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Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

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TRDN

Introduction

Triadin, also known as TRDN, is a human gene.[1]

References

References

  1. ↑ “Entrez Gene: TRDN triadin”.
Further reading

Further reading

  • Taske NL, Eyre HJ, O’Brien RO; et al. (1995). “Molecular cloning of the cDNA encoding human skeletal muscle triadin and its localisation to chromosome 6q22-6q23”. Eur. J. Biochem. 233 (1): 258–65. PMID 7588753.
  • Guo W, Campbell KP (1995). “Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum”. J. Biol. Chem. 270 (16): 9027–30. PMID 7721813.
  • Zhang L, Kelley J, Schmeisser G; et al. (1997). “Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane”. J. Biol. Chem. 272 (37): 23389–97. PMID 9287354.
  • Caswell AH, Motoike HK, Fan H, Brandt NR (1999). “Location of ryanodine receptor binding site on skeletal muscle triadin”. Biochemistry. 38 (1): 90–7. doi:10.1021/bi981306+. PMID 9890886.
  • Groh S, Marty I, Ottolia M; et al. (1999). “Functional interaction of the cytoplasmic domain of triadin with the skeletal ryanodine receptor”. J. Biol. Chem. 274 (18): 12278–83. PMID 10212196.
  • Sacchetto R, Turcato F, Damiani E, Margreth A (1999). “Interaction of triadin with histidine-rich Ca(2+)-binding protein at the triadic junction in skeletal muscle fibers”. J. Muscle Res. Cell. Motil. 20 (4): 403–15. PMID 10531621.
  • Kobayashi YM, Alseikhan BA, Jones LR (2000). “Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction”. J. Biol. Chem. 275 (23): 17639–46. doi:10.1074/jbc.M002091200. PMID 10748065.
  • Kirchhefer U, Neumann J, Baba HA; et al. (2001). “Cardiac hypertrophy and impaired relaxation in transgenic mice overexpressing triadin 1”. J. Biol. Chem. 276 (6): 4142–9. doi:10.1074/jbc.M006443200. PMID 11069905.
  • Shin DW, Ma J, Kim DH (2001). “The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca(2+) and interacts with triadin”. FEBS Lett. 486 (2): 178–82. PMID 11113462.
  • Lee HG, Kang H, Kim DH, Park WJ (2001). “Interaction of HRC (histidine-rich Ca(2+)-binding protein) and triadin in the lumen of sarcoplasmic reticulum”. J. Biol. Chem. 276 (43): 39533–8. doi:10.1074/jbc.M010664200. PMID 11504710.
  • Hong CS, Ji JH, Kim JP; et al. (2002). “Molecular cloning and characterization of mouse cardiac triadin isoforms”. Gene. 278 (1–2): 193–9. PMID 11707337.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Kim E, Shin DW, Hong CS; et al. (2003). “Increased Ca2+ storage capacity in the sarcoplasmic reticulum by overexpression of HRC (histidine-rich Ca2+ binding protein)”. Biochem. Biophys. Res. Commun. 300 (1): 192–6. PMID 12480542.
  • Thevenon D, Smida-Rezgui S, Chevessier F; et al. (2003). “Human skeletal muscle triadin: gene organization and cloning of the major isoform, Trisk 51”. Biochem. Biophys. Res. Commun. 303 (2): 669–75. PMID 12659871.
  • Lee JM, Rho SH, Shin DW; et al. (2004). “Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin”. J. Biol. Chem. 279 (8): 6994–7000. doi:10.1074/jbc.M312446200. PMID 14638677.
  • Olsen JV, Blagoev B, Gnad F; et al. (2006). “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks”. Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
  • Arvanitis DA, Vafiadaki E, Fan GC; et al. (2007). “Histidine-rich Ca-binding protein interacts with sarcoplasmic reticulum Ca-ATPase”. Am. J. Physiol. Heart Circ. Physiol. 293 (3): H1581–9. doi:10.1152/ajpheart.00278.2007. PMID 17526652.

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