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Journal articles on the topic 'Biochemistry and Cell Biology N.E.C'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Van Langevelde, Arjen, Kees Van Malssen, René Driessen, Kees Goubitz, Frank Hollander, René Peschar, Peter Zwart, and Henk Schenk. "Structure of C n C n+2C n -type (n = even) β′-triacylglycerols." Acta Crystallographica Section B Structural Science 56, no. 6 (December 1, 2000): 1103–11. http://dx.doi.org/10.1107/s0108768100009927.

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The crystal structures of the β′ phase of CLC (1,3-didecanoyl-2-dodecanoylglycerol) and MPM (1,3-ditetradecanoyl-2-hexadecanoylglycerol) have been determined from single-crystal X-ray diffraction and high-resolution X-ray powder diffraction data, respectively. Both these crystals are orthorhombic with space group Iba2 and Z = 8. The unit-cell parameters of β′-CLC are a = 57.368 (6), b = 22.783 (2) and c = 5.6945 (6) Å and the final R value is 0.175. The unit-cell parameters of β′-MPM are a = 76.21 (4), b = 22.63 (1) and c = 5.673 (2) Å and the final Rp value is 0.057. Both the β′-CLC and β′-MPM molecules are crystallized in a chair conformation, having a bend at the glycerol moiety. The zigzag planes of the acyl chains are orthogonally packed, as is typical for a β′ phase. Furthermore, unit-cell parameters of some other members of the C n C n+2C n -type triacylglycerol series have been refined on their high-resolution X-ray powder diffraction pattern. Finally, the crystal structures are compared with the currently known structures and models of triacylglycerols.

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2

Yang, Ruojing, and James M. Trevillyan. "c-Jun N-terminal kinase pathways in diabetes." International Journal of Biochemistry & Cell Biology 40, no. 12 (January 2008): 2702–6. http://dx.doi.org/10.1016/j.biocel.2008.06.012.

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3

Barth, Holger, Klaus Aktories, Michel R. Popoff, and Bradley G. Stiles. "Binary Bacterial Toxins: Biochemistry, Biology, and Applications of Common Clostridium and Bacillus Proteins." Microbiology and Molecular Biology Reviews 68, no. 3 (September 1, 2004): 373–402. http://dx.doi.org/10.1128/mmbr.68.3.373-402.2004.

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SUMMARY Certain pathogenic species of Bacillus and Clostridium have developed unique methods for intoxicating cells that employ the classic enzymatic “A-B” paradigm for protein toxins. The binary toxins produced by B. anthracis, B. cereus, C. botulinum, C. difficile, C. perfringens, and C. spiroforme consist of components not physically associated in solution that are linked to various diseases in humans, animals, or insects. The “B” components are synthesized as precursors that are subsequently activated by serine-type proteases on the targeted cell surface and/or in solution. Following release of a 20-kDa N-terminal peptide, the activated “B” components form homoheptameric rings that subsequently dock with an “A” component(s) on the cell surface. By following an acidified endosomal route and translocation into the cytosol, “A” molecules disable a cell (and host organism) via disruption of the actin cytoskeleton, increasing intracellular levels of cyclic AMP, or inactivation of signaling pathways linked to mitogen-activated protein kinase kinases. Recently, B. anthracis has gleaned much notoriety as a biowarfare/bioterrorism agent, and of primary interest has been the edema and lethal toxins, their role in anthrax, as well as the development of efficacious vaccines and therapeutics targeting these virulence factors and ultimately B. anthracis. This review comprehensively surveys the literature and discusses the similarities, as well as distinct differences, between each Clostridium and Bacillus binary toxin in terms of their biochemistry, biology, genetics, structure, and applications in science and medicine. The information may foster future studies that aid novel vaccine and drug development, as well as a better understanding of a conserved intoxication process utilized by various gram-positive, spore-forming bacteria.

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4

FORMICKA-KOZLOWSKA, Grazyna, Helga SCHNEIDER-BERNLOHR, Jean-Pierre WARTBURG, and Michael ZEPPEZAUER. "H8Zn(c)2 and Zn(c)2Co(n)2 human liver alcohol dehydrogenase." European Journal of Biochemistry 173, no. 2 (April 1988): 281–85. http://dx.doi.org/10.1111/j.1432-1033.1988.tb13996.x.

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5

Krapp, Anne, Vera Saliba-Colombani, and Françoise Daniel-Vedele. "Analysis of C and N metabolisms and of C/N interactions using quantitative genetics." Photosynthesis Research 83, no. 2 (February 2005): 251–63. http://dx.doi.org/10.1007/s11120-004-3196-7.

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6

May, Gerhard H. W., K. Elizabeth Allen, William Clark, Martin Funk, and David A. F. Gillespie. "Analysis of the Interaction between c-Jun and c-Jun N-terminal Kinasein Vivo." Journal of Biological Chemistry 273, no. 50 (December 11, 1998): 33429–35. http://dx.doi.org/10.1074/jbc.273.50.33429.

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7

Yeap, Yvonne Y. C., Ivan H. W. Ng, Bahareh Badrian, Tuong-Vi Nguyen, Yan Y. Yip, Amardeep S. Dhillon, Steven E. Mutsaers, John Silke, Marie A. Bogoyevitch, and Dominic C. H. Ng. "c-Jun N-terminal kinase/c-Jun inhibits fibroblast proliferation by negatively regulating the levels of stathmin/oncoprotein 18." Biochemical Journal 430, no. 2 (August 13, 2010): 345–54. http://dx.doi.org/10.1042/bj20100425.

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The JNKs (c-Jun N-terminal kinases) are stress-activated serine/threonine kinases that can regulate both cell death and cell proliferation. We have developed a cell system to control JNK re-expression at physiological levels in JNK1/2-null MEFs (murine embryonic fibroblasts). JNK re-expression restored basal and stress-activated phosphorylation of the c-Jun transcription factor and attenuated cellular proliferation with increased cells in G1/S-phase of the cell cycle. To explore JNK actions to regulate cell proliferation, we evaluated a role for the cytosolic protein, STMN (stathmin)/Op18 (oncoprotein 18). STMN, up-regulated in a range of cancer types, plays a crucial role in the control of cell division through its regulation of microtubule dynamics of the mitotic spindle. In JNK1/2-null or c-Jun-null MEFs or cells treated with c-Jun siRNA (small interfering RNA), STMN levels were significantly increased. Furthermore, a requirement for JNK/cJun signalling was demonstrated by expression of wild-type c-Jun, but not a phosphorylation-defective c-Jun mutant, being sufficient to down-regulate STMN. Critically, shRNA (small hairpin RNA)-directed STMN down-regulation in JNK1/2-null MEFs attenuated proliferation. Thus JNK/c-Jun regulation of STMN levels provides a novel pathway in regulation of cell proliferation with important implications for understanding the actions of JNK as a physiological regulator of the cell cycle and tumour suppressor protein.

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8

Mooney, Lorraine M., and Alan J. Whitmarsh. "Docking Interactions in the c-Jun N-terminal Kinase Pathway." Journal of Biological Chemistry 279, no. 12 (December 29, 2003): 11843–52. http://dx.doi.org/10.1074/jbc.m311841200.

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9

Cain, Stuart A., Andrew K. Baldwin, Yashithra Mahalingam, Bertrand Raynal, Thomas A. Jowitt, C. Adrian Shuttleworth, John R. Couchman, and Cay M. Kielty. "Heparan Sulfate Regulates Fibrillin-1 N- and C-terminal Interactions." Journal of Biological Chemistry 283, no. 40 (July 31, 2008): 27017–27. http://dx.doi.org/10.1074/jbc.m803373200.

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10

Bagowski, Christoph P., Wen Xiong, and James E. Ferrell. "c-Jun N-terminal Kinase Activation inXenopus laevisEggs and Embryos." Journal of Biological Chemistry 276, no. 2 (October 11, 2000): 1459–65. http://dx.doi.org/10.1074/jbc.m008050200.

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11

Miller, Gregory J., Stanley D. Dunn, and Eric H. Ball. "Interaction of the N- and C-terminal Domains of Vinculin." Journal of Biological Chemistry 276, no. 15 (December 21, 2000): 11729–34. http://dx.doi.org/10.1074/jbc.m008646200.

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The vinculin head to tail intramolecular self-association controls its binding sites for other components of focal adhesions. To study this interaction, the head and tail domains were expressed, purified, and assayed for various characteristics of complex formation. Analytical centrifugation demonstrated a strong interaction in solution and formation of a complex more asymmetric than either of the individual domains. A survey of binding conditions using a solid-phase binding assay revealed characteristics of both electrostatic and hydrophobic forces involved in the binding. In addition, circular dichroism of the individual domains and the complex demonstrated that conformational changes likely occur in both domains during association. The interaction sites were more closely mapped on the protein sequence by deletion mutagenesis. Amino acids 181–226, a basic region within the acidic head domain, were identified as a binding site for the vinculin tail, and residues 1009–1066 were identified as sufficient for binding the head. Moreover, mutation of an acidic patch in the tail (residues 1013–1015) almost completely eliminated its ability to interact with the head domain further supporting the significance of ionic interactions in the binding. Our data indicate that the interaction between the head and tail domains of vinculin occurs through oppositely charged contact sites and results in conformational changes in both domains.

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12

Brito, R. M., G. A. Krudy, J. C. Negele, J. A. Putkey, and P. R. Rosevear. "Calcium plays distinctive structural roles in the N- and C-terminal domains of cardiac troponin C." Journal of Biological Chemistry 268, no. 28 (October 1993): 20966–73. http://dx.doi.org/10.1016/s0021-9258(19)36880-2.

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13

Laidler, P., and A. Lityńska. "Tumor cell N-glycans in metastasis." Acta Biochimica Polonica 44, no. 2 (June 30, 1997): 343–57. http://dx.doi.org/10.18388/abp.1997_4431.

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Metastasis accounts for most of deaths caused by cancer. The increasing body of evidence suggests that changes in N-glycosylation of tumor cell proteins such as increased branching, increased sialylation, polysialylation, decreased fucosylation, enhanced formation of Lewis X and sialyl Lewis X antigens are among important factors determining metastatic potential of tumor cell. Most of the adhesion proteins, e.g., integrins, members of immunoglobulin superfamily, and cadherins are heavily N-glycosylated. The other proteins involved in adhesion, like galectins and type-C selectins, recognize N-glycans as a part of their specific ligands. In this review we focus on recent reports concerning the contribution of N-glycosylation of tumor cell adhesion molecules and some selected membrane proteins in the tumor invasion and metastasis.

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14

Piotrowski, Markus, Tim Janowitz, and Helmut Kneifel. "Plant C-N Hydrolases and the Identification of a Plant N-Carbamoylputrescine Amidohydrolase Involved in Polyamine Biosynthesis." Journal of Biological Chemistry 278, no. 3 (November 14, 2002): 1708–12. http://dx.doi.org/10.1074/jbc.m205699200.

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15

Dowd, Marla M., John W. Baynes, and Suzanne R. Thorpe. "Synthesis of N,N-dilactitol ethylenediamine: A versatile spacer for attachment of residualizing labels to protein." Analytical Biochemistry 205, no. 2 (September 1992): 369–71. http://dx.doi.org/10.1016/0003-2697(92)90451-c.

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16

Horrobin, D. F. "Interactions between n-3 and n-6 essential fatty acids (EFAs) in the regulation of cardiovascular disorders and inflammation." Prostaglandins, Leukotrienes and Essential Fatty Acids 44, no. 2 (October 1991): 127–31. http://dx.doi.org/10.1016/0952-3278(91)90196-c.

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17

BLUME, Astrid, Wenke WEIDEMANN, Ulrich STELZL, Erich E. WANKER, Lothar LUCKA, Peter DONNER, Werner REUTTER, Rüdiger HORSTKORTE, and Stephan HINDERLICH. "Domain-specific characteristics of the bifunctional key enzyme of sialic acid biosynthesis, UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase." Biochemical Journal 384, no. 3 (December 7, 2004): 599–607. http://dx.doi.org/10.1042/bj20040917.

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UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is a bifunctional enzyme, which initiates and regulates sialic acid biosynthesis. Sialic acids are important compounds of mammalian glycoconjugates, mediating several biological processes, such as cell–cell or cell–matrix interactions. In order to characterize the function of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, a number of deletion mutants were generated, lacking either parts of the N-terminal epimerase or the C-terminal kinase domain. N-terminal deletion of only 39 amino acids results in a complete loss of epimerase activity. Deletions in the C-terminal part result in a reduction or complete loss of kinase activity, depending on the size of the deletion. Deletions at either the N- or the C-terminus also result in a reduction of the other enzyme activity. These results indicate that a separate expression of both domains is possible, but that a strong intramolecular dependency of the two domains has arisen during evolution of the enzyme. N-terminal, as well as C-terminal, mutants tend to form trimers, in addition to the hexameric structure of the native enzyme. These results and yeast two-hybrid experiments show that structures required for dimerization are localized within the kinase domain, and a potential trimerization site is possibly located in a region between the two domains. In conclusion, our results reveal that the activities, as well as the oligomeric structure, of this bifunctional enzyme seem to be organized and regulated in a complex manner.

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18

Wong, Kenneth, Xue-Bin Li, and Nicole Hunchuk. "N-Acetylsphingosine (C-ceramide) Inhibited Neutrophil Superoxide Formation and Calcium Influx." Journal of Biological Chemistry 270, no. 7 (February 17, 1995): 3056–62. http://dx.doi.org/10.1074/jbc.270.7.3056.

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19

Fujita, Yasuyuki, Takuya Sasaki, Koji Fukui, Hirokazu Kotani, Toshihiro Kimura, Yutaka Hata, Thomas C. Südhof, Richard H. Scheller, and Yoshimi Takai. "Phosphorylation of Munc-18/n-Sec1/rbSec1 by Protein Kinase C." Journal of Biological Chemistry 271, no. 13 (March 29, 1996): 7265–68. http://dx.doi.org/10.1074/jbc.271.13.7265.

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20

Wolfman, Janice C., and Alan Wolfman. "Endogenous c-N-Ras Provides a Steady-state Anti-apoptotic Signal." Journal of Biological Chemistry 275, no. 25 (April 20, 2000): 19315–23. http://dx.doi.org/10.1074/jbc.m000250200.

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21

Chong, Huira, and Kun-Liang Guan. "Regulation of Raf through Phosphorylation and N Terminus-C Terminus Interaction." Journal of Biological Chemistry 278, no. 38 (July 14, 2003): 36269–76. http://dx.doi.org/10.1074/jbc.m212803200.

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22

Solanas, Guiomar, Susana Miravet, David Casagolda, Julio Castaño, Imma Raurell, Ana Corrionero, Antonio García de Herreros, and Mireia Duñach. "β-Catenin and Plakoglobin N- and C-tails Determine Ligand Specificity." Journal of Biological Chemistry 279, no. 48 (September 20, 2004): 49849–56. http://dx.doi.org/10.1074/jbc.m408685200.

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23

Tao, Nengbing, Steven J. Wagner, and Douglas M. Lublin. "CD36 Is Palmitoylated on Both N- and C-terminal Cytoplasmic Tails." Journal of Biological Chemistry 271, no. 37 (September 13, 1996): 22315–20. http://dx.doi.org/10.1074/jbc.271.37.22315.

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24

Jones, Emma V., Mark J. Dickman, and Alan J. Whitmarsh. "Regulation of p73-mediated apoptosis by c-Jun N-terminal kinase." Biochemical Journal 405, no. 3 (July 13, 2007): 617–23. http://dx.doi.org/10.1042/bj20061778.

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The JNK (c-Jun N-terminal kinase)/mitogen-activated protein kinase signalling pathway is a major mediator of stress responses in cells, including the response to DNA damage. DNA damage also causes the stabilization and activation of p73, a member of the p53 family of transcription factors. p73, like p53, can mediate apoptosis by up-regulating the expression of pro-apoptotic genes, including Bax (Bcl2-associated X protein) and PUMA (p53 up-regulated modulator of apoptosis). Changes in p73 expression have been linked to tumour progression, particularly in neuroblastomas, whereas in tumours that feature inactivated p53 there is evidence that p73 may mediate the apoptotic response to chemotherapeutic agents. In the present study, we demonstrate a novel link between the JNK signalling pathway and p73. We use pharmacological and genetic approaches to show that JNK is required for p73-mediated apoptosis induced by the DNA damaging agent cisplatin. JNK forms a complex with p73 and phosphorylates it at several serine and threonine residues. The mutation of JNK phosphorylation sites in p73 abrogates cisplatin-induced stabilization of p73 protein, leading to a reduction in p73 transcriptional activity and reduced p73-mediated apoptosis. Our results demonstrate that the JNK pathway is an important regulator of DNA damage-induced apoptosis mediated by p73.

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25

Solanas, Guiomar, Susana Miravet, David Casagolda, Julio Castaño, Imma Raurell, Ana Corrionero, Antonio García de Herreros, and Mireia Duñach. "β-Catenin and plakoglobin N- and C-tails determine ligand specificity." Journal of Biological Chemistry 291, no. 46 (November 11, 2016): 23925–27. http://dx.doi.org/10.1074/jbc.a116.408685.

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26

Campeau, Eric, and Roy A. Gravel. "Expression inEscherichia coliof N- and C-terminally Deleted Human Holocarboxylase Synthetase." Journal of Biological Chemistry 276, no. 15 (December 21, 2000): 12310–16. http://dx.doi.org/10.1074/jbc.m009717200.

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Biotin functions as a covalently bound cofactor of biotindependent carboxylases. Biotin attachment is catalyzed by biotin protein ligases, called holocarboxylase synthetase in mammals and BirA in prokaryotes. These enzymes show a high degree of sequence similarity in their biotinylation domains but differ markedly in the length and sequence of their N terminus. BirA is also the repressor of the biotin operon, and its DNA attachment site is located in its N terminus. The function of the eukaryotic N terminus is unknown. Holocarboxylase synthetase with N- and C-terminal deletions were evaluated for the ability to catalyze biotinylation after expression inEscherichia coliusing bacterial and human acceptor substrates. We showed that the minimum functional protein is comprised of the last 349 of the 726-residue protein, which includes the biotinylation domain. Significantly, enzyme containing intermediate length, N-terminal deletions interfered with biotin transfer and interaction with different peptide acceptor substrates. We propose that the N terminus of holocarboxylase synthetase contributes to biotinylation through N- and C-terminal interactions and may affect acceptor substrate recognition. Our findings provide a rationale for the biotin responsiveness of patients with point mutations in the N-terminal sequence of holocarboxylase synthetase. Such mutant enzyme may respond to biotin-mediated stabilization of the substrate-bound complex.

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27

Xie, Zhi, Wan-Ting Ho, and John H. Exton. "Association of the N- and C-terminal Domains of Phospholipase D." Journal of Biological Chemistry 275, no. 32 (May 23, 2000): 24962–69. http://dx.doi.org/10.1074/jbc.m909745199.

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28

Pan, Min, Hua Yuan, Michael Brent, Emily Chen Ding, and Ronen Marmorstein. "SIRT1 Contains N- and C-terminal Regions That Potentiate Deacetylase Activity." Journal of Biological Chemistry 287, no. 4 (December 7, 2011): 2468–76. http://dx.doi.org/10.1074/jbc.m111.285031.

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29

Papadimitriou, E., M. Heroult, J. Courty, A. Polykratis, C. Stergiou, and P. Katsoris. "Endothelial Cell Proliferation Induced by HARP: Implication of N or C Terminal Peptides." Biochemical and Biophysical Research Communications 274, no. 1 (July 2000): 242–48. http://dx.doi.org/10.1006/bbrc.2000.3126.

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30

MacCorkle-Chosnek, Rebecca A., Aaron VanHooser, David W. Goodrich, B. R. Brinkley, and Tse-Hua Tan. "Cell Cycle Regulation of c-Jun N-Terminal Kinase Activity at the Centrosomes." Biochemical and Biophysical Research Communications 289, no. 1 (November 2001): 173–80. http://dx.doi.org/10.1006/bbrc.2001.5948.

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31

Schwenger, Paul, Deborah Alpert, Edward Y. Skolnik, and Jan Vil?ek. "Cell-type-specific activation of c-Jun N-terminal kinase by salicylates." Journal of Cellular Physiology 179, no. 1 (April 1999): 109–14. http://dx.doi.org/10.1002/(sici)1097-4652(199904)179:1<109::aid-jcp13>3.0.co;2-w.

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32

Kubota, Yoshihisa, Sun Hee Kim, Sanae M. M. Iguchi-Ariga, and Hiroyoshi Ariga. "Transrepression of the N-myc expression by c-myc protein." Biochemical and Biophysical Research Communications 162, no. 3 (August 1989): 991–97. http://dx.doi.org/10.1016/0006-291x(89)90771-7.

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33

Ortega-Pérez, Inmaculada, Eva Cano, Felipe Were, Margarita Villar, Jesús Vázquez, and Juan Miguel Redondo. "c-Jun N-terminal Kinase (JNK) Positively Regulates NFATc2 Transactivation through Phosphorylation within the N-terminal Regulatory Domain." Journal of Biological Chemistry 280, no. 21 (March 2, 2005): 20867–78. http://dx.doi.org/10.1074/jbc.m501898200.

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34

Sun, Wei, Simon Parry, Maria Panico, Howard R. Morris, Margareta Kjellberg, Åke Engström, Anne Dell, and Sophia Schedin-Weiss. "N-Glycans and the N Terminus of Protein C Inhibitor Affect the Cofactor-enhanced Rates of Thrombin Inhibition." Journal of Biological Chemistry 283, no. 27 (May 8, 2008): 18601–11. http://dx.doi.org/10.1074/jbc.m800608200.

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35

Linden, Michael A., Nicole Kirchhof, and Brian G. Van Ness. "Targeted Overexpression of Mutant Activated N-ras Leads to Aberrant Plasma Cell Biology." Blood 104, no. 11 (November 16, 2004): 1416. http://dx.doi.org/10.1182/blood.v104.11.1416.1416.

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Abstract The ras oncogene regulates a variety of cellular functions, and its dysregulation has been implicated in a variety of human cancers, including multiple myeloma. Indeed, activating ras mutations have been described in 35 – 50% of myeloma patients, 50% of human myeloma cell lines, and 12.5% of patients with monoclonal gammopathy of undetermined significance (MGUS). Given the higher incidence of activating ras mutations in myeloma compared to MGUS, the current models of myelomagenesis suggest that activating ras mutations are involved in the progression of MGUS to myeloma. While there has been a fairly extensive analysis of activating ras mutations in myeloma patients, there have been few studies to investigate the biology of an activated ras mutation in the context of B- and plasma cell development and tumorigenesis. We previously described a transgenic platform that uses the 3′ kappa immunoglobulin light chain enhancer (3′KE) to target transgene expression to B-cells in late developmental stages, including plasma cells (Blood103: 2779, 2004). To study the potential influence of elevated mutant ras expression on B- and plasma cell survival and proliferation, we used the 3′KE to generate a 3′KE/N-ras V12 transgenic mouse. We hypothesized that the presence of the mutant ras gene would affect normal B- and plasma cell homeostasis. Indeed, samples of mononuclear splenocytes from 4-week-old transgenic mice demonstrate a 70% increase in the number of B220+kappa+ B-cells and a 250% increase in the number of CD138+B220hi plasmablastic cells compared to littermate controls. While survival of the 3′KE/N-ras V12 mice appears similar to littermate controls and transgenic animals do not develop tumors at 35 weeks of age, aberrant lymphocyte biology was noted in multiple founder lines. All aged 3′KE/N-ras V12 transgenic founders demonstrated an immunoglobulinemia. Interestingly, the animal with the highest transgene copy number had the least pronounced immunoglobulinemia, while the animal with the lowest transgene copy number had the most pronounced immunoglobulinemia, suggesting an inversely dose-dependent relationship between over-expression of an activated Ras protein and immunoglobulinemia. We performed extensive necropsies and histopathological analyses on all founder mice and aged-matched littermate controls. While no tumors were found in any of the mice, three of the founder mice demonstrated abnormal accumulations of plasma cells in extramedullary sites, such as the kidney. These data indicate that an activated ras transgene can affect B- and plasma cell homeostasis, and this transgenic model could prove useful in studying the role of activating ras mutations in plasma cell tumorigenesis. We are currently using three targeted c-myc gene expression systems to elicit B- and/or plasma cell tumors by co-expressing c-myc and N-ras V12.

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36

Marui, Nobuyuki, Toshiyuki Sakai, Nobuko Hosokawa, Mitsunori Yoshida, Akira Aoike, Keiichi Kawai, Hoyoku Nishino, and Masanori Fukushima. "N-myc suppression and cell cycle arrest at G1 phase by prostaglandins." FEBS Letters 270, no. 1-2 (September 17, 1990): 15–18. http://dx.doi.org/10.1016/0014-5793(90)81224-c.

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37

Noguchi, Kohji, Chifumi Kitanaka, Hironobu Yamana, Akiko Kokubu, Toshihiro Mochizuki, and Yoshiyuki Kuchino. "Regulation of c-Myc through Phosphorylation at Ser-62 and Ser-71 by c-Jun N-Terminal Kinase." Journal of Biological Chemistry 274, no. 46 (November 12, 1999): 32580–87. http://dx.doi.org/10.1074/jbc.274.46.32580.

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38

Chen, Yi-Rong, Xiaoping Wang, Dennis Templeton, Roger J. Davis, and Tse-Hua Tan. "The Role of c-Jun N-terminal Kinase (JNK) in Apoptosis Induced by Ultraviolet C and γ Radiation." Journal of Biological Chemistry 271, no. 50 (December 13, 1996): 31929–36. http://dx.doi.org/10.1074/jbc.271.50.31929.

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39

Hamilton, Mark, Jinhui Liao, Martha K. Cathcart, and Alan Wolfman. "Constitutive Association of c-N-Ras with c-Raf-1 and Protein Kinase Cε in Latent Signaling Modules." Journal of Biological Chemistry 276, no. 31 (May 17, 2001): 29079–90. http://dx.doi.org/10.1074/jbc.m102001200.

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40

Maaty, Walid S., Connie I. Lord, Jeannie M. Gripentrog, Marcia Riesselman, Gal Keren-Aviram, Ting Liu, Edward A. Dratz, Brian Bothner, and Algirdas J. Jesaitis. "Identification of C-terminal Phosphorylation Sites of N-Formyl Peptide Receptor-1 (FPR1) in Human Blood Neutrophils." Journal of Biological Chemistry 288, no. 38 (July 19, 2013): 27042–58. http://dx.doi.org/10.1074/jbc.m113.484113.

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Accumulation, activation, and control of neutrophils at inflammation sites is partly driven by N-formyl peptide chemoattractant receptors (FPRs). Occupancy of these G-protein-coupled receptors by formyl peptides has been shown to induce regulatory phosphorylation of cytoplasmic serine/threonine amino acid residues in heterologously expressed recombinant receptors, but the biochemistry of these modifications in primary human neutrophils remains relatively unstudied. FPR1 and FPR2 were partially immunopurified using antibodies that recognize both receptors (NFPRa) or unphosphorylated FPR1 (NFPRb) in dodecylmaltoside extracts of unstimulated and N-formyl-Met-Leu-Phe (fMLF) + cytochalasin B-stimulated neutrophils or their membrane fractions. After deglycosylation and separation by SDS-PAGE, excised Coomassie Blue-staining bands (∼34,000 Mr) were tryptically digested, and FPR1, phospho-FPR1, and FPR2 content was confirmed by peptide mass spectrometry. C-terminal FPR1 peptides (Leu312–Arg322 and Arg323–Lys350) and extracellular FPR1 peptide (Ile191–Arg201) as well as three similarly placed FPR2 peptides were identified in unstimulated and fMLF + cytochalasin B-stimulated samples. LC/MS/MS identified seven isoforms of Ala323–Lys350only in the fMLF + cytochalasin B-stimulated sample. These were individually phosphorylated at Thr325, Ser328, Thr329, Thr331, Ser332, Thr334, and Thr339. No phospho-FPR2 peptides were detected. Cytochalasin B treatment of neutrophils decreased the sensitivity of fMLF-dependent NFPRb recognition 2-fold, from EC50 = 33 ± 8 to 74 ± 21 nm. Our results suggest that 1) partial immunopurification, deglycosylation, and SDS-PAGE separation of FPRs is sufficient to identify C-terminal FPR1 Ser/Thr phosphorylations by LC/MS/MS; 2) kinases/phosphatases activated in fMLF/cytochalasin B-stimulated neutrophils produce multiple C-terminal tail FPR1 Ser/Thr phosphorylations but have little effect on corresponding FPR2 sites; and 3) the extent of FPR1 phosphorylation can be monitored with C-terminal tail FPR1-phosphospecific antibodies.

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41

Gillbro, Tomas, Andrei V. Sharkov, Igor V. Kryukov, Eugeny V. Khoroshilov, Piotr G. Kryukov, Richard Fischer, and Hugo Scheer. "Förster energy transfer between neighbouring chromophores in C-phycocyanin trimers." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1140, no. 3 (January 1993): 321–26. http://dx.doi.org/10.1016/0005-2728(93)90072-n.

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42

Nieuwesteeg, M. A., L. A. Walsh, M. A. Fox, and S. Damjanovski. "Domain specific overexpression of TIMP-2 and TIMP-3 reveals MMP-independent functions of TIMPs during Xenopus laevis development." Biochemistry and Cell Biology 90, no. 4 (August 2012): 585–95. http://dx.doi.org/10.1139/o2012-014.

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Extracellular matrix remodelling mediates many processes including cell migration and differentiation and is regulated through the enzymatic action of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). TIMPs are secreted proteins, consisting of structurally and functionally distinct N- and C-terminal domains. TIMP N-terminal domains inhibit MMP activity, whereas their C-terminal domains may have cell signalling activity. The in vivo role of TIMP N- and C-terminal domains in regulating developmental events has not previously been demonstrated. Here we investigated the roles of TIMP-2 and TIMP-3 N- and C-terminal domains in Xenopus laevis embryos. We show that overexpression of TIMP-2 N- and C-terminal domains results in severe developmental defects and death, as well as unique changes in MMP-2 and -9 expression, indicating that the individual domains may regulate MMPs through distinct mechanisms. In contrast, we show that only the N-terminal, but not the C-terminal domain of TIMP-3, results in developmental defects.

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Volkmann, Gerrit, and Xiang-Qin Liu. "Intein lacking conserved C-terminal motif G retains controllable N-cleavage activity." FEBS Journal 278, no. 18 (August 31, 2011): 3431–46. http://dx.doi.org/10.1111/j.1742-4658.2011.08266.x.

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SCHWALLER, Marc-Antoine, Jean AUBARD, Christian AUCLAIR, Claude PAOLETTI, and Guy DODIN. "The G . C base-pair preference of 2-N-methyl 9-hydroxyellipticinium." European Journal of Biochemistry 181, no. 1 (April 1989): 129–34. http://dx.doi.org/10.1111/j.1432-1033.1989.tb14703.x.

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Kaneko, Hiroshi, Eri Kobayashi, Masayuki Yamamoto, and Ritsuko Shimizu. "N- and C-terminal Transactivation Domains of GATA1 Protein Coordinate Hematopoietic Program." Journal of Biological Chemistry 287, no. 25 (May 2, 2012): 21439–49. http://dx.doi.org/10.1074/jbc.m112.370437.

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46

Hendricks, Gabriel L., Kim L. Weirich, Karthik Viswanathan, Jing Li, Zachary H. Shriver, Joseph Ashour, Hidde L. Ploegh, et al. "Sialylneolacto-N-tetraose c (LSTc)-bearing Liposomal Decoys Capture Influenza A Virus." Journal of Biological Chemistry 288, no. 12 (January 28, 2013): 8061–73. http://dx.doi.org/10.1074/jbc.m112.437202.

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47

Xu, You Cheng, Ru Feng Wu, Ying Gu, Yih-Sheng Yang, Meng-Chun Yang, Fiemu E. Nwariaku, and Lance S. Terada. "Involvement of TRAF4 in Oxidative Activation of c-Jun N-terminal Kinase." Journal of Biological Chemistry 277, no. 31 (May 22, 2002): 28051–57. http://dx.doi.org/10.1074/jbc.m202665200.

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48

Perrella, Frank W. "Characterization of phosphatidylinositol phospholipase C activity in human melanoma." Biochemical and Biophysical Research Communications 166, no. 2 (January 1990): 715–22. http://dx.doi.org/10.1016/0006-291x(90)90868-n.

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Zhang, Mengkun, Caroline Miller, Yulan He, Johanne Martel-Pelletier, Jean-Pierre Pelletier, and John A. Di Battista. "Calphostin C induces AP1 synthesis and AP1-dependent c-jun transactivation in normal human chondrocytes independent of protein kinase c-? inhibition: Possible role for c-jun N-terminal kinase." Journal of Cellular Biochemistry 76, no. 2 (February 1, 2000): 290–302. http://dx.doi.org/10.1002/(sici)1097-4644(20000201)76:2<290::aid-jcb12>3.0.co;2-v.

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Dang, C. V., and W. M. Lee. "Nuclear and nucleolar targeting sequences of c-erb-A, c-myb, N-myc, p53, HSP70, and HIV tat proteins." Journal of Biological Chemistry 264, no. 30 (October 1989): 18019–23. http://dx.doi.org/10.1016/s0021-9258(19)84673-2.

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