Papers associated with LOC100887844 (and LOC576642)

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	Major yolk protein and HSC70 are essential for the activation of the TLR pathway via interacting with MyD88 in Apostichopus japonicus., Lv Z, Li C, Guo M, Shao Y, Zhang W, Zhao X., Arch Biochem Biophys. April 15, 2019; 665 57-68.
	The solute carrier SLC9C1 is a Na+/H+-exchanger gated by an S4-type voltage-sensor and cyclic-nucleotide binding., Windler F, Bönigk W, Körschen HG, Grahn E, Strünker T, Seifert R, Kaupp UB., Nat Commun. July 18, 2018; 9 (1): 2809.
	HSP70 from the Antarctic sea urchin Sterechinus neumayeri: molecular characterization and expression in response to heat stress., González-Aravena M, Calfio C, Mercado L, Morales-Lange B, Bethke J, De Lorgeril J, Cárdenas CA., Biol Res. March 27, 2018; 51 (1): 8.
	Network model predicts that CatSper is the main Ca2+ channel in the regulation of sea urchin sperm motility., Espinal-Enríquez J, Priego-Espinosa DA, Darszon A, Beltrán C, Martínez-Mekler G., Sci Rep. June 26, 2017; 7 (1): 4236.
	Speract, a sea urchin egg peptide that regulates sperm motility, also stimulates sperm mitochondrial metabolism., García-Rincón J, Darszon A, Beltrán C., Biochim Biophys Acta. April 1, 2016; 1857 (4): 415-26.
	FRET analysis using sperm-activating peptides tagged with fluorescent proteins reveals that ligand-binding sites exist as clusters., Arcos-Hernández C, Romero F, Sánchez-Guevara Y, Beltrán C, Nishigaki T., J Exp Biol. February 1, 2016; 219 (Pt 4): 508-15.
	Single cell imaging reveals that the motility regulator speract induces a flagellar alkalinization that precedes and is independent of Ca²⁺ influx in sea urchin spermatozoa., González-Cota AL, Silva PÂ, Carneiro J, Darszon A., FEBS Lett. July 22, 2015; 589 (16): 2146-54.
	De novo assembly of the transcriptome of Acanthaster planci testes., Stewart MJ, Stewart P, Rivera-Posada J., Mol Ecol Resour. July 1, 2015; 15 (4): 953-66.
	Evolution of gamete attraction molecules: evidence for purifying selection in speract and its receptor, in the pantropical sea urchin Diadema., Jagadeeshan S, Coppard SE, Lessios HA., Evol Dev. January 1, 2015; 17 (1): 92-108.
	Zn(2+) induces hyperpolarization by activation of a K(+) channel and increases intracellular Ca(2+) and pH in sea urchin spermatozoa., Beltrán C, Rodríguez-Miranda E, Granados-González G, de De la Torre LG, Nishigaki T, Darszon A., Dev Biol. October 1, 2014; 394 (1): 15-23.
	In silico determination of the effect of multi-target drugs on calcium dynamics signaling network underlying sea urchin spermatozoa motility., Espinal-Enríquez J, Darszon A, Guerrero A, Martínez-Mekler G., PLoS One. August 27, 2014; 9 (8): e104451.
	Manganese overload affects p38 MAPK phosphorylation and metalloproteinase activity during sea urchin embryonic development., Pinsino A, Roccheri MC, Matranga V., Mar Environ Res. February 1, 2014; 93 64-9.
	Certain Strongylocentrotus purpuratus sperm mitochondrial proteins co-purify with low density detergent-insoluble membranes and are PKA or PKC-substrates possibly involved in sperm motility regulation., Loza-Huerta A, Vera-Estrella R, Darszon A, Beltrán C., Biochim Biophys Acta. November 1, 2013; 1830 (11): 5305-15.
	Molecular characterization and expression analysis of heat shock cognate 70 after heat stress and lipopolysaccharide challenge in sea cucumber (Apostichopus japonicus)., Wang X, Zhou Z, Yang A, Dong Y, Chen Z, Guan X, Jiang B, Wang B., Biochem Genet. June 1, 2013; 51 (5-6): 443-57.
	Niflumic acid disrupts marine spermatozoan chemotaxis without impairing the spatiotemporal detection of chemoattractant gradients., Guerrero A, Espinal J, Wood CD, Rendón JM, Carneiro J, Martínez-Mekler G, Darszon A., J Cell Sci. March 15, 2013; 126 (Pt 6): 1477-87.
	What is the core oscillator in the speract-activated pathway of the Strongylocentrotus purpuratus sperm flagellum?, Aguilera LU, Galindo BE, Sánchez D, Santillán M., Biophys J. June 6, 2012; 102 (11): 2481-8.
	Long-term environmental exposure to metals (Cu, Cd, Pb, Zn) activates the immune cell stress response in the common European sea star (Asterias rubens)., Matranga V, Pinsino A, Randazzo D, Giallongo A, Dubois P., Mar Environ Res. May 1, 2012; 76 122-7.
	Toxicity of metal oxide nanoparticles in immune cells of the sea urchin., Falugi C, Aluigi MG, Chiantore MC, Privitera D, Ramoino P, Gatti MA, Fabrizi A, Pinsino A, Matranga V., Mar Environ Res. May 1, 2012; 76 114-21.
	Rapid changes in heat-shock cognate 70 levels, heat-shock cognate phosphorylation state, heat-shock transcription factor, and metal transcription factor activity levels in response to heavy metal exposure during sea urchin embryonic development., Pinsino A, Turturici G, Sconzo G, Geraci F., Ecotoxicology. January 1, 2011; 20 (1): 246-54.
	Discrete dynamics model for the speract-activated Ca2+ signaling network relevant to sperm motility., Espinal J, Aldana M, Guerrero A, Wood C, Darszon A, Martínez-Mekler G., PLoS One. January 1, 2011; 6 (8): e22619.
	Calmodulin antagonists inhibit sea urchin sperm hyperpolarization necessary for directed movement toward the egg., Galindo BE, Darszon A., Proc West Pharmacol Soc. January 1, 2011; 54 80-2.
	Tuning sperm chemotaxis by calcium burst timing., Guerrero A, Nishigaki T, Carneiro J, Yoshiro Tatsu, Wood CD, Darszon A., Dev Biol. August 1, 2010; 344 (1): 52-65.
	Sea urchin embryos as an in vivo model for the assessment of manganese toxicity: developmental and stress response effects., Pinsino A, Matranga V, Trinchella F, Roccheri MC., Ecotoxicology. March 1, 2010; 19 (3): 555-62.
	Sea urchin coelomocytes as a novel cellular biosensor of environmental stress: a field study in the Tremiti Island Marine Protected Area, Southern Adriatic Sea, Italy., Pinsino A, Della Torre C, Sammarini V, Bonaventura R, Amato E, Matranga V., Cell Biol Toxicol. December 1, 2008; 24 (6): 541-52.
	Sperm-activating peptides in the regulation of ion fluxes, signal transduction and motility., Darszon A, Guerrero A, Galindo BE, Nishigaki T, Wood CD., Int J Dev Biol. January 1, 2008; 52 (5-6): 595-606.
	Altering the speract-induced ion permeability changes that generate flagellar Ca2+ spikes regulates their kinetics and sea urchin sperm motility., Wood CD, Nishigaki T, Tatsu Y, Yumoto N, Baba SA, Whitaker M, Darszon A., Dev Biol. June 15, 2007; 306 (2): 525-37.
	Extracellular heat shock protein 70 has novel functional effects on sea urchin eggs and coelomocytes., Browne CL, Swan JB, Rankin EE, Calvert H, Griffiths S, Tytell M., J Exp Biol. April 1, 2007; 210 (Pt 7): 1275-87.
	Ion channels in sperm motility and capacitation., Darszon A, Treviño CL, Wood C, Galindo B, Rodríguez-Miranda E, Acevedo JJ, Hernandez-González EO, Beltrán C, Martínez-López P, Nishigaki T., Soc Reprod Fertil Suppl. January 1, 2007; 65 229-44.
	Proteins associated with soluble adenylyl cyclase in sea urchin sperm flagella., Nomura M, Vacquier VD., Cell Motil Cytoskeleton. September 1, 2006; 63 (9): 582-90.
	Sperm-activating peptide induces asymmetric flagellar bending in sea urchin sperm., Shiba K, Ohmuro J, Mogami Y, Nishigaki T, Wood CD, Darszon A, Tatsu Y, Yumoto N, Baba SA., Zoolog Sci. March 1, 2005; 22 (3): 293-9.
	A major flagellum sialoglycoprotein in sea urchin sperm contains a novel polysialic acid, an alpha2,9-linked poly-N-acetylneuraminic acid chain, capped by an 8-O-sulfated sialic acid residue., Miyata S, Sato C, Kitamura S, Toriyama M, Kitajima K., Glycobiology. September 1, 2004; 14 (9): 827-40.
	A sea urchin egg jelly peptide induces a cGMP-mediated decrease in sperm intracellular Ca(2+) before its increase., Nishigaki T, Wood CD, Tatsu Y, Yumoto N, Furuta T, Elias D, Shiba K, Baba SA, Darszon A., Dev Biol. August 15, 2004; 272 (2): 376-88.
	Revisiting the role of H+ in chemotactic signaling of sperm., Solzin J, Helbig A, Van Q, Brown JE, Hildebrand E, Weyand I, Kaupp UB., J Gen Physiol. August 1, 2004; 124 (2): 115-24.
	Speract induces calcium oscillations in the sperm tail., Wood CD, Darszon A, Whitaker M., J Cell Biol. April 14, 2003; 161 (1): 89-101.
	Intracellular sodium changes during the speract response and the acrosome reaction in sea urchin sperm., Rodríguez E, Darszon A., J Physiol. January 1, 2003; 546 (Pt 1): 89-100.
	Egg fucose sulfate polymer, sialoglycan, and speract all trigger the sea urchin sperm acrosome reaction., Hirohashi N, Vacquier VD., Biochem Biophys Res Commun. August 30, 2002; 296 (4): 833-9.
	Fertilization of sea urchin eggs and sperm motility are negatively impacted under low hypergravitational forces significant to space flight., Tash JS, Kim S, Schuber M, Seibt D, Kinsey WH., Biol Reprod. October 1, 2001; 65 (4): 1224-31.
	The aglycone of sulfogalactolipids can alter the sulfate ester substitution position required for hsc70 recognition., Mamelak D, Mylvaganam M, Tanahashi E, Ito H, Ishida H, Kiso M, Lingwood C., Carbohydr Res. September 28, 2001; 335 (2): 91-100.
	Sea urchin sperm cation-selective channels directly modulated by cAMP., Sánchez D, Labarca P, Darszon A., FEBS Lett. August 10, 2001; 503 (1): 111-5.
	Time-resolved sperm responses to an egg peptide measured by stopped-flow fluorometry., Nishigaki T, Zamudio FZ, Possani LD, Darszon A., Biochem Biophys Res Commun. June 8, 2001; 284 (2): 531-5.
	Real-time measurements of the interactions between fluorescent speract and its sperm receptor., Nishigaki T, Darszon A., Dev Biol. July 1, 2000; 223 (1): 17-26.
	Participation of a K(+) channel modulated directly by cGMP in the speract-induced signaling cascade of strongylocentrotus purpuratus sea urchin sperm., Galindo BE, Beltrán C, Cragoe EJ, Darszon A., Dev Biol. May 15, 2000; 221 (2): 285-94.
	Speract-receptor interaction and the modulation of ion transport in Strongylocentrotus purpuratus sea urchin sperm., Galindo BE, Nishigaki T, Rodríguez E, Sánchez D, Beltrán C, Darszon A., Zygote. January 1, 2000; 8 Suppl 1 S20-1.
	Co-localization of receptor and transducer proteins in the glycosphingolipid-enriched, low density, detergent-insoluble membrane fraction of sea urchin sperm., Ohta K, Sato C, Matsuda T, Toriyama M, Vacquier VD, Lennarz WJ, Kitajima K., Glycoconj J. January 1, 2000; 17 (3 -4): 205-14.
	Microgravity alters protein phosphorylation changes during initiation of sea urchin sperm motility., Tash JS, Bracho GE., FASEB J. January 1, 1999; 13 Suppl S43-54.
	A novel member of an ancient superfamily: sponge (Geodia cydonium, Porifera) putative protein that features scavenger receptor cysteine-rich repeats., Pancer Z, Munkner J, Muller I, Muller WE., Gene. July 9, 1997; 193 (2): 211-8.
	Membrane potential regulates sea urchin sperm adenylylcyclase., Beltrán C, Zapata O, Darszon A., Biochemistry. June 11, 1996; 35 (23): 7591-8.
	Speract receptors are localized on sea urchin sperm flagella using a fluorescent peptide analog., Cardullo RA, Herrick SB, Peterson MJ, Dangott LJ., Dev Biol. April 1, 1994; 162 (2): 600-7.
	Ionic bases of the membrane potential and intracellular pH changes induced by speract in swollen sea urchin sperm., Reynaud E, De de La Torre L, Zapata O, Liévano A, Darszon A., FEBS Lett. August 23, 1993; 329 (1-2): 210-4.
	The lymphocyte glycoprotein CD6 contains a repeated domain structure characteristic of a new family of cell surface and secreted proteins., Aruffo A, Melnick MB, Linsley PS, Seed B., J Exp Med. October 1, 1991; 174 (4): 949-52.

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