane-bound enzymes that are coupled to the receptors, specifically hydrolyzing polyphosphoinositides and activated by membrane guanine nucleotide-binding proteins. Recent reports have tried to assess the involvement of GTP-binding proteins in the agonist-induced stimulation of phospholipase C, and various related aspects have been reported. These are concerned with: (a) detection of various GTP-binding proteins in platelets, (b) the effects of known inhibitors of GTP-binding proteins such as GDPgS or pertussis toxin on the agonist-induced stimulation of phospholipase C, (c) the direct effects of stimulators of GTP-binding proteins such as GTP, GTP-analogs and fluoride on phospholipase C activity, (d) the possible association of GTP-binding proteins to cytosolic phospholipase C that would then lead to degradation of the membrane-bound inositides and (e) cytosolic phospholipase C response to the activation of cell surface receptors. The emerging information has had contradictory conclusions. (1) Pretreatment of saponin-permeabilized platelets with pertussis toxin has been shown to enhance and to inhibit the thrombin-induced activation of phospholipase C. Therefore, it is not clear if a G protein that is affected by pertussis toxin in a manner similar to Gi or Go plays a central role in activation of phospholipase C. (2) Studies on the effect of GDPβ;S are also conflicting indicating that there may be GTP-independent and/or -dependent pathways for the activation of phosphoinositide hydrolysis. (3) A cytosolic phospholipase C is activated by GTP, and it has been advanced that this activity might trigger the hydrolysis of membrane-bound inositides. A cytosolic GTP-binding protein might be involved in this action, and it is speculated that an α-subunit might be released to the cytoplasm by a receptor-coupled mechanism to activate phospholipase C. However, no direct evidence exists to support this conclusion. Moreover, the exact contribution of phospholipase C from the membranes or the cytosol to inositide hydrolysis in response to cellular agonists and the relationship of those activites to membrane-bound or soluble GTP-binding proteins are unknown. Our results indicate that the stimulation of phospholipase C in platelets by GDPβS and thrombin are affected differently by GDPβS. GDPgSinhibits the formation of inositol phosphates produced by GTPγS but not that induced by thrombin. Thrombin, therefore, can directly stimulate phospholipase C without the involvement of a “stimulatory” GTP-binding protein, such as Gs, for the agonist stimulation of adenylate cyclase. However, an “inhibitory” GTP-binding protein might have some influence on thrombin-stimulated phospholipase C, since in the presence of GDPγS thrombin produces a more profound stimulation of phospholipase C.This “inhibitory” GTP-binding protein might be ADP-ribosylated by pertussis toxin because pertussis toxin can also enhance thrombin action on phospholipase C activity. Therefore, phospholipase C that responds to thrombin could be different from the one that responds to GTPγS. Cytosolic phospholipase C can be activated by GTP or GTP analogs, and the one that responds to thrombin should be coupled to the receptors present in the plasma membrane. The initial action of thrombin is to directly activate the plasma membrane-bound phospholipase C and the mechanism of this activation is probably related to the proteolytic action of thrombin or the activation of platelet proteases by thrombin. In agreement with this, trypsin can also directly activate platelet phospholipase C and, subsequently, GTPyS produces further activation of phospholipase C. If these two mechanisms are operative in platelets, the inhibition of cytosolic phospholipase C by GDPβS would allow a larger fraction of inositides for degradation of the thrombin-stimulated phospholipase C, as our results show.
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Philip, Subha, and Gopal C. Kundu. "OSTEOPONTIN REGULATES ACTIVATION OF PROMATRIX METALLOPROTEINASE-2 THROUGH NUCLEAR FACTOR-k-B-MEDIATED INDUCTION OF MEMBRANE TYPE 1 MATRIX METALLOPROTEINASE IN B16F10 CELLS." In 3rd International Conference on Osteopontin and SIBLING (Small Integrin-Binding Ligand, N-linked Glycoprotein) Proteins, 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.242.

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Wasi, S., P. Alles, D. Gauthier, U. Bhargava, J. Farsi, J. E. Aubin, and J. Sodeki. "STUDIES ON SMALL MOLECULAR WEIGHT ADHESION PROTEINS (SAPs) FROM CONNECTIVE TISSUES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643556.

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We have identified a family of low molecular weight proteins with cell attachment properties in a variety of soft and mineralised connective tissues (Wong et al., Biochem. J. 232, 119, 1985). For further characterisation of these proteins we extracted porcine bones with 4 M guanidine hydrochloride and purified the proteins on a series of gel filtration columns The purifed SAPs comprise three bands with Mr -14 000 -17 000. All three proteins bound to heparin-sepahrose in both the presence and absence of 4M urea, and when eluted with 2 M NaCl they retained their cell binding capacity. These proteins promoted the adhesion and spreading of a variety of cell types, including normal fibroblasts, osteoblasts, and epithelial cells, and tumour (osteosarcoma) cells. On Western blotting SAPs did not cross-react with antibodies against fibronectin, laminin or type I collagen; however, they were recognised by a monoclonal antibody to human vitronectin, a polyclonal antibody to bovine vitronectin and polyclonal antibody to human somatomedin B. Dose response experiments indicated that maximum attachment of human gingival fibroblasts occurred in the presence or absence of fetal bovine serum on wells precoated with 2.5 μg/cm2 of SAPs. Attachment of cells to these proteins was partially inhibited by the synthetic pentapeptide Gly-Arg-Gly-Asp-Ser. Utilising the nitrocellulose cell binding assay of Hayman et al (J. Cell. Biol. 95, 20, 1982), the cell attachment to these proteins could be completely inhibited by heparin (100 units/mL) whereas up to 1000 units/mL of heparin had no inhibitory effect on cell attachment to fibronectin and vitronectin. The occurrence of these proteins in a variety of connective tissues and their recognition by different cell types may reflect their general biological role in adhesive mechanisms in both hard and soft connective tissues. Currently, we are investigating the relationship between SAPs and vitronectin, since it is possible that SAPs represent a tissue-processed form of vitronectin or may be novel attachment proteins with regions of homology with vitronectin
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7

Stenflo, J., A.-K. öhlin, Å. Lundvall, and B. Dahlback. "β-HYDROXY ASPARTIC ACID AND ft-HYDROXYASPARAGINE IN THEEGF-HOMOLOGY REGIONS OF PROTEIN C AND PROTEINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643995.

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The amino acid sequence has been determined for all of the vitamin K-dependent proteins and the gene structure is known for some of them. These findings have shown the proteins to consist of four clearly discernible domains, except protein S which has six domains. The protein domains seem to be coded on separate exons (Foster, D. C. et. al. 1985 Proc. Natl. Acad. Sci. USA 82,4673). The vitamin K-dependent γ-carboxyglutamic acid (Gla) containing domain isthe common structural denominator of the members of this protein family. In addition, all of these proteins except prothrombin contain domains that are homologous to the precursor of the epidermal growth factor (EGF). Such domains arealso found in proteins that are not vitamin K-dependent, such as the low density lipoprotein receptor, thrombomodulin, factor XII, plasminogen, the tissue type plasminogen activator, urokinase and the complement protein Clr. The vitamin K-dependent proteins can be dividedinto three groups. Factors VII, IX, X, protein C and protein Z form one group, which in addition to the Gla-region have two EGF-homology regions and one domain that is homologous to the serine proteases. Prothrombin has two 'kringle' structures and a serine protease domain and constitutes a group of its own. Protein S is also unique in that it has four EGF-homology regions and a COOH-terminal region that is homologous to the sexual hormone binding globulin (see poster by Edenbrand et. al.).Recently a posttranslationally modified amino acid, B-hydroxyaspatic acid (Hya), was identified in position 71 in the NH2-terminal EGF-homology region ofbovine protein C. The amino acid is formed by hydroxylation of aspartic acid. It has also been identified in the corresponding positions in factors VII, IX,X and protein Z (i. e. proteins which like protein C have two EGF-homology regions each). In protein S the N2-terminal of four EGF-homology regions has hydroxy lated aspartic acid .whereas the following three EGF-like domains have B-hydroxyasparagine. The nucleotide sequence codes for asparagine in the three latter positions. Neither vitamin K nor vitamin C seem to be involvedin the formation of the two hydroxylated amino acids. Recently, Hya was identified in acid hydrolysates of the complement protein Clr. Hya and Hyn have onlybeen found in domains that are homologous to the EGF precursor. In an attempt to identify the structural requirement of the hydroxylating enzyme, we have compared the sequences of EGF-homology regions that contain Hya or Hyn with the corresponding sequences that have been shown not to contain the modified amino acids. The domains that have Hya or Hyn have the consensus sequence Cx xxxx xCxC. This sequence has been found in three EGF-like domains in the EGF-precursor, in two in the LDL-receptor and in two in thrombomodulin. Furthermore, the neurogenic Notch locus in Drosophila melanogaster codes for 36 EGF-homolgy regions, 22 of which contain the consensussequence, whereas the Lin-12 locus in Caenorhabditis elegans codes for at least 11 EGF-like repeats, two of which comply with the consensus sequence. Whether any of these proteins contain Hya orHyn is not yet known with certainty.It has been hypothesized that Hya isinvolved in the Gla independent Ca2+binding of factors IX, X and protein C. In an attempt to resolve this issue, we have isolated the EGF-homology region from human protein C and been able to demonstrate that it binds Ca2+ (see poster by öhlin and Stenflo). However, we do not yet know whether Hya is directly involved in the Ca2+binding.
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8

de Serres, M., H. M. Reisner, D. Monroe, and H. Roberts. "A MONOCLONAL ANTIBODY WHOSE BINDING IS INHIBITED BY DIVALENT CATIONS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644075.

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Factor IX (FIX), a vitamin K dependent coagulation protein, is functionally deficient or absent in patients with hemophilia B. Binding of Ca++ by the gammacarboxyglutamic acid residues (Gla) of FIX is necessary for coagulant activity. Antibodies havebeendes-cribed which selectively bind to FIX in the presence of Ca++ and appear to interact with Ca-H- stabilized epitopes of FIX. One IgM, Kappa murine monoclonal antibody (Mab), 129-1, has been found to react preferentially with FIX in the absence of Ca-H- or with FIX having a reduction in gammacarboxylation. 129-1 was characterized by direct binding ELISA assays, the standard assay buffer (.02M Tris - .15M NaCL pH 7.5) was supplemented with Ca-H- or ED TA to final concentrations to 5mM and lOmM respectively. In the presence of Ca-H-, titers ranged from 10 to 100 as compared to 100 K to 500 K in the presence of EDTA. Control Mab's, FIX-30 and 2D521 showed no such effect. Maximum inhibition occurred ≥2.5 mM Ca-H- concentration. Mg++, Sr-H- and Mn-H- were tested with similar results. Chemically degammacarboxylated FIXa was compared to FIX and FIXa controls in the presence of Ca-H- or EDTA, to determine the importance of Gla residues. In the presence of EDTA, Mab 129-1 had essentially equal reactivity with all these proteins (titers 100 K). In the presence of Ca-H-, binding to FIX and FIXa was inhibited (500 and 1 K respectively). However, the binding to Gla modified FIXa in the presence of Ca-H- was only slightly reduced (10 K), suggesting the importance of Gla residues in the Ca-H- mediated inhibition. FIX was purified from concentrate, coumadinized plasma and culture supernatant (produced in the absence of vitamin K) from the cell line PMN45 using HPLC affinity chromatography with Mab 2D521. Mab 129-1 binding to FIX immunopurified from concentrate and a control biochemically purified FIX protein preparation was significantly higher in the presence of EDTA (titers 500 and 5 K) than in Ca-H- (titers 10 and 10). FIX purified from coumadinized plasma or PMN45 cells showed equal low reactivity with 129-1 in the presence or absence of Ca-H- (titer 10 in all cases). FIX-30 and 2D521 controls showed no such reduction in binding. Therefore, Gla residues may play a role in the binding of 129-1 to FIX.
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9

Wu, K., C. Manner, and A. Tsai. "CHARACTERIZATION OF SERUM PROSTACYCLIN BINDING DEFECTS IN THROMBOTIC THROMBOCYTOPENIC PURPURA (TTP)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643978.

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To understand further the pathophysiologic significance of PGI2 binding defects in TTP, we measured serum PGI2 binding activity in 12 TTP patients and matched controls. Serum binding of PGI2 was measured by Sephadex G-25 gel filtration. The mean binding activity in 33 healthy subjects ages 20-40 years was 39.9 ± S.D 4.4%. The mean value of TTP (n=12) was significantly lower (26.2 ± 4.1, P <0.01). Serum from 5 severe ITP, 5 DIC and 5 thrombocythemia exhibited normal binding ctivity. To determine the binding kinetics we utilized 3H-iloprost in a gel filtration method described by Hirose and Kano (Biochim. Biophys. Acta. 751:376, 1971). To 50 mg of Sephadex G-50, 0.435 ml of 50mM Tris buffer (pH 7.4) was added. After swelling of the gel was completed 0.195 ml of the buffer solution containing serum and 3H-iloprost was added. The sample was mixed and the protein and ligand concentration was determined. The computer fitting of the binding isotherm according to the originally proposed equation yielded a binding curve consistent with a single class of binding sites. The Kd value of normal serum was 70 μM and the B 48 nmol/ml. Acute TTP serum exhibited a reduced bindingXaffinity (Kd 236 μM) and a slightly elevated capacity (Bmax 85 nmols/ml). The binding parameters improved following successful treatment but the Kd remained subnormal (120 μM). These data indicate that reduced PGI2 binding activity is due to lower affinity of the PGI2 binding proteins. The relationship between defective PGI2 binding activity and PGI2 production was then evaluated. Serial serum and 24 hour urine were collected. Urinary samples were extracted and their 6-Keto-PGF1α (6KP) and thromboxane TXB2 levels were measured by RIA. TTP patients in remission had normal levels of urinary 6KP and TXB2 while urinary 6KP and TXB2 were elevated in relapsing TTP. Defective binding was noted when relapse began to occur while elevated 6KP and TXB2 were noted 48 hrs later. Both 6KP and TXB2 were normalized when the disease was controlled. Our findings indicate that defective PGI2 binding plays an important role in causing excessive platelet activation and platelet-vessel wall interaction in TTP.
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10

Gustafson, E. J., H. Lukasiewicz, A. H. Schmaier, S. Niewiarowski, and R. W. Colman. "FIBRINOGEN BINDS TO HUMAN NEUTROPHILS AT A SITE DISTINCT FROM GPIIb/IIIa." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643850.

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Many observations suggest a potential role for neutrophils in the modulation of hemostasis and thrombosis. Arterial thrombi are characterized by the presence of large numbers of neutrophils lining the perimeter of platelet aggregates. While investigating binding of high molecular weight kininogen (HMWK) to neutrophils, we found that fibrinogen (Fb) could inhibit binding of 125I-HMWK as well as displace HMWK already bound to neutrophils. We therefore initiated studies to determine whether Fb could bind to human neutrophils. Both Zn++ and Ca++ were required for maximal binding of 125I-Fb to neutrophils. Binding did not occur with Ca++ (ZmM) alone and was only 1/3 the maximal amount with Zn++ (50 μM) alone. At 4° the amount of 125I-Fb bound to neutrophils reached a plateau by 15 minutes and remained at this level over the next 30 minutes. At 23° and 37° the amount of 125I-Fb bound peaked by 4 minutes and then decreased over the next 30 minutes indicating receptor-mediated internalization. Excess Fb inhibited binding of 125I-Fb to neutrophils while prekal1ikrein, factor XII, and fibronectin did not. Binding of 125I-Fb was 99% reversible at 4° within 10 minutes with a 50-fold molar excess of Fb and 90% displaceable by excess HMWK. The apparent Kd was approximately 0.45 μM. Arg-Gly-Asp-Ser (RGDS) is a tetrapeptide common to Fb, fibronectin, vitronectin and other cel 1-attachment proteins. Fb has been demonstrated to bind to the glycoprotein IIb/111 a (GPIIb/IIIa) complex which is the platelet membrane receptor for RGDS. Although this RGDS-GPIIb/IIIa interaction occurs with Fb binding to platelets, it is apparently not involved with Fb binding to monocytes. To investigate if Fb binding to neutrophils involved this interaction of GPIIb/II la -RGDS we performed further studies. Binding of 125I-Fb to neutrophils was not inhibited by RGDS nor was it inhibited by a monoclonal antibody (10E5) to the platelet GPI I b/IIIa complex. In addition, the amount of 125I-Fb that hound to neutrophils from a patient with Glanzman's thrombosthenia was the same as that bound to normal neutrophils. These studies indicate that human neutrophils specifically bind Fb at a site similar to HMWK and distinct from GPIIb/IIIa.
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