메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

Ryanodine receptors are targeted by anti-apoptotic Bcl-XL involving its BH4 domain and Lys87 from its BH3 domain

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; PROTEIN BCL X; PROTEIN BINDING; RYANODINE RECEPTOR;

EID: 84928142792     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep09641     Document Type: Article
Times cited : (32)

References (60)
  • 1
    • 64849113485 scopus 로고    scopus 로고
    • Control of mitochondrial apoptosis by the Bcl-2 family
    • Brunelle, J. K. & Letai, A. Control of mitochondrial apoptosis by the Bcl-2 family. J Cell Sci 122, 437-441 (2009).
    • (2009) J Cell Sci , vol.122 , pp. 437-441
    • Brunelle, J.K.1    Letai, A.2
  • 2
    • 41149152733 scopus 로고    scopus 로고
    • How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?
    • Chipuk, J. E. & Green, D. R. How do BCL-2 proteins induce mitochondrial outer membrane permeabilization? Trends Cell Biol 18, 157-164 (2008).
    • (2008) Trends Cell Biol , vol.18 , pp. 157-164
    • Chipuk, J.E.1    Green, D.R.2
  • 3
    • 11144243134 scopus 로고    scopus 로고
    • 21signaling, which do not depend on their putative pore-forming region
    • 21signaling, which do not depend on their putative pore-forming region. J Biol Chem 279, 54581-54589 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 54581-54589
    • Chami, M.1
  • 4
    • 0036878819 scopus 로고    scopus 로고
    • 21 handling in apoptosis
    • 21 handling in apoptosis. Cell Calcium 32, 413-420 (2002).
    • (2002) Cell Calcium , vol.32 , pp. 413-420
    • Ferrari, D.1
  • 5
    • 84876680098 scopus 로고    scopus 로고
    • The selective BH4-domain biology of Bcl-2-family members: IP3Rs and beyond
    • Monaco, G., Vervliet, T., Akl, H. & Bultynck, G. The selective BH4-domain biology of Bcl-2-family members: IP3Rs and beyond. Cell Mol Life Sci 70, 1171-1183 (2013).
    • (2013) Cell Mol Life Sci , vol.70 , pp. 1171-1183
    • Monaco, G.1    Vervliet, T.2    Akl, H.3    Bultynck, G.4
  • 6
    • 84863316405 scopus 로고    scopus 로고
    • Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein
    • Arbel, N., Ben-Hail, D. & Shoshan-Barmatz, V. Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein. J Biol Chem 287, 23152-23161 (2012).
    • (2012) J Biol Chem , vol.287 , pp. 23152-23161
    • Arbel, N.1    Ben-Hail, D.2    Shoshan-Barmatz, V.3
  • 7
    • 77949881804 scopus 로고    scopus 로고
    • Voltage-dependent anion channel 1-based peptides interact with Bcl-2 to prevent antiapoptotic activity
    • Arbel, N. & Shoshan-Barmatz, V. Voltage-dependent anion channel 1-based peptides interact with Bcl-2 to prevent antiapoptotic activity. J Biol Chem 285, 6053-6062 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 6053-6062
    • Arbel, N.1    Shoshan-Barmatz, V.2
  • 8
    • 84869081493 scopus 로고    scopus 로고
    • Disruption of the VDAC2-Bak interaction by Bcl-xS mediates efficient induction of apoptosis in melanoma cells
    • Plotz, M., Gillissen, B., Hossini, A. M., Daniel, P. T. & Eberle, J. Disruption of the VDAC2-Bak interaction by Bcl-xS mediates efficient induction of apoptosis in melanoma cells. Cell Death Differ 19, 1928-1938 (2012).
    • (2012) Cell Death Differ , vol.19 , pp. 1928-1938
    • Plotz, M.1    Gillissen, B.2    Hossini, A.M.3    Daniel, P.T.4    Eberle, J.5
  • 9
    • 84863727484 scopus 로고    scopus 로고
    • Anovel role for Bcl-2 in regulation of cellular calcium extrusion
    • Ferdek, P. E. et al.Anovel role for Bcl-2 in regulation of cellular calcium extrusion. Curr Biol 22, 1241-1246 (2012).
    • (2012) Curr Biol , vol.22 , pp. 1241-1246
    • Ferdek, P.E.1
  • 10
    • 0032532213 scopus 로고    scopus 로고
    • Modulation of endoplasmic reticulum calcium pump by Bcl-2
    • Kuo, T. H. et al. Modulation of endoplasmic reticulum calcium pump by Bcl-2. Oncogene 17, 1903-1910 (1998).
    • (1998) Oncogene , vol.17 , pp. 1903-1910
    • Kuo, T.H.1
  • 12
    • 0031993255 scopus 로고    scopus 로고
    • Bax inhibitor-1, amammalian apoptosis suppressor identified by functional screening in yeast
    • Xu,Q. & Reed, J. C. Bax inhibitor-1, amammalian apoptosis suppressor identified by functional screening in yeast. Mol Cell 1, 337-346 (1998).
    • (1998) Mol Cell , vol.1 , pp. 337-346
    • Xu, Q.1    Reed, J.C.2
  • 13
    • 11844284861 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum
    • Oakes, S. A. et al. Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum. Proc Natl Acad Sci U S A 102, 105-110 (2005).
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 105-110
    • Oakes, S.A.1
  • 14
    • 47349089719 scopus 로고    scopus 로고
    • Targeting Bcl-2-IP3 receptor interaction to reverse Bcl-2's inhibition of apoptotic calcium signals
    • Rong, Y. P. et al. Targeting Bcl-2-IP3 receptor interaction to reverse Bcl-2's inhibition of apoptotic calcium signals. Mol Cell 31, 255-265 (2008).
    • (2008) Mol Cell , vol.31 , pp. 255-265
    • Rong, Y.P.1
  • 15
    • 27144487808 scopus 로고    scopus 로고
    • The endoplasmic reticulum gateway to apoptosis by Bcl-XL modulation of the InsP3R
    • White, C. et al. The endoplasmic reticulum gateway to apoptosis by Bcl-XL modulation of the InsP3R. Nat Cell Biol 7, 1021-1028 (2005).
    • (2005) Nat Cell Biol , vol.7 , pp. 1021-1028
    • White, C.1
  • 16
    • 84902531937 scopus 로고    scopus 로고
    • Bcl-2 binds to and inhibits ryanodine receptors
    • Vervliet, T. et al. Bcl-2 binds to and inhibits ryanodine receptors. J Cell Sci 127, 2782-2792 (2014).
    • (2014) J Cell Sci , vol.127 , pp. 2782-2792
    • Vervliet, T.1
  • 17
    • 38549145044 scopus 로고    scopus 로고
    • Diagnosing and exploiting cancer's addiction to blocks in apoptosis
    • Letai, A. G. Diagnosing and exploiting cancer's addiction to blocks in apoptosis. Nat Rev Cancer 8, 121-132 (2008).
    • (2008) Nat Rev Cancer , vol.8 , pp. 121-132
    • Letai, A.G.1
  • 18
    • 67349156098 scopus 로고    scopus 로고
    • Targeting Bcl-2 based on the interaction of its BH4 domain with the inositol 1,4,5-trisphosphate receptor
    • Rong, Y. P., Barr, P., Yee, V. C. & Distelhorst, C.W. Targeting Bcl-2 based on the interaction of its BH4 domain with the inositol 1,4,5-trisphosphate receptor. Biochim Biophys Acta 1793, 971-978 (2009).
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 971-978
    • Rong, Y.P.1    Barr, P.2    Yee, V.C.3    Distelhorst, C.W.4
  • 19
    • 84855679389 scopus 로고    scopus 로고
    • 21 signaling and apoptosis by the BH4 domain of Bcl-2 versus Bcl-Xl
    • 21 signaling and apoptosis by the BH4 domain of Bcl-2 versus Bcl-Xl. Cell Death Differ 19, 295-309 (2012).
    • (2012) Cell Death Differ , vol.19 , pp. 295-309
    • Monaco, G.1
  • 20
    • 84861570613 scopus 로고    scopus 로고
    • Identification of a phenylacylsulfonamide series of dual Bcl-2/Bcl-xL antagonists
    • Perez, H. L. et al. Identification of a phenylacylsulfonamide series of dual Bcl-2/Bcl-xL antagonists. Bioorg Med Chem Lett 22, 3946-3950 (2012).
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 3946-3950
    • Perez, H.L.1
  • 21
    • 0346457100 scopus 로고    scopus 로고
    • Bcl-XLmutations suppress cellular sensitivity to antimycinA
    • Manion,M. K. et al. Bcl-XLmutations suppress cellular sensitivity to antimycinA. J Biol Chem 279, 2159-2165 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 2159-2165
    • Manion, M.K.1
  • 22
    • 0035199166 scopus 로고    scopus 로고
    • Design and application of a cytokine-receptor-based interaction trap
    • Eyckerman, S. et al. Design and application of a cytokine-receptor-based interaction trap. Nat Cell Biol 3, 1114-1119 (2001).
    • (2001) Nat Cell Biol , vol.3 , pp. 1114-1119
    • Eyckerman, S.1
  • 23
    • 0031959032 scopus 로고    scopus 로고
    • Partial cloning and differential expression of ryanodine receptor calcium-release channel genes in human tissues including the hippocampus and cerebellum
    • Martin, C., Chapman, K. E., Seckl, J. R. & Ashley, R. H. Partial cloning and differential expression of ryanodine receptor calcium-release channel genes in human tissues including the hippocampus and cerebellum. Neuroscience 85, 205-216 (1998).
    • (1998) Neuroscience , vol.85 , pp. 205-216
    • Martin, C.1    Chapman, K.E.2    Seckl, J.R.3    Ashley, R.H.4
  • 24
    • 0034724190 scopus 로고    scopus 로고
    • BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death
    • Shimizu, S., Konishi, A., Kodama, T. & Tsujimoto, Y. BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death. Proc Natl Acad Sci U S A 97, 3100-3105 (2000).
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 3100-3105
    • Shimizu, S.1    Konishi, A.2    Kodama, T.3    Tsujimoto, Y.4
  • 25
    • 84880082132 scopus 로고    scopus 로고
    • 21 uptake
    • 21 uptake. J Biol Chem 288, 19870-19881 (2013).
    • (2013) J Biol Chem , vol.288 , pp. 19870-19881
    • Huang, H.1
  • 26
    • 84902436962 scopus 로고    scopus 로고
    • 21 at subcellular resolution using CEPIA
    • 21 at subcellular resolution using CEPIA. Nat Commun 5, 4153 (2014).
    • (2014) Nat Commun , vol.5 , pp. 4153
    • Suzuki, J.1
  • 27
    • 84926443310 scopus 로고    scopus 로고
    • 21 signals to mitochondria
    • Epub ahead of print
    • 21 signals to mitochondria. J Biol Chem Epub ahead of print (2015).
    • (2015) J Biol Chem
    • Monaco, G.1
  • 28
    • 81255135930 scopus 로고    scopus 로고
    • Systemic delivery of BH4 anti-apoptotic peptide using CPPs prevents cardiac ischemia-reperfusion injuries in vivo
    • Boisguerin, P. et al. Systemic delivery of BH4 anti-apoptotic peptide using CPPs prevents cardiac ischemia-reperfusion injuries in vivo. J Control Release 156, 146-153 (2011).
    • (2011) J Control Release , vol.156 , pp. 146-153
    • Boisguerin, P.1
  • 29
    • 11144260163 scopus 로고    scopus 로고
    • BH4 peptide derivative from Bcl-xL attenuates ischemia/reperfusion injury thorough anti-apoptotic mechanism in rat hearts
    • Ono, M. et al. BH4 peptide derivative from Bcl-xL attenuates ischemia/reperfusion injury thorough anti-apoptotic mechanism in rat hearts. Eur J Cardiothorac Surg 27, 117-121 (2005).
    • (2005) Eur J Cardiothorac Surg , vol.27 , pp. 117-121
    • Ono, M.1
  • 30
    • 0346753589 scopus 로고    scopus 로고
    • BH4-domain peptide from Bcl-xL exerts anti-apoptotic activity in vivo
    • Sugioka, R. et al. BH4-domain peptide from Bcl-xL exerts anti-apoptotic activity in vivo. Oncogene 22, 8432-8440 (2003).
    • (2003) Oncogene , vol.22 , pp. 8432-8440
    • Sugioka, R.1
  • 31
    • 1842628551 scopus 로고    scopus 로고
    • Exogenous BH4/Bcl-2 peptide reverts coronary endothelial cell apoptosis induced by oxidative stress
    • Cantara, S., Donnini, S., Giachetti, A., Thorpe, P. E. & Ziche, M. Exogenous BH4/Bcl-2 peptide reverts coronary endothelial cell apoptosis induced by oxidative stress. J Vasc Res 41, 202-207 (2004).
    • (2004) J Vasc Res , vol.41 , pp. 202-207
    • Cantara, S.1    Donnini, S.2    Giachetti, A.3    Thorpe, P.E.4    Ziche, M.5
  • 32
    • 33846781454 scopus 로고    scopus 로고
    • TAT-BH4 counteracts Abeta toxicity on capillary endothelium
    • Cantara, S., Thorpe, P. E., Ziche, M. & Donnini, S. TAT-BH4 counteracts Abeta toxicity on capillary endothelium. FEBS Lett 581, 702-706 (2007).
    • (2007) FEBS Lett , vol.581 , pp. 702-706
    • Cantara, S.1    Thorpe, P.E.2    Ziche, M.3    Donnini, S.4
  • 33
    • 33645988546 scopus 로고    scopus 로고
    • TAT-BH4 and TAT-Bcl-xL peptides protect against sepsisinduced lymphocyte apoptosis in vivo
    • Hotchkiss, R. S. et al. TAT-BH4 and TAT-Bcl-xL peptides protect against sepsisinduced lymphocyte apoptosis in vivo. J Immunol 176, 5471-5477 (2006).
    • (2006) J Immunol , vol.176 , pp. 5471-5477
    • Hotchkiss, R.S.1
  • 34
    • 33847143210 scopus 로고    scopus 로고
    • Anti-apoptotic peptides protect against radiation-induced cell death
    • McConnell, K. W. et al. Anti-apoptotic peptides protect against radiation-induced cell death. Biochem Biophys Res Commun 355, 501-507 (2007).
    • (2007) Biochem Biophys Res Commun , vol.355 , pp. 501-507
    • McConnell, K.W.1
  • 35
    • 67149093479 scopus 로고    scopus 로고
    • Bcl-xL prevents peritoneal dialysis solution-induced leukocyte apoptosis
    • Santamaria, B. et al. Bcl-xL prevents peritoneal dialysis solution-induced leukocyte apoptosis. Perit Dial Int 28 Suppl 5, S48-52 (2008).
    • (2008) Perit Dial Int , vol.28 , pp. S48-52
    • Santamaria, B.1
  • 36
    • 4544325016 scopus 로고    scopus 로고
    • Delivery of Bcl-XL or its BH4 domain by protein transduction inhibits apoptosis in human islets
    • Klein, D. et al. Delivery of Bcl-XL or its BH4 domain by protein transduction inhibits apoptosis in human islets. Biochem Biophys Res Commun 323, 473-478 (2004).
    • (2004) Biochem Biophys Res Commun , vol.323 , pp. 473-478
    • Klein, D.1
  • 37
    • 84856331327 scopus 로고    scopus 로고
    • The BH4 domain of Bcl-XL rescues astrocyte degeneration in amyotrophic lateral sclerosis by modulating intracellular calcium signals
    • Martorana, F. et al. The BH4 domain of Bcl-XL rescues astrocyte degeneration in amyotrophic lateral sclerosis by modulating intracellular calcium signals. Hum Mol Genet 21, 826-840 (2012).
    • (2012) Hum Mol Genet , vol.21 , pp. 826-840
    • Martorana, F.1
  • 38
    • 84875058166 scopus 로고    scopus 로고
    • 21 signaling and EC-coupling
    • 21 signaling and EC-coupling. Biochim Biophys Acta 1833, 866-875 (2013).
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 866-875
    • Niggli, E.1
  • 39
    • 0031951413 scopus 로고    scopus 로고
    • Sulfhydryl oxidation modifies the calcium dependence of ryanodine-sensitive calcium channels of excitable cells
    • Marengo, J. J., Hidalgo, C. & Bull, R. Sulfhydryl oxidation modifies the calcium dependence of ryanodine-sensitive calcium channels of excitable cells. Biophys J 74, 1263-1277 (1998).
    • (1998) Biophys J , vol.74 , pp. 1263-1277
    • Marengo, J.J.1    Hidalgo, C.2    Bull, R.3
  • 40
    • 0032498185 scopus 로고    scopus 로고
    • Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation
    • Xu, L., Eu, J. P., Meissner, G. & Stamler, J. S. Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation. Science 279, 234-237 (1998).
    • (1998) Science , vol.279 , pp. 234-237
    • Xu, L.1    Eu, J.P.2    Meissner, G.3    Stamler, J.S.4
  • 41
    • 34247150261 scopus 로고    scopus 로고
    • 21 leak via stabilization of ryanodine receptor in heart failure
    • 21 leak via stabilization of ryanodine receptor in heart failure. J Am Coll Cardiol 49, 1722-1732 (2007).
    • (2007) J Am Coll Cardiol , vol.49 , pp. 1722-1732
    • Mochizuki, M.1
  • 42
    • 21544451389 scopus 로고    scopus 로고
    • Defective regulation of interdomain interactions within the ryanodine receptor plays a key role in the pathogenesis of heart failure
    • Oda, T. et al. Defective regulation of interdomain interactions within the ryanodine receptor plays a key role in the pathogenesis of heart failure. Circulation 111, 3400-3410 (2005).
    • (2005) Circulation , vol.111 , pp. 3400-3410
    • Oda, T.1
  • 43
    • 77953920801 scopus 로고    scopus 로고
    • Calciumsignaling in the islets
    • Islam,M. S.Calciumsignaling in the islets. Adv Exp Med Biol 654, 235-259 (2010).
    • (2010) Adv Exp Med Biol , vol.654 , pp. 235-259
    • Islam, M.S.1
  • 44
    • 79952478406 scopus 로고    scopus 로고
    • Ryanodine receptors: Structure, expression, molecular details, and function in calcium release
    • Lanner, J. T., Georgiou, D. K., Joshi, A. D. & Hamilton, S. L. Ryanodine receptors: structure, expression, molecular details, and function in calcium release. Cold Spring Harb Perspect Biol 2, a003996 (2010).
    • (2010) Cold Spring Harb Perspect Biol , vol.2 , pp. a003996
    • Lanner, J.T.1    Georgiou, D.K.2    Joshi, A.D.3    Hamilton, S.L.4
  • 45
    • 79960672046 scopus 로고    scopus 로고
    • 21 handling in excitable cells in health and disease
    • 21 handling in excitable cells in health and disease. Pharmacol Rev 63, 700-727 (2011).
    • (2011) Pharmacol Rev , vol.63 , pp. 700-727
    • Stutzmann, G.E.1    Mattson, M.P.2
  • 46
    • 84866395344 scopus 로고    scopus 로고
    • Ryanodine receptors: Structure and function
    • Van Petegem, F. Ryanodine receptors: structure and function. J Biol Chem 287, 31624-31632 (2012).
    • (2012) J Biol Chem , vol.287 , pp. 31624-31632
    • Van Petegem, F.1
  • 48
    • 33748997392 scopus 로고    scopus 로고
    • Mutations in RYR1 in malignant hyperthermia and central core disease
    • Robinson, R., Carpenter, D., Shaw, M. A., Halsall, J. & Hopkins, P. Mutations in RYR1 in malignant hyperthermia and central core disease. Hum Mutat 27, 977-989 (2006).
    • (2006) Hum Mutat , vol.27 , pp. 977-989
    • Robinson, R.1    Carpenter, D.2    Shaw, M.A.3    Halsall, J.4    Hopkins, P.5
  • 49
    • 67349116018 scopus 로고    scopus 로고
    • Ryanodine receptor-mediated arrhythmias and sudden cardiac death
    • Blayney, L. M. & Lai, F. A. Ryanodine receptor-mediated arrhythmias and sudden cardiac death. Pharmacol Ther 123, 151-177 (2009).
    • (2009) Pharmacol Ther , vol.123 , pp. 151-177
    • Blayney, L.M.1    Lai, F.A.2
  • 50
    • 84876304597 scopus 로고    scopus 로고
    • Dysfunctional ryanodine receptors in the heart: New insights into complex cardiovascular diseases
    • Marx, S. O. & Marks, A. R. Dysfunctional ryanodine receptors in the heart: new insights into complex cardiovascular diseases. J Mol Cell Cardiol 58, 225-231 (2013).
    • (2013) J Mol Cell Cardiol , vol.58 , pp. 225-231
    • Marx, S.O.1    Marks, A.R.2
  • 51
    • 79954594124 scopus 로고    scopus 로고
    • 21 handling and arrhythmogenesis
    • 21 handling and arrhythmogenesis. Circ Res 108, 871-883 (2011).
    • (2011) Circ Res , vol.108 , pp. 871-883
    • Priori, S.G.1    Chen, S.R.2
  • 52
    • 84858336607 scopus 로고    scopus 로고
    • Altered ryanodine receptor expression in mild cognitive impairment and Alzheimer's disease
    • e1001-1006
    • Bruno, A. M. et al. Altered ryanodine receptor expression in mild cognitive impairment and Alzheimer's disease. Neurobiol Aging 33, 1001 e1001-1006 (2012).
    • (2012) Neurobiol Aging , vol.33 , pp. 1001
    • Bruno, A.M.1
  • 53
    • 84903209626 scopus 로고    scopus 로고
    • Ryanodine receptors: Physiological function and deregulation in Alzheimer disease
    • Del Prete, D., Checler, F. & Chami, M. Ryanodine receptors: physiological function and deregulation in Alzheimer disease. Mol Neurodegener 9, 21 (2014).
    • (2014) Mol Neurodegener , vol.9 , pp. 21
    • Del Prete, D.1    Checler, F.2    Chami, M.3
  • 54
    • 84901341037 scopus 로고    scopus 로고
    • The role of ryanodine receptor type 3 in a mouse model of Alzheimer disease
    • Liu, J. et al. The role of ryanodine receptor type 3 in a mouse model of Alzheimer disease. Channels (Austin) 8, 230-242 (2014).
    • (2014) Channels (Austin) , vol.8 , pp. 230-242
    • Liu, J.1
  • 55
    • 82055164052 scopus 로고    scopus 로고
    • Dantrolene is neuroprotective in Huntington's disease transgenic mouse model
    • Chen, X. et al. Dantrolene is neuroprotective in Huntington's disease transgenic mouse model. Mol Neurodegener 6, 81 (2011).
    • (2011) Mol Neurodegener , vol.6 , pp. 81
    • Chen, X.1
  • 56
    • 0037096163 scopus 로고    scopus 로고
    • 21 signals in HEK 293 cells
    • 21 signals in HEK 293 cells. J Cell Sci 115, 2497-2504 (2002).
    • (2002) J Cell Sci , vol.115 , pp. 2497-2504
    • Rossi, D.1
  • 57
    • 0034548763 scopus 로고    scopus 로고
    • Identification of the Y985 and Y1077 motifs as SOCS3 recruitment sites in the murine leptin receptor
    • Eyckerman, S., Broekaert, D., Verhee, A., Vandekerckhove, J. & Tavernier, J. Identification of the Y985 and Y1077 motifs as SOCS3 recruitment sites in the murine leptin receptor. FEBS Lett 486, 33-37 (2000).
    • (2000) FEBS Lett , vol.486 , pp. 33-37
    • Eyckerman, S.1    Broekaert, D.2    Verhee, A.3    Vandekerckhove, J.4    Tavernier, J.5
  • 58
    • 80054839023 scopus 로고    scopus 로고
    • Rapid synthesis of the Xlinked mental retardation protein OPHN1 mediates mGluR-dependent LTD through interaction with the endocytic machinery
    • Nadif Kasri, N., Nakano-Kobayashi, A. & Van Aelst, L. Rapid synthesis of the Xlinked mental retardation protein OPHN1 mediates mGluR-dependent LTD through interaction with the endocytic machinery. Neuron 72, 300-315 (2011).
    • (2011) Neuron , vol.72 , pp. 300-315
    • Nadif Kasri, N.1    Nakano-Kobayashi, A.2    Van Aelst, L.3
  • 59
    • 0242317457 scopus 로고    scopus 로고
    • Heteromeric MAPPIT: A novel strategy to study modificationdependent protein-protein interactions in mammalian cells
    • Lemmens, I. et al. Heteromeric MAPPIT: a novel strategy to study modificationdependent protein-protein interactions in mammalian cells. Nucleic Acids Res 31, e75 (2003).
    • (2003) Nucleic Acids Res , vol.31 , pp. e75
    • Lemmens, I.1
  • 60
    • 84902441134 scopus 로고    scopus 로고
    • 21 signaling
    • ed. Parys, J. B., Bootman,M., Yule,D. I. & Bultynck, G. Cold SpringHarbor
    • 21 signaling in Calcium Techniques: A Laboratory Manual (ed. Parys, J. B., Bootman,M., Yule,D. I. & Bultynck, G.) 93-112 (Cold SpringHarbor, 2014).
    • (2014) Calcium Techniques: A Laboratory Manual , pp. 93-112
    • Decrock, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.