Готові списки джерел за темами / Calcium and integrin binding protein

Добірка наукової літератури з теми "Calcium and integrin binding protein"

Автор: Grafiati
Опубліковано: 10 грудня 2022
Оновлено: 28 січня 2023

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Статті в журналах з теми "Calcium and integrin binding protein"

1

Tsuboi, Shigeru. "Calcium Integrin-binding Protein Activates Platelet Integrin αIIbβ3". Journal of Biological Chemistry 277, № 3 (9 листопада 2001): 1919–23. http://dx.doi.org/10.1074/jbc.m110643200.

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2

Dickens, Olivia, Raul Mendez-Giraldez, and Nikolay Dokholyan. "Modeling the Calcium and Integrin Binding Protein 2." Biophysical Journal 108, no. 2 (January 2015): 213a. http://dx.doi.org/10.1016/j.bpj.2014.11.1178.

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3

Hodivala, KJ, and FM Watt. "Evidence that cadherins play a role in the downregulation of integrin expression that occurs during keratinocyte terminal differentiation." Journal of Cell Biology 124, no. 4 (February 15, 1994): 589–600. http://dx.doi.org/10.1083/jcb.124.4.589.

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In epidermis the onset of terminal differentiation normally coincides with inhibition of integrin function and expression, thereby ensuring that differentiating cells are selectively expelled from the basal layer. However, when stratification of cultured human epidermal keratinocytes is prevented by reducing the calcium concentration of the medium to 0.1 mM, keratinocytes initiate terminal differentiation while still attached to the culture substrate. We have examined the mechanism by which differentiating keratinocytes adhere to extracellular matrix proteins in low calcium medium and the consequences of inducing stratification by raising the calcium ion concentration to 1.8 mM (Standard Medium). In low calcium medium keratinocytes co-expressed integrins and terminal differentiation markers such as involucrin and peanut lectin-binding glycoproteins: differentiating cells contained integrin mRNA, synthesized integrin proteins de novo and expressed functional mature integrins. There were no differences in integrin synthesis, maturation or break down in low calcium or standard medium, although the level of beta 1 integrins on the surface of proliferating cells was higher in standard medium. Within 6 h of transfer from low calcium to standard medium integrin mRNA was no longer detectable in terminally differentiating cells, integrins were being lost from the cell surface, and selective migration out of the basal layer had begun. Antibodies to P- and E-cadherin, which block calcium-induced stratification, prevented the selective loss of integrin mRNA and protein from terminally differentiating cells. This suggests that cadherins may play a role in the down-regulation of integrin expression that is associated with terminal differentiation.
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4

Huang, Hao, Joel N. Bogstie, and Hans J. Vogel. "Biophysical and structural studies of the human calcium- and integrin-binding protein family: understanding their functional similarities and differences." Biochemistry and Cell Biology 90, no. 5 (October 2012): 646–56. http://dx.doi.org/10.1139/o2012-021.

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The human calcium- and integrin-binding protein 1 (CIB1) plays important roles in various cellular functions. In this study, three other members of this protein family (CIB2–4: CIB2, CIB3, and CIB4) were purified and subsequently characterized using biophysical and structural approaches. As expected from sequence alignments, CIB2–4 were shown to bind calcium (Ca2+) and magnesium (Mg2+) ions. Binding of Ca2+ or Mg2+ ions changes the secondary structure of CIB2–4 and the exposure of hydrophobic surface area. Ca2+ and Mg2+ ions also stabilize the tertiary structures for CIB2 and CIB3. Through in vitro binding experiments, we show that CIB2 can interact with the integrin αIIb cytoplasmic domain and the integrin α7b membrane-proximal fragment. Fluorescence experiments using a 7-azatryptophan labeled peptide demonstrate that CIB2, CIB3, and CIB4 are binding partners for the integrin αIIb subunit, which suggests that they are potentially involved in regulating integrin αIIb subunit activation. The distinct responses of αIIb to the different CIB3 and CIB4 metal (Ca2+ and Mg2+) binding states imply a potential connection between the calcium and integrin signaling pathways.
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5

Vallar, Laurent, Chantal Melchior, Sébastien Plançon, Hervé Drobecq, Guy Lippens, Véronique Regnault та Nelly Kieffer. "Divalent Cations Differentially Regulate Integrin αIIbCytoplasmic Tail Binding to β3and to Calcium- and Integrin-binding Protein". Journal of Biological Chemistry 274, № 24 (11 червня 1999): 17257–66. http://dx.doi.org/10.1074/jbc.274.24.17257.

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6

Yamniuk, Aaron P., та Hans J. Vogel. "Calcium- and magnesium-dependent interactions between calcium- and integrin-binding protein and the integrin αIIb cytoplasmic domain". Protein Science 14, № 6 (1 січня 2009): 1429–37. http://dx.doi.org/10.1110/ps.041312805.

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7

Arora, Pamela D., Michael Glogauer, Andras Kapus, David J. Kwiatkowski, and Christopher A. McCulloch. "Gelsolin Mediates Collagen Phagocytosis through a Rac-dependent Step." Molecular Biology of the Cell 15, no. 2 (February 2004): 588–99. http://dx.doi.org/10.1091/mbc.e03-07-0468.

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The role of gelsolin, a calcium-dependent actin-severing protein, in mediating collagen phagocytosis, is not defined. We examined α2β1 integrin-mediated phagocytosis in fibroblasts from wild-type (WT) and gelsolin knockout (Gsn-) mice. After initial contact with collagen beads, collagen binding and internalization were 60% lower in Gsn- than WT cells. This deficiency was restored by transfection with gelsolin or with β1 integrin-activating antibodies. WT cells showed robust rac activation and increased [Ca2+]i during early contact with collagen beads, but Gsn- cells showed very limited responses. Transfected gelsolin in Gsn- cells restored rac activation after collagen binding. Transfection of Gsn- cells with active rac increased collagen binding to WT levels. Chelation of intracellular calcium inhibited collagen binding and rac activation, whereas calcium ionophore induced rac activation in WT and Gsn- cells. We conclude that the ability of gelsolin to remodel actin filaments is important for collagen-induced calcium entry; calcium in turn is required for rac activation, which subsequently enhances collagen binding to unoccupied α2β1 integrins.
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8

Yamniuk, Aaron P., Leonard T. Nguyen, Tung T. Hoang, and Hans J. Vogel. "Metal Ion Binding Properties and Conformational States of Calcium- and Integrin-Binding Protein†." Biochemistry 43, no. 9 (March 2004): 2558–68. http://dx.doi.org/10.1021/bi035432b.

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SHOCK, David D., Ulhas P. NAIK, Julia E. BRITTAIN, Suresh K. ALAHARI, John SONDEK та Leslie V. PARISE. "Calcium-dependent properties of CIB binding to the integrin αIIb cytoplasmic domain and translocation to the platelet cytoskeleton". Biochemical Journal 342, № 3 (5 вересня 1999): 729–35. http://dx.doi.org/10.1042/bj3420729.

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The αIIbβ3 integrin receives signals in agonist-activated platelets, resulting in its conversion to an active conformation that binds fibrinogen, thereby mediating platelet aggregation. Fibrinogen binding to αIIbβ3 subsequently induces a cascade of intracellular signalling events. The molecular mechanisms of this bi-directional αIIbβ3-mediated signalling are unknown but may involve the binding of proteins to the integrin cytoplasmic domains. We reported previously the sequence of a novel 22-kDa, EF-hand-containing, protein termed CIB (calcium- and integrin-binding protein) that interacts specifically with the αIIb cytoplasmic domain in the yeast two-hybrid system. Further analysis of numerous tissues and cell lines indicated that CIB mRNA and protein are widely expressed. In addition, isothermal titration calorimetry indicated that CIB binds to an αIIb cytoplasmic-domain peptide in a Ca2+-dependent manner, with moderate affinity (Kd, 700 nM) and 1:1 stoichiometry. In aggregated platelets, endogenous CIB and αIIbβ3 translocate to the Triton X-100-insoluble cytoskeleton in a parallel manner, demonstrating that the cellular localization of CIB is regulated, potentially by αIIbβ3. Thus CIB may contribute to integrin-related functions by mechanisms involving Ca2+-modulated binding to the αIIb cytoplasmic domain and changes in intracellular distribution.
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10

Sekimoto, Hiroko, Jodi Eipper-Mains, Sunthorn Pond-Tor та Charlotte M. Boney. "αvβ3 Integrins and Pyk2 Mediate Insulin-Like Growth Factor I Activation of Src and Mitogen-Activated Protein Kinase in 3T3-L1 Cells". Molecular Endocrinology 19, № 7 (1 липня 2005): 1859–67. http://dx.doi.org/10.1210/me.2004-0481.

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Abstract IGF-I stimulates cell growth through interaction of the IGF receptor with multiprotein signaling complexes. However, the mechanisms of IGF-I receptor-mediated signaling are not completely understood. We have previously shown that IGF-I-stimulated 3T3-L1 cell proliferation is dependent on Src activation of the ERK-1/2 MAPK pathway. We hypothesized that IGF-I activation of the MAPK pathway is mediated through integrin activation of Src-containing signaling complexes. The disintegrin echistatin decreased IGF-I phosphorylation of Src and MAPK, and blocking antibodies to αv and β3 integrin subunits inhibited IGF-I activation of MAPK, suggesting that αvβ3 integrins mediate IGF-I mitogenic signaling. IGF-I increased ligand binding to αvβ3 as detected by immunofluorescent staining of ligand-induced binding site antibody and stimulated phosphorylation of the β3 subunit, consistent with inside-out activation of αvβ3 integrins. IGF-I increased tyrosine phosphorylation of the focal adhesion kinase (FAK) Pyk2 (calcium-dependent proline-rich tyrosine kinase-2) to a much greater extent than FAK, and increased association of Src with Pyk2 but not FAK. The intracellular calcium chelator BAPTA prevented IGF-I phosphorylation of Pyk2, Src, and MAPK, suggesting that IGF-I activation of Pyk2 is calcium dependent. Transient transfection with a dominant-negative Pyk2, which lacks the autophosphorylation and Src binding site, decreased IGF-I activation of MAPK, but no inhibition was seen with transfected wild-type Pyk2. These results indicate that IGF-I signaling to MAPK is dependent on inside-out activation of αvβ3 integrins and integrin-facilitated multiprotein complex formation involving Pyk2 activation and association with Src.
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Дисертації з теми "Calcium and integrin binding protein"

1

Blamey, Chad Joseph. "Calcium- and integrin-binding protein 1 structure and function /." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file 3.06 Mb., p, 2006. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pqdiss&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&rft_dat=xri:pqdiss:3220732.

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Thesis (Ph.D.)--University of Delaware, 2006.
Principal faculty advisors: Ulhas P. Naik, Dept. of Biological Sciences and Brian J. Bahnson, Dept. of Chemistry and Biochemistry. Includes bibliographical references.
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2

Maddox, Katherine. "A characterization of the calcium- and integrin-binding protein family." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 112 p, 2009. http://proquest.umi.com/pqdweb?did=1654487501&sid=7&Fmt=2&clientId=8331&RQT=309&VName=PQD.

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3

Rousset, Céline. "Étude de l'interaction entre le domaine cytoplasmique de l'intégrine [alpha]IIb et la "calcium- and integrin-binding protein (CIB)"." Lille 1, 2002. https://pepite-depot.univ-lille.fr/RESTREINT/Th_Num/2002/50376-2002-331.pdf.

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La "calcium- and integrin-binding protein" (CIB) est une protéine cytoplasmique fixatrice de calcium, interagissant spécifiquement avec le domaine cytoplasmique de la sous-unité alpha de l'intégrine [alpha]IIb[bêta]3 (intégrine spécifique des plaquettes sanguines). Dans le but d'apporter des informations structurales concernant cette interaction et de façon à contribuer à élucider le rôle de CIB vis-à-vis du récepteur plaquettaire [alpha]IIb[bêta]3, nous avons étudié l'interaction in vitro entre un peptide correspondant à la partie cytoplasmique de la sous-unité [alpha]IIb : le peptide [alpha]IIb(Kexp. 989-Eexp. 1008) et le domaine C-terminal de CIB, celui là même capable de fixer le calcium. La RMN a été notre technique de choix pour étudier cette interaction au niveau moléculaire. L'obtention de l'un et l'autre des partenaires pur et enrichi en isotopes stables 15N et 13C s'est effectuée grâce à l'utilisation du domaine B1 de la protéine G de streptocoque en tant que protéine de fusion. Cette étape nous a permis dans un premier temps de définir les conditions d'expression, de purification et de solubilisation adéquates pour l'obtention de spectres RMN de qualité et exploitables pour chacune des molécules seules en solution, et d'en étudier les caractéristiques structurales et biochimiques. Dans un second temps, nous avons étudié l'une et l'autre des molécules dans leur interaction avec leur partenaire moléculaire. Nous avons tout d'abord constaté que l'interaction est caractérisée par une faible affinité
Ceci nous a notamment permis de montrer que sur le peptide correspondant au domaine cytoplasmique de [alpha]IIb, l'interaction implique des résidus situés dans une séquence juxta-membranaire conservée entre les sous-unités alpha des intégrines (GFFKR). Cette séquence est justement importante pour une interaction de nature électrostatique et hydrophobe avec la séquence conservée juxta-membranaire des sous-unités bêta (LLxxxHDR). Ainsi, si une interaction entre les domaines cytoplasmiques des intégrines [alpha] et [bêta] permet le maintien d'un récepteur inactif (récepteur de faible affinité pour un ligand extracellulaire), alors en interagissant avec cette séquence conservée juxta-membranaire de la sous-unité [alpha]IIb, il est probable que CIB soit un des facteurs intracellulaire susceptible de supprimer cette interaction et ainsi susceptible de provoquer l'activation du récepteur (conversion du récepteur de basse affinité vers un récepteur de haute affinité pour un ligand extracellulaire), ou bien de le maintenir dans une conformation active (haute affinité pour le ligand). Selon nos résultats, l'affinité entre le peptide [alpha]IIb(Kexp. 989-Eexp. 1008) et le domaine C-terminal de CIB est faible. Cette donnée associée aux résultats d'une autre équipe de recherche selon laquelle il existe une forte affinité entre un peptide plus long [alpha]IIb(Lexp. 983-Eexp. 1008) et CIB suggère que CIB occupe très certainement un rôle dans le maintien d'une intégrine [alpha]IIb[bêta]3 activée plutôt que dans l'activation proprement dite du récepteur
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4

Wang, Xue. "Predicting Protein Calcium Binding Sites." Digital Archive @ GSU, 2009. http://digitalarchive.gsu.edu/cs_diss/46.

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Calcium is one of the closely relevant metal ions that involves in enormous physicochemical activities in human body, including cell division and apoptosis, muscle contraction, neurotransmitter release, enzyme activation, and blood-clotting. Calcium fulfills its functions through the binding to different classes of calcium-binding proteins. To facilitate our understanding of the roles of calcium in biological systems, and to design novel metal-binding proteins with tailored binding capabilities, it is important to develop computation algorithms to predict calcium-binding sites in different classes of proteins. In literature, calcium-binding sites may be represented by either a spacial point, or the set of residues chelating calcium ion. A thorough statistical analysis of known calcium-binding proteins deposited in Protein Data Bank gives reference values of various parameters characterizing geometric and chemical features in calcium-binding sites including distances, angles, dihedral angles, the Hull property, coordination numbers, ligand types and formal charges. It also reveals clear differences between the well-known EF-hand calcium-binding motif and other calcium-binding motifs. Utilizing the above multiple geometric and chemical parameters in well-formed calcium binding sites, we developed MUG (MUltiple Geometries) program. MUG can re-identify the coordinates of the documented calcium ion and the set of ligand residues. Three previously published data sets were tested. They are comprised of, respectively, 19, 44 and 54 holo protein structures with 48, 92 and 91 documented calcium-binding sites. Defining a "correct hit" as a point within 3.5 angstrom to the documented calcium location, MUG has a sensitivity around 90% and selectivity around 80%. The set of ligand residues (calcium-binding pockets) were identified for 43, 66 and 63 documented calcium ion in these three data set respectively. In order to achieve true prediction, our program was then enhanced to predict calcium-binding pockets in apo (calcium-free) proteins. Our new program MUGSR accounts for the conformational changes involved in calcium-binding pockets before and after the binding of calcium ions. It is able to capture calcium binding pockets that may undergo local conformational changes or side chain torsional rotations, which is validated by referring back to the corresponding holo protein structure sharing more than 98% sequence similarity with the apo protein.
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5

Vosnidou, Nancy Carol Hoffman. "Computational analysis of cadherins : sequence analysis of dimerization properties and quantum caculations of calcium coordination characteristics /." free to MU campus, to others for purchase, 2002. http://wwwlib.umi.com/cr/mo/fullcit?p3060154.

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6

Bouissou, Camille. "Encapsulation of an integrin-binding protein into PLGA microspheres." Thesis, University of Bath, 2006. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.432835.

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7

Walker, Simon W. "Studies on the intracellular calcium-binding protein calmodulin." Thesis, University of Oxford, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.235957.

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8

Rönning, Sanne. "Selection of a calcium-dependent IgG1-binding protein domain." Thesis, Uppsala universitet, Institutionen för biologisk grundutbildning, 2020. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-417065.

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Standard purification processes in large scale antibody production are largely dependent on Protein A chromatography. Protein A binds specifically to many subclasses of IgG with high affinity. However, in order to elute the proteins, the pH needs to be lowered. Since lowering of the pH can be detrimental to some antibodies, a milder purification process is of great interest. A variant of Protein A, called ZCa, has previously been engineered to bind to IgG in a calcium-dependent manner. The antibody binds to ZCa when calcium is present and releases when calcium is removed. For the IgG1 subclass, the elution still requires a slight lowering of the pH, which is why there is room for improvement of the molecule. A phage display selection has been performed with the aim to obtain calcium-dependent IgG1 binders that are able to release the antibodies upon calcium depletion at neutral pH. In addition, an attempt on increasing the alkaline stability of the binders was made. Sequence analysis of the selection output showed almost no indications of increased alkaline stability. Instead, M13K07 helper phages were exposed to new selections for increased alkaline tolerance which might be useful in future phage display selections. Even though the binders selected for in this project did show some promising characteristics, none of them were able to elute upon calcium depletion at neutral pH as aimed for. However, one of the variants did show promising results during most of the performed characterizations. Most interestingly, the elution properties of this variant could indicate a higher calcium-dependence in the interaction with the target than that of ZCa, although further characterizations need to be performed in order to draw any conclusions about possible improvements of this protein domain.
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9

Kumar, Mohit. "Cardiac Myosin Binding Protein-C phosphorylation Regulates Calcium Homeostasis." University of Cincinnati / OhioLINK, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=ucin159584822092564.

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Woodard-Grice, Alencia V. "Hyposialylation regulates [alpha]4[beta]1 integrin binding to VCAM-1." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2008. https://www.mhsl.uab.edu/dt/2009r/woodard.pdf.

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Книги з теми "Calcium and integrin binding protein"

1

Vogel, Hans J. Calcium-Binding Protein Protocols. New Jersey: Humana Press, 2002. http://dx.doi.org/10.1385/1592591833.

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2

Vogel, Hans J. Calcium-Binding Protein Protocols. New Jersey: Humana Press, 2002. http://dx.doi.org/10.1385/1592591841.

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J, Vogel Hans, ed. Calcium-binding protein protocols. Totowa, NJ: Humana Press, 2002.

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4

International Symposium on Calcium-Binding Proteins in Health and Disease (6th 1988 Nagoya-shi, Japan). Calcium protein signaling. Edited by Hidaka Hiroyoshi 1938-. New York: Plenum Press, 1989.

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5

Blum-Moonesinghe, Janaki Kumari. Expression of calcium-binding proteins in chemically transformed rat fibroblasts. Konstanz: Hartung-Gorre Verlag, 1993.

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6

Berchtold, Martin W. Structure and expression of genes for parvalbumin and other EF-hand type CA2 - binding proteins. Zürich: Hartung-Gorre, 1990.

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7

European, Symposium on Calcium Binding Proteins in Normal and Transformed Cells (1st 1989 Brussels Belgium). Calcium binding proteins in normal and transformed cells. New York: Plenum Press, 1990.

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8

Berchtold, Martin W. Structure and expression of genes for parvalbumin and other EF-hand type CA²⁺--binding proteins. Zürich: Hartung-Gorre, 1990.

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9

Means, Anthony R. Calcium regulation of cellular function. New York: Raven Press, 1995.

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10

Eng, Susan Y. Metal binding studies on pig intestinal calcium binding protein. 1987.

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Частини книг з теми "Calcium and integrin binding protein"

1

Huang, Hao, and Hans J. Vogel. "Purification and Stable Isotope Labeling of the Calcium- and Integrin-Binding Protein 1 for Structural and Functional NMR Studies." In Methods in Molecular Biology, 99–113. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-230-8_7.

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2

Doyle, D. John. "Calcium Protein Binding (CALCIUM)." In Computer Programs in Clinical and Laboratory Medicine, 138–41. New York, NY: Springer New York, 1989. http://dx.doi.org/10.1007/978-1-4612-3576-7_31.

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3

Dempsey, Brian R., Anne C. Rintala-Dempsey, Gary S. Shaw, Yuan Xiao Zhu, A. Keith Stewart, Jaime O. Claudio, Constance E. Runyan, et al. "S100 Calcium-Binding Protein." In Encyclopedia of Signaling Molecules, 1711. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101220.

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4

Ogawa, Yasuo. "Cooperativity in Calcium Binding and Calcium Dependent Reactions." In Calcium Protein Signaling, 205–14. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5679-0_22.

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5

Kuźnicki, Jacek. "Calcyclin, from Gene to Protein." In Novel Calcium-Binding Proteins, 157–67. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76150-8_10.

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6

Tanaka, Toshio, and Hiroyoshi Hidaka. "Calcium Signaling of Calcium-Binding Proteins and Drug Actions." In Calcium Protein Signaling, 165–71. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5679-0_18.

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Kirberger, Michael, and Jenny J. Yang. "Calcium-Binding Protein Site Types." In Encyclopedia of Metalloproteins, 511–21. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_35.

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8

Suzuki, Koichi, Yasufumi Minami, Yasufumi Emori, Shinobu Imajoh, and Hiroshi Kawasaki. "Analysis of Calcium-Binding Sites in Calcium-Activated Neutral Protease." In Calcium Protein Signaling, 173–83. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5679-0_19.

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Rao, Ramachandra M., Eric W. Young, and David A. McCarron. "Disregulation of Cell Calcium and Calcium-Binding Proteins in Experimental Hypertension." In Calcium Protein Signaling, 505–14. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5679-0_53.

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10

Winsky, Lois, and David M. Jacobowitz. "Purification, Identification and Regional Localization of a Brain-Specific Calretinin-Like Calcium Binding Protein (Protein 10)." In Novel Calcium-Binding Proteins, 277–300. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76150-8_16.

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Тези доповідей конференцій з теми "Calcium and integrin binding protein"

1

Ringuette, Maurice, Rong Xhu, Baoqian Zhu, Jaro Sodek, and Theodore J. Brown. "IDENTIFICATION OF A NOVEL ATP/GTP-BINDING PROTEIN PARTNER FOR OSTEOPONTIN." 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.2002.278.

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2

Udomsom, Suruk, Punramon Rattakorn, Ukrit Mankong, Toshimasa Umezawa, Atsushi Matsumoto, Atsushi Kanno, Naokatsu Yamamoto, et al. "Detection of S100 Calcium Binding Protein A6 by Silicon Nitride Photonic Sensor." In 2022 International Electrical Engineering Congress (iEECON). IEEE, 2022. http://dx.doi.org/10.1109/ieecon53204.2022.9741660.

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3

Dahiback, Bjorn, Ake Lundwall, Andreas Hillarp, Johan Malm, and Johan Stenflo. "STRUCTURE AND FUNCTION OF VITAMIN K-DEPENDENT PROTEIN S, a cofactor to activated protein C which also interacts with the complement protein C4b-binding protein." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642960.

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Анотація:
Protein S is a single chain (Mr 75.000) plasma protein. It is a cofactor to activated protein C (APC) in the regulation of coagulation factors Va and Villa. It has high affinity for negatively charged phospolipids and it forms a 1:1 complex with APC on phospholipid surfaces, platelets and on endothelial cells. Patients with heterozygous protein S deficiency have a high incidence of thrombosis. Protein S is cleaved by thrombin, which leads to a loss of calcium binding sites and of APC cofactor activity. Protein S has two to three high affinity (KD 20uM) calcium binding sites - unrelated to the Gla-region - that are unaffected by the thrombin cleavage. In human plasma protein S (25 mg/liter) circulates in two forms; free (approx. 40%) and in a 1:1 noncovalent complex (KD 1× 10-7M) with the complement protein C4b-binding protein (C4BP). C4BP (Mr 570.000) is composed of seven identical 70 kDa subunits that are linked by disulfide bonds. When visualized by electron microscopy, C4BP has a spiderlike structure with the single protein S binding site located close to the central core and one C4b-binding site on each of the seven tentacles. When bound to C4BP, protein S looses its APC cofactor activity, whereas the function-of C4BP is not directly affected by the protein S binding. Chymotrypsin cleaves each of the seven C4BP subunits close to the central core which results in the liberation of multiple 48 kDa “tentacte” fragments and the formation of a 160 kDa central core fragment. We have successfully isolated a 160 kDa central core fragment with essentially intact protein S binding ability.The primary structure of both bovine and human protein S has been determined and found to contain 635 and 634 amino acids, respectively, with 82 % homology to each other. Four different regions were distinguished; the N-terminal Gla-domain (position 1-45) was followed by a region which has two thrombin-sensitive bonds positioned within a disulfide loop. Position 76 to 244 was occupied by four repeats homologous to the epidermal growth factor (EGF) precursor. In the first EGF-domain a modified aspartic acid was identified at position 95, B-hydroxaspartic acid (Hya), and in corresponding positions in the three following EGF-domains (positions 136,178 and 217) we found B-hydroxyasparagine (Hyn). Hyn has not previously been identified in proteins. The C-terminal half of protein S (from position 245) shows no homology to the serine proteases but instead to human Sexual Hormon Binding Globulin (SHBG)(see separate abstract). To study the structure-function relationship we made eighteen monoclonal antibodies to human protein S. The effects of the monoclonals on the C4BP-protein S interaction and on the APC cofactor activity were analysed. Eight of the antibodies were calciumdependent, four of these were against the Gla-domain, two against the thrombin sensitive portion and two against the region bearing the high affinity calcium binding sites. Three of the monoclonals were dependent on the presence of chelating agents, EDTA or EGTA, and were probably directed against the high affinity calcium binding region. Three other monoclonals inhibited the protein S-C4BP interaction. At present, efforts are made to localize the epitopes to gain information about functionally important regions of protein S.
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4

Akiyama, N., H. Hozumi, H. Yasui, M. Kono, Y. Suzuki, M. Karayama, K. Furuhashi, et al. "Clinical Utility of Serum S100 Calcium Binding Protein A4 in Idiopathic Pulmonary Fibrosis." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a7131.

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5

Ren, Hui, Ting Wang, and Mingwei Chen. "Expression and clinical significance of S100 calcium binding protein A2 in lung cancer." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa2868.

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6

Jain, Prachi, Somesh Baranawal, and Suresh K. Alahari. "Abstract 2196: Tumor suppressor LKB1 cooperates with the integrin-binding protein Nischarin to inhibit breast cancer." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2196.

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7

KÖhlin, A., and J. Stenflo. "HIGH AFFINITY CALCIUM BINDING TO DOMAINES OF PROTEIN C THAT ARE HOMOLOGUS TO THE EPIDERMAL GROWTH FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643645.

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In addition to γ-carboxyglutamic acid (Gla)-dependent calcium binding all of the vitamin K-dependent plasma proteins, except prothrombin, have one or two high affinity calcium binding sites that do not require the Gla residues. A common denominator among these proteins (factors IX, X, protein C, protein Z and protein S) is that they have domaines that are homologus to the epidermal growth factor (EGF) precursor. In factors VII,IX,X, protein C and in protein Z the aminoterminal of two EGF homology regions contain one residue of β-hydroxyaspartic acid (Hya) whereas in protein S the aminoterminal EGF homology region contains Hya and the three following contain one β-hydroxyasparagine residue each.In an attempt to elucidate the role of the EGF homology regions in the Gla independent calcium binding we have isolated a tryptic fragment (residue 44-138) from the light chain of human protein C. The fragment was isolated using a monoclonal antibody that recognizes a calcium ion stabilized epitope that is expressed both in intact protein C and in protein C lacking the Gla domaine.The antibody bound the isolated EGF homology region in the presence of calcium ions but not in EDTA containing buffer. A calcium ion titration showed half maximal binding at approximately 200 μM Ca2+. The metal ion induced conformational change in the isolated fragment was also studied with affinity purified rabbit antibodies against Gla domainless protein C. Antibodies that bound in the presence of calcium ions and that could be eluted with EDTA recognized the metal ion induced conformational change in the isolated EGF homology domain. Our results suggest that one or both of the EGF homology regions are involved in the Gla-independent high affinity calcium binding in the vitamin K-dependent plasma proteins.
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8

Shala, Kastriot, Bin Yang, Teng Teng To, Richard W. Pickersgill, Norbert Krauss, and Robert Donnan. "Millimeter wave spectrometry of glucose and a calcium-binding protein using a vector network analyzer." In 2010 35th International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz 2010). IEEE, 2010. http://dx.doi.org/10.1109/icimw.2010.5612418.

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9

Speer, Mei Y., Marc D. McKee, Robert E. Guldberg, Lucy Liaw, Gerard Karsenty, Hsueh-Ying Yang, Elyse Tung, and Cecilia M. Giachelli. "OSTEOPONTIN, AN INDUCIBLE INHIBITOR OF VASCULAR CALCIFICATION IN MATRIX GLA PROTEIN-DEFICIENT MICE." 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.2002.244.

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10

Cavalier, Michael C., Laura McKnight, David Weber, and Paul Wilder. "Abstract 2226: Structure/function characterization of SBi4225, a novel inhibitor of the calcium-binding protein S100B." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-2226.

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Звіти організацій з теми "Calcium and integrin binding protein"

1

Nelson, Nathan, and Charles F. Yocum. Structure, Function and Utilization of Plant Photosynthetic Reaction Centers. United States Department of Agriculture, September 2012. http://dx.doi.org/10.32747/2012.7699846.bard.

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Light capturing and energy conversion by PSI is one of the most fundamental processes in nature. In the heart of these adaptations stand PSI, PSII and their light harvesting antenna complexes. The main goal of this grant proposal was to obtain by X-ray crystallography information on the structure of plant photosystem I (PSI) and photosystem II (PSII) supercomplexes. We achieved several milestones along this line but as yet, like several strong laboratories around the world, we have no crystal structure of plant PSII. We have redesigned the purification and crystallization procedures and recently solved the crystal structure of the PSI supercomplex at 3.3 Å resolution. Even though this advance in resolution appears to be relatively small, we obtained a significantly improved model of the supercomplex. The work was published in J. Biol. Chem. (Amunts et al., 2010). The improved electron density map yielded identification and tracing of the PsaK subunit. The location of an additional 10 ß-carotenes, as well as 5 chlorophylls and several loop regions that were previously uninterruptable have been modeled. This represents the most complete plant PSI structure obtained thus far, revealing the locations of and interactions among 17 protein subunits and 193 non-covalently bound photochemical cofactors. We have continued extensive experimental efforts to improve the structure of plant PSI and to obtain PSII preparation amenable to crystallization. Most of our efforts were devoted to obtain well-defined subcomplexes of plant PSII preparations that are amenable to crystallization. We studied the apparent paradox of the high sensitivity of oxygen evolution of isolated thylakoids while BBY particles exhibit remarkable resilience to the same treatment. The integrity of the photosystem II (PSII) extrinsic protein complement as well as calcium effects arise from the Ca2+ atom associated with the site of photosynthetic water oxidation were investigated. This work provides deeper insights into the interaction of PsbO with PSII. Sight-directed mutagenesis indicated the location of critical sites involved in the stability of the water oxidation reaction. When combined with previous results, the data lead to a more detailed model for PsbO binding in eukaryotic PSII.
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2

Fromm, A., Avihai Danon, and Jian-Kang Zhu. Genes Controlling Calcium-Enhanced Tolerance to Salinity in Plants. United States Department of Agriculture, March 2003. http://dx.doi.org/10.32747/2003.7585201.bard.

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The specific objectives of the proposed research were to identify, clone and characterize downstream cellular target(s) of SOS3 in Arabidopsis thaliana, to analyze the Ca2+-binding characteristics of SOS3 and the sos3-1 mutant and their interactions with SOS3 cellular targets to analyze the SOS3 cell-specific expression patterns, and its subcellular localization, and to assess the in vivo role of SOS3 target protein(s) in plant tolerance to salinity stress. In the course of the study, in view of recent opportunities in identifying Ca2+ - responsive genes using microarrays, the group at Weizmann has moved into identifying Ca2+-responsive stress genes by using a combination of aqeuorin-based measurements of cytosolic Ca and analysis by DNA microarrays of early Ca-responsive genes at the whole genome level. Analysis of SOS3 (University of Arizona) revealed its expression in both roots and shoots. However, the expression of this gene is not induced by stress. This is reminiscent of other stress proteins that are regulated by post-transcriptional mechanisms such as the activation by second messengers like Ca. Further analysis of the expression of the gene using promoter - GUS fusions revealed expression in lateral root primordial. Studies at the Weizmann Institute identified a large number of genes whose expression is up-regulated by a specific cytosolic Ca burst evoked by CaM antagonists. Fewer genes were found to be down-regulated by the Ca burst. Among the up-regulated genes many are associated with early stress responses. Moreover, this study revealed a large number of newly identified Ca-responsive genes. These genes could be useful to investigate yet unknown Ca-responsive gene networks involved in plant response to stress.
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3

Wicker, Louise, Ilan Shomer, and Uzi Merin. Membrane Processing of Citrus Extracts: Effects on Pectinesterase Activity and Cloud Stability. United States Department of Agriculture, October 1993. http://dx.doi.org/10.32747/1993.7568754.bard.

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The U.S. team studied the role of cations and pH on thermolabile (TL-PE) and thermostable (TS-PE), permeation in ultrafiltration (UF) membranes, affinity to ion exchange membranes, mechanism of cation and pH activation, and effect on PE stability. An optimum pH and cation concentration exists for activity and UF permeation, which is specific for each cation type. Incomplete release of PE from a pectin complex resulted in low PE binding to cationic and anionic membranes. Incubation of PE at low pH increases the surface hydrophobicity, especially TL-PE, but the secondary structure of TL-PE is not greatly affected. The Israeli team showed that stable cloud colloidal constituents flocculate following the conversion of soluble to insoluble biopolymers. First, formation of pectic acid by pectinesterase activity is followed by the formation of calcium pectate gel. This process initiates a myriad of poorly defined reactions that result in juice clarification. Second, protein coagulation by heat resulted in flocculation of proteinacous bound cloud constituents, particularly after enzymatic pectin degradation. Pectinesterase activity is proposed to be an indirect cause for clarification; whereas binding of cloud constituents is the primary event in clarification by pectate gel and coagulated proteins. Understanding the mechanism of interaction of protein and pectic polymers is key to understanding cloud instability. Based on the above, it was hypothesized that the structure of pectin-protein coagulates plays a key role in cloud instability.
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4

Rafaeli, Ada, Russell Jurenka, and Daniel Segal. Isolation, Purification and Sequence Determination of Pheromonotropic-Receptors. United States Department of Agriculture, July 2003. http://dx.doi.org/10.32747/2003.7695850.bard.

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Moths constitute a major group of pest insects in agriculture. Pheromone blends are utilised by a variety of moth species to attract conspecific mates, which is under circadian control by the neurohormone, PBAN (pheromone-biosynthesis-activating neuropeptide). Our working hypothesis was that, since the emission of sex-pheromone is necessary to attract a mate, then failure to produce and emit pheromone is a potential strategy for manipulating adult moth behavior. The project aimed at identifying, characterising and determining the sequence of specific receptors responsible for the interaction with pheromonotropic neuropeptide/s using two related moth species: Helicoverpa armigera and H. lea as model insects. We established specific binding to a membrane protein estimated at 50 kDa in mature adult females using a photoaffinity-biotin probe for PBAN. We showed that JH is required for the up-regulation of this putative receptor protein. In vitro studies established that the binding initiates a cascade of second messengers including channel opening for calcium ions and intracellular cAMP production. Pharmacological studies (using sodium fluoride) established that the receptor is coupled to a G-protein, that is, the pheromone-biosynthesis-activating neuropeptide receptor (PBAN-R) belongs to the family of G protein-coupled receptor (GPCR)'s. We showed that PBAN-like peptides are present in Drosophila melanogaster based on bioassay and immunocytochemical data. Using the annotated genome of D. melanogaster to search for a GPCR, we found that some were similar to neuromedin U- receptors of vertebrates, which contain a similar C-terminal ending as PBAN. We established that neuromedin U does indeed induce pheromone biosynthesis and cAMP production. Using a PCR based cloning strategy and mRNA isolated from pheromone glands of H. zea, we successfully identified a gene encoding a GPCR from pheromone glands. The full-length PBAN-R was subsequently cloned and expressed in Sf9 insect cells and was shown to mobilize calcium in response to PBAN in a dose-dependent manner. The successful progress in the identification of a gene, encoding a GPCR for the neurohormone, PBAN, provides a basis for the design of a novel battery of compounds that will specifically antagonize pheromone production. Furthermore, since PBAN belongs to a family of insect neuropeptides with more than one function in different life stages, this rationale may be extended to other physiological key-regulatory processes in different insects.
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5

Locy, Robert D., Hillel Fromm, Joe H. Cherry, and Narendra K. Singh. Regulation of Arabidopsis Glutamate Decarboxylase in Response to Heat Stress: Modulation of Enzyme Activity and Gene Expression. United States Department of Agriculture, January 2001. http://dx.doi.org/10.32747/2001.7575288.bard.

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Анотація:
Most plants accumulate the nonprotein amino acid, g-aminobutyric acid (GABA), in response to heat stress. GABA is made from glutamate in a reaction catalyzed by glutamate decarboxylase (GAD), an enzyme that has been shown by the Israeli PI to be a calmodulin (CaM) binding protein whose activity is regulated in vitro by calcium and CaM. In Arabidopsis there are at least 5 GAD genes, two isoforms of GAD, GAD1 and GAD2, are known to be expressed, both of which appear to be calmodulin-binding proteins. The role of GABA accumulation in stress tolerance remains unclear, and thus the objectives of the proposed work are intended to clarify the possible roles of GABA in stress tolerance by studying the factors which regulate the activity of GAD in vivo. Our intent was to demonstrate the factors that mediate the expression of GAD activity by analyzing the promoters of the GAD1 and GAD2 genes, to determine the role of stress induced calcium signaling in the regulation of GAD activity, to investigate the role of phosphorylation of the CaM-binding domain in the regulation of GAD activity, and to investigate whether ABA signaling could be involved in GAD regulation via the following set of original Project Objectives: 1. Construction of chimeric GAD1 and GAD2 promoter/reporter gene fusions and their utilization for determining cell-specific expression of GAD genes in Arabidopsis. 2. Utilizing transgenic plants harboring chimeric GAD1 promoter-luciferase constructs for isolating mutants in genes controlling GAD1 gene activation in response to heat shock. 3. Assess the role of Ca2+/CaM in the regulation of GAD activity in vivo in Arabidopsis. 4. Study the possible phosphorylation of GAD as a means of regulation of GAD activity. 5. Utilize ABA mutants of Arabidopsis to assess the involvement of this phytohormone in GAD activation by stress stimuli. The major conclusions of Objective 1 was that GAD1 was strongly expressed in the elongating region of the root, while GAD2 was mainly expressed along the phloem in both roots and shoots. In addition, GAD activity was found not to be transcriptionally regulated in response to heat stress. Subsequently, The Israeli side obtained a GAD1 knockout mutation, and in light of the objective 1 results it was determined that characterization of this knockout mutation would contribute more to the project than the proposed Objective 2. The major conclusion of Objective 3 is that heat-stress-induced changes in GAD activity can be explained by heat-stress-induced changes in cytosolic calcium levels. No evidence that GAD activity was transcriptionally or translationally regulated or that protein phosphorylation was involved in GAD regulation (objective 4) was obtained. Previously published data by others showing that in wheat roots ABA regulated GABA accumulation proved not to be the case in Arabidopsis (Objective 5). Consequently, we put the remaining effort in the project into the selection of mutants related to temperature adaptation and GABA utilization and attempting to characterize events resulting from GABA accumulation. A set of 3 heat sensitive mutants that appear to have GABA related mutations have been isolated and partially characterized, and a study linking GABA accumulation to growth stimulation and altered nitrate assimilation were conducted. By providing a better understanding of how GAD activity was and was not regulated in vivo, we have ruled out the use of certain genes for genetically engineering thermotolerance, and suggested other areas of endeavor related to the thrust of the project that may be more likely approaches to genetically engineering thermotolerance.
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6

Levy, Maggie, Raymond Zielinski, and Anireddy S. Reddy. IQD1 Function in Defense Responses. United States Department of Agriculture, January 2012. http://dx.doi.org/10.32747/2012.7699842.bard.

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The main objective of the proposed research was to study IQD1's mechanism of action and elucidate its role in plant protection. Preliminary experiments suggest that IQD1 binds CaM in a Ca²⁺-dependent manner and functions in general defense responses. We propose to identify proteins and genes that interact with IQD1, which may provide some clues to its mechanism of action. We also plan to dissect IQD1's integration in defense pathways and to study and modulate its binding affinity to CaM in order to enhance crop resistance. Our specific objectives were: (1) Analysis of IQD1's CaM-binding properties; (2) Identification of IQD1 targets;(3) Dissection of IQD1 integration into defense signaling pathways. Analysis of IQD1's CaM-binding properties defined four potential classes of sequences that should affect CaM binding: one is predicted to raise the affinity for Ca²⁺-dependent interaction but have no effect on Ca²⁺-independent binding; a second is predicted to act like the first mutation but eliminate Ca²⁺-independent binding; a third has no predicted effect on Ca²⁺-dependent binding but eliminates Ca²⁺-independent binding; and the fourth is predicted to eliminate or greatly reduce both Ca²⁺-dependent and Ca²⁺-independent binding. Following yeast two hybrid analysis we found that IQD1 interact with AtSR1 (Arabidopsis thalianaSIGNALRESPONSIVE1), a calcium/calmodulin-binding transcription factor, which has been shown to play an important role in biotic and abiotic stresses. We tested IQD1 interaction with both N-terminal or C-terminal half of SR1. These studies have uncovered that only the N-terminal half of the SR1 interacts with the IQD1. Since IQD1 has an important role in herbivory, its interaction with SR1 suggests that it might also be involved in plant responses to insect herbivory. Since AtSR1, like IQD1, is a calmodulin-binding protein and the mutant showed increased sensitivity to a herbivore, we analyzed WT, Atsr1 and the complemented line for the levels of GS to determine if the increased susceptibility of Atsr1 plants to T. ni feeding is associated with altered GS content. In general, Atsr1 showed a significant reduction in both aliphatic and aromatic GS levels as compared to WT. In order to study IQD1's molecular basis integration into hormone-signaling pathways we tested the epistatic relationships between IQD1 and hormone-signaling mutants. For that purpose we construct double mutants between IQD1ᴼXᴾ and mutants defective in plant-hormone signaling and GS accumulation. Epitasis with SA mutant NahG and npr1-1 and JA mutant jar1-1 suggested IQD1 function is dependent on both JA and SA as indicated by B. cinerea infection assays. We also verified the glucosinolate content in the crosses siblings and found that aliphatic GSL content is reduced in the double transgenic plants NahG:IQD1ᴼXᴾ as compare to parental lines while the aliphatic GSL content in the npr1-1:IQD1ᴼXᴾ and jar1-1: IQD1ᴼXᴾ double mutants was intimidated to the parental lines. This suggests that GSL content dependency on SA is downstream to IQD1. As a whole, this project should contribute to the development of new defense strategies that will improve crop protection and reduce yield losses and the amount of pesticides required; these will genuinely benefit farmers, consumers and the environment.
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7

O'Neill, Sharman, Abraham Halevy, and Amihud Borochov. Molecular Genetic Analysis of Pollination-Induced Senescence in Phalaenopsis Orchids. United States Department of Agriculture, 1991. http://dx.doi.org/10.32747/1991.7612837.bard.

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The project investigated the molecular genetic and biochemical basis of pollination-induced senescence of Phalaenopsis flowers. This experimental system offered unique advantages in that senescence is strictly regulated by pollination, providing the basis to experimentally initiate and synchronize senescence in populations of flowers. The postpollination syndrome in the Phalaenopsis orchid system was dissected by investigating the temporal and spatial regulation of ACC synthase gene expression. In the stigma, pollen-borne auxin induces the expression of the auxin-regulated ACC synthase (PS-ACS2) gene, resulting in ACC synthesis within 1 h following pollination. Newly formed ACC is oxidized by basal constitutive ACC oxidase to ethylene, which then induces the expression of the ethylene-regulated ACC synthase(PS-ACS1) and oxidase (ACO1) genes for further autocatalytic production of ethylene. It is speculated that during the 6-h period following pollination, emasculation leads to the production or release of a sensitivity factor that sensitizes the cells of the stigma to ethylene. ACC and ethylene molecules are translocated from the stigma to the labellum and perianth where ethylene induces the expression of PS-ACS1 and ACO1 resulting in an increased production of ACC and ethylene. Organ-localized ethylene is responsible for inrolling and senescence of the labellum and perianth. The regulation of ethylene sensitivity and signal transduction events in pollinated flowers was also investigated. The increase in ethylene sensitivity appeared in both the flower column and the perianth, and was detected as early as 4 h after pollination. The increase in ethylene sensitivity following pollination was not dependent on endogenous ethylene production. Application of linoleic and linoleic acids to Phalaenopsis and Dendrobium flowers enhanced their senescence and promoted ethylene production. Several major lipoxygenase pathway products including JA-ME, traumatic acid, trans-2-hexenal and cis-3-hexenol, also enhanced flower senescence. However, lipoxygenase appears to not be directly involved in the endogenous regulation of pollination-induced Phalaenopsis and Dendrobium flower senescence. The data suggest that short-chain saturated fatty acids may be the ethylene "sensitivity factors" produced following pollination, and that their mode of action involves a decrease in the order of specific regions i the membrane lipid bilayer, consequently altering ethylene action. Examination of potential signal transduction intermediates indicate a direct involvement of GTP-binding proteins, calcium ions and protein phosphorylation in the cellular signal transduction response to ethylene following pollination. Modulations of cytosolic calcium levels allowed us to modify the flowers responsiveness to ethylene.
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