메뉴 건너뛰기




Volumn 22, Issue 6, 2015, Pages 458-465

Repulsive guidance molecule is a structural bridge between neogenin and bone morphogenetic protein

Author keywords

[No Author keywords available]

Indexed keywords

BONE MORPHOGENETIC PROTEIN 2; BONE MORPHOGENETIC PROTEIN RECEPTOR 1; MEMBRANE PROTEIN; NEOGENIN; REPULSIVE GUIDANCE MOLECULE; UNCLASSIFIED DRUG; BMP2 PROTEIN, HUMAN; NERVE CELL ADHESION MOLECULE; PROTEIN BINDING;

EID: 84930397648     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3016     Document Type: Article
Times cited : (79)

References (91)
  • 1
    • 33846857963 scopus 로고    scopus 로고
    • Neogenin and repulsive guidance molecule signaling in the central nervous system
    • Yamashita, T., Mueller, B.K. & Hata, K. Neogenin and repulsive guidance molecule signaling in the central nervous system. Curr. Opin. Neurobiol. 17, 29-34 (2007).
    • (2007) Curr. Opin. Neurobiol. , vol.17 , pp. 29-34
    • Yamashita, T.1    Mueller, B.K.2    Hata, K.3
  • 2
    • 79955586868 scopus 로고    scopus 로고
    • Repulsive guidance molecule-A (RGM-A) inhibits leukocyte migration and mitigates infammation
    • Mirakaj, V. et al. Repulsive guidance molecule-A (RGM-A) inhibits leukocyte migration and mitigates infammation. Proc. Natl. Acad. Sci. USA 108, 6555-6560 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 6555-6560
    • Mirakaj, V.1
  • 3
    • 79953743514 scopus 로고    scopus 로고
    • RGMa modulates T cell responses and is involved in autoimmune encephalomyelitis
    • Muramatsu, R. et al. RGMa modulates T cell responses and is involved in autoimmune encephalomyelitis. Nat. Med. 17, 488-494 (2011).
    • (2011) Nat. Med. , vol.17 , pp. 488-494
    • Muramatsu, R.1
  • 4
    • 67649215234 scopus 로고    scopus 로고
    • Frequent inactivation of axon guidance molecule RGMA in human colon cancer through genetic and epigenetic mechanisms
    • Li, V.S. et al. Frequent inactivation of axon guidance molecule RGMA in human colon cancer through genetic and epigenetic mechanisms. Gastroenterology 137, 176-187 (2009).
    • (2009) Gastroenterology , vol.137 , pp. 176-187
    • Li, V.S.1
  • 5
    • 9144252017 scopus 로고    scopus 로고
    • Mutations in HFE2 cause iron overload in chromosome 1q-linked juvenile hemochromatosis
    • Papanikolaou, G. et al. Mutations in HFE2 cause iron overload in chromosome 1q-linked juvenile hemochromatosis. Nat. Genet. 36, 77-82 (2004).
    • (2004) Nat. Genet. , vol.36 , pp. 77-82
    • Papanikolaou, G.1
  • 6
    • 18544379947 scopus 로고    scopus 로고
    • RGM is a repulsive guidance molecule for retinal axons
    • Monnier, P.P. et al. RGM is a repulsive guidance molecule for retinal axons. Nature 419, 392-395 (2002).
    • (2002) Nature , vol.419 , pp. 392-395
    • Monnier, P.P.1
  • 7
    • 4143124603 scopus 로고    scopus 로고
    • Neogenin mediates the action of repulsive guidance molecule
    • Rajagopalan, S. et al. Neogenin mediates the action of repulsive guidance molecule. Nat. Cell Biol. 6, 756-762 (2004).
    • (2004) Nat. Cell Biol. , vol.6 , pp. 756-762
    • Rajagopalan, S.1
  • 8
    • 11144245556 scopus 로고    scopus 로고
    • Repulsive guidance molecule/neogenin: A novel ligand-receptor system playing multiple roles in neural development
    • Matsunaga, E. & Chedotal, A. Repulsive guidance molecule/neogenin: a novel ligand-receptor system playing multiple roles in neural development. Dev. Growth Differ. 46, 481-486 (2004).
    • (2004) Dev. Growth Differ. , vol.46 , pp. 481-486
    • Matsunaga, E.1    Chedotal, A.2
  • 9
    • 84879793105 scopus 로고    scopus 로고
    • Structure of the repulsive guidance molecule (RGM)-neogenin signaling hub
    • Bell, C.H. et al. Structure of the repulsive guidance molecule (RGM)-neogenin signaling hub. Science 341, 77-80 (2013).
    • (2013) Science , vol.341 , pp. 77-80
    • Bell, C.H.1
  • 10
    • 33646370235 scopus 로고    scopus 로고
    • Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression
    • Babitt, J.L. et al. Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression. Nat. Genet. 38, 531-539 (2006).
    • (2006) Nat. Genet. , vol.38 , pp. 531-539
    • Babitt, J.L.1
  • 11
    • 20244375259 scopus 로고    scopus 로고
    • DRAGON, a bone morphogenetic protein co-receptor
    • Samad, T.A. et al. DRAGON, a bone morphogenetic protein co-receptor. J. Biol. Chem. 280, 14122-14129 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 14122-14129
    • Samad, T.A.1
  • 12
    • 23844456919 scopus 로고    scopus 로고
    • Repulsive guidance molecule (RGMa), a DRAGON homologue, is a bone morphogenetic protein co-receptor
    • Babitt, J.L. et al. Repulsive guidance molecule (RGMa), a DRAGON homologue, is a bone morphogenetic protein co-receptor. J. Biol. Chem. 280, 29820-29827 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 29820-29827
    • Babitt, J.L.1
  • 13
    • 77951086900 scopus 로고    scopus 로고
    • Neogenin inhibits HJV secretion and regulates BMP-induced hepcidin expression and iron homeostasis
    • Lee, D.H. et al. Neogenin inhibits HJV secretion and regulates BMP-induced hepcidin expression and iron homeostasis. Blood 115, 3136-3145 (2010).
    • (2010) Blood , vol.115 , pp. 3136-3145
    • Lee, D.H.1
  • 14
    • 69249118614 scopus 로고    scopus 로고
    • Hemojuvelin-neogenin interaction is required for bone morphogenic protein-4-induced hepcidin expression
    • Zhang, A.S., Yang, F. , Wang, J., Tsukamoto, H. & Enns, C.A. Hemojuvelin-neogenin interaction is required for bone morphogenic protein-4-induced hepcidin expression. J. Biol. Chem. 284, 22580-22589 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 22580-22589
    • Zhang, A.S.1    Yang, F.2    Wang, J.3    Tsukamoto, H.4    Enns, C.A.5
  • 15
    • 84866742560 scopus 로고    scopus 로고
    • TGFβ signalling in context
    • Massagué, J. TGFβ signalling in context. Nat. Rev. Mol. Cell Biol. 13, 616-630 (2012).
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 616-630
    • Massagué, J.1
  • 17
    • 79151473137 scopus 로고    scopus 로고
    • Bone morphogenetic proteins: A critical review
    • Bragdon, B. et al. Bone morphogenetic proteins: a critical review. Cell. Signal. 23, 609-620 (2011).
    • (2011) Cell. Signal. , vol.23 , pp. 609-620
    • Bragdon, B.1
  • 18
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-beta signaling from cell membrane to the nucleus
    • Shi, Y. & Massagué, J. Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Cell 113, 685-700 (2003).
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massagué, J.2
  • 19
    • 23044466047 scopus 로고    scopus 로고
    • Specifcity and versatility in tgf-beta signaling through Smads
    • Feng, X.H. & Derynck, R. Specifcity and versatility in tgf-beta signaling through Smads. Annu. Rev. Cell Dev. Biol. 21, 659-693 (2005).
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 659-693
    • Feng, X.H.1    Derynck, R.2
  • 20
    • 0142104985 scopus 로고    scopus 로고
    • Smad-dependent and Smad-independent pathways in TGF-β family signalling
    • Derynck, R. & Zhang, Y.E. Smad-dependent and Smad-independent pathways in TGF-β family signalling. Nature 425, 577-584 (2003).
    • (2003) Nature , vol.425 , pp. 577-584
    • Derynck, R.1    Zhang, Y.E.2
  • 21
    • 0037598870 scopus 로고    scopus 로고
    • Distinct endocytic pathways regulate TGF-β receptor signalling and turnover
    • Di Guglielmo, G.M., Le Roy, C., Goodfellow, A.F. & Wrana, J.L. Distinct endocytic pathways regulate TGF-β receptor signalling and turnover. Nat. Cell Biol. 5, 410-421 (2003).
    • (2003) Nat. Cell Biol. , vol.5 , pp. 410-421
    • Di Guglielmo, G.M.1    Le Roy, C.2    Goodfellow, A.F.3    Wrana, J.L.4
  • 22
    • 33749586993 scopus 로고    scopus 로고
    • Different routes of bone morphogenic protein (BMP) receptor endocytosis infuence BMP signaling
    • Hartung, A. et al. Different routes of bone morphogenic protein (BMP) receptor endocytosis infuence BMP signaling. Mol. Cell. Biol. 26, 7791-7805 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 7791-7805
    • Hartung, A.1
  • 23
    • 80053595685 scopus 로고    scopus 로고
    • Spatial segregation of BMP/Smad signaling affects osteoblast differentiation in C2C12 cells
    • Heining, E., Bhushan, R., Paarmann, P., Henis, Y.I. & Knaus, P. Spatial segregation of BMP/Smad signaling affects osteoblast differentiation in C2C12 cells. PLoS ONE 6, e25163 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e25163
    • Heining, E.1    Bhushan, R.2    Paarmann, P.3    Henis, Y.I.4    Knaus, P.5
  • 24
    • 84875635566 scopus 로고    scopus 로고
    • Quantitative kinetics analysis of BMP2 uptake into cells and its modulation by BMP antagonists
    • Alborzinia, H. et al. Quantitative kinetics analysis of BMP2 uptake into cells and its modulation by BMP antagonists. J. Cell Sci. 126, 117-127 (2013).
    • (2013) J. Cell Sci. , vol.126 , pp. 117-127
    • Alborzinia, H.1
  • 25
    • 34248231196 scopus 로고    scopus 로고
    • Endofn acts as a Smad anchor for receptor activation in BMP signaling
    • Shi, W. et al. Endofn acts as a Smad anchor for receptor activation in BMP signaling. J. Cell Sci. 120, 1216-1224 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 1216-1224
    • Shi, W.1
  • 27
    • 79251564772 scopus 로고    scopus 로고
    • Dragon (repulsive guidance molecule b) inhibits IL-6 expression in macrophages
    • Xia, Y. et al. Dragon (repulsive guidance molecule b) inhibits IL-6 expression in macrophages. J. Immunol. 186, 1369-1376 (2011).
    • (2011) J. Immunol. , vol.186 , pp. 1369-1376
    • Xia, Y.1
  • 28
    • 2942619988 scopus 로고    scopus 로고
    • Genetic abnormalities and juvenile hemochromatosis: Mutations of the HJV gene encoding hemojuvelin
    • Lee, P.L., Beutler, E., Rao, S.V. & Barton, J.C. Genetic abnormalities and juvenile hemochromatosis: mutations of the HJV gene encoding hemojuvelin. Blood 103, 4669-4671 (2004).
    • (2004) Blood , vol.103 , pp. 4669-4671
    • Lee, P.L.1    Beutler, E.2    Rao, S.V.3    Barton, J.C.4
  • 29
    • 67651018727 scopus 로고    scopus 로고
    • Iron overload in the Asian community
    • Lok, C.Y. et al. Iron overload in the Asian community. Blood 114, 20-25 (2009).
    • (2009) Blood , vol.114 , pp. 20-25
    • Lok, C.Y.1
  • 30
    • 84904666636 scopus 로고    scopus 로고
    • Bone morphogenetic proteins as regulators of iron metabolism
    • Parrow, N.L. & Fleming, R.E. Bone morphogenetic proteins as regulators of iron metabolism. Annu. Rev. Nutr. 34, 77-94 (2014).
    • (2014) Annu. Rev. Nutr. , vol.34 , pp. 77-94
    • Parrow, N.L.1    Fleming, R.E.2
  • 31
    • 41849096388 scopus 로고    scopus 로고
    • Neogenin interacts with hemojuvelin through its two membrane-proximal fbronectin type III domains
    • Yang, F. , West, A.P. Jr., Allendorph, G.P., Choe, S. & Bjorkman, P.J. Neogenin interacts with hemojuvelin through its two membrane-proximal fbronectin type III domains. Biochemistry 47, 4237-4245 (2008).
    • (2008) Biochemistry , vol.47 , pp. 4237-4245
    • Yang, F.1    West, A.P.2    Allendorph, G.P.3    Choe, S.4    Bjorkman, P.J.5
  • 32
    • 84866928814 scopus 로고    scopus 로고
    • Repulsive guidance molecule (RGM) family proteins exhibit differential binding kinetics for bone morphogenetic proteins (BMPs)
    • Wu, Q., Sun, C.C., Lin, H.Y. & Babitt, J.L. Repulsive guidance molecule (RGM) family proteins exhibit differential binding kinetics for bone morphogenetic proteins (BMPs). PLoS ONE 7, e46307 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e46307
    • Wu, Q.1    Sun, C.C.2    Lin, H.Y.3    Babitt, J.L.4
  • 33
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand
    • Xiong, J.P. et al. Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand. Science 296, 151-155 (2002).
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.P.1
  • 34
    • 34547687760 scopus 로고    scopus 로고
    • Molecular evolution of hemojuvelin and the repulsive guidance molecule family
    • Camus, L.M. & Lambert, L.A. Molecular evolution of hemojuvelin and the repulsive guidance molecule family. J. Mol. Evol. 65, 68-81 (2007).
    • (2007) J. Mol. Evol. , vol.65 , pp. 68-81
    • Camus, L.M.1    Lambert, L.A.2
  • 35
    • 41949115757 scopus 로고    scopus 로고
    • Selective binding of RGMc/hemojuvelin, a key protein in systemic iron metabolism, to BMP-2 and neogenin
    • Kuns-Hashimoto, R., Kuninger, D., Nili, M. & Rotwein, P. Selective binding of RGMc/hemojuvelin, a key protein in systemic iron metabolism, to BMP-2 and neogenin. Am. J. Physiol. Cell Physiol. 294, C994-C1003 (2008).
    • (2008) Am. J. Physiol. Cell Physiol. , vol.294 , pp. C994-C1003
    • Kuns-Hashimoto, R.1    Kuninger, D.2    Nili, M.3    Rotwein, P.4
  • 36
    • 20244388240 scopus 로고    scopus 로고
    • Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis
    • Roetto, A. et al. Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis. Nat. Genet. 33, 21-22 (2003).
    • (2003) Nat. Genet. , vol.33 , pp. 21-22
    • Roetto, A.1
  • 37
    • 0037111732 scopus 로고    scopus 로고
    • Inappropriate expression of hepcidin is associated with iron refractory anemia: Implications for the anemia of chronic disease
    • Weinstein, D.A. et al. Inappropriate expression of hepcidin is associated with iron refractory anemia: implications for the anemia of chronic disease. Blood 100, 3776-3781 (2002).
    • (2002) Blood , vol.100 , pp. 3776-3781
    • Weinstein, D.A.1
  • 38
    • 54349097980 scopus 로고    scopus 로고
    • Hemojuvelin N-terminal mutants reach the plasma membrane but do not activate the hepcidin response
    • Pagani, A., Silvestri, L., Nai, A. & Camaschella, C. Hemojuvelin N-terminal mutants reach the plasma membrane but do not activate the hepcidin response. Haematologica 93, 1466-1472 (2008).
    • (2008) Haematologica , vol.93 , pp. 1466-1472
    • Pagani, A.1    Silvestri, L.2    Nai, A.3    Camaschella, C.4
  • 39
    • 33646749327 scopus 로고    scopus 로고
    • Structure of the ternary signaling complex of a TGF-beta superfamily member
    • Allendorph, G.P., Vale, W.W. & Choe, S. Structure of the ternary signaling complex of a TGF-beta superfamily member. Proc. Natl. Acad. Sci. USA 103, 7643-7648 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7643-7648
    • Allendorph, G.P.1    Vale, W.W.2    Choe, S.3
  • 40
    • 33847118974 scopus 로고    scopus 로고
    • A silent H-bond can be mutationally activated for high-affnity interaction of BMP-2 and activin type IIB receptor
    • Weber, D. et al. A silent H-bond can be mutationally activated for high-affnity interaction of BMP-2 and activin type IIB receptor. BMC Struct. Biol. 7, 6 (2007).
    • (2007) BMC Struct. Biol. , vol.7 , pp. 6
    • Weber, D.1
  • 41
    • 84864990335 scopus 로고    scopus 로고
    • Specifcity and structure of a high affnity activin receptor-like kinase 1 (ALK1) signaling complex
    • Townson, S.A. et al. Specifcity and structure of a high affnity activin receptor-like kinase 1 (ALK1) signaling complex. J. Biol. Chem. 287, 27313-27325 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 27313-27325
    • Townson, S.A.1
  • 42
    • 70350037984 scopus 로고    scopus 로고
    • Receptor oligomerization and beyond: A case study in bone morphogenetic proteins
    • Heinecke, K. et al. Receptor oligomerization and beyond: a case study in bone morphogenetic proteins. BMC Biol. 7, 59 (2009).
    • (2009) BMC Biol. , vol.7 , pp. 59
    • Heinecke, K.1
  • 44
    • 0037085441 scopus 로고    scopus 로고
    • Identifcation and functional characterization of distinct critically important bone morphogenetic protein-specifc response elements in the Id1 promoter
    • Korchynskyi, O. & ten Dijke, P. Identifcation and functional characterization of distinct critically important bone morphogenetic protein-specifc response elements in the Id1 promoter. J. Biol. Chem. 277, 4883-4891 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 4883-4891
    • Korchynskyi, O.1    Ten Dijke, P.2
  • 45
    • 84871201282 scopus 로고    scopus 로고
    • Conformational states of the kinase Lck regulate clustering in early T cell signaling
    • Rossy, J., Owen, D.M., Williamson, D.J., Yang, Z. & Gaus, K. Conformational states of the kinase Lck regulate clustering in early T cell signaling. Nat. Immunol. 14, 82-89 (2013).
    • (2013) Nat. Immunol. , vol.14 , pp. 82-89
    • Rossy, J.1    Owen, D.M.2    Williamson, D.J.3    Yang, Z.4    Gaus, K.5
  • 46
    • 77954894949 scopus 로고    scopus 로고
    • Neogenin regulation of BMP-induced canonical Smad signaling and endochondral bone formation
    • Zhou, Z. et al. Neogenin regulation of BMP-induced canonical Smad signaling and endochondral bone formation. Dev. Cell 19, 90-102 (2010).
    • (2010) Dev. Cell , vol.19 , pp. 90-102
    • Zhou, Z.1
  • 47
    • 46749158788 scopus 로고    scopus 로고
    • Hemojuvelin regulates hepcidin expression via a selective subset of BMP ligands and receptors independently of neogenin
    • Xia, Y., Babitt, J.L., Sidis, Y., Chung, R.T. & Lin, H.Y. Hemojuvelin regulates hepcidin expression via a selective subset of BMP ligands and receptors independently of neogenin. Blood 111, 5195-5204 (2008).
    • (2008) Blood , vol.111 , pp. 5195-5204
    • Xia, Y.1    Babitt, J.L.2    Sidis, Y.3    Chung, R.T.4    Lin, H.Y.5
  • 48
    • 84908356476 scopus 로고    scopus 로고
    • Modifying lipid rafts promotes regeneration and functional recovery
    • Tassew, N.G. et al. Modifying lipid rafts promotes regeneration and functional recovery. Cell Reports 8, 1146-1159 (2014).
    • (2014) Cell Reports , vol.8 , pp. 1146-1159
    • Tassew, N.G.1
  • 49
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrin-mediated endocytosis
    • Vieira, A.V., Lamaze, C. & Schmid, S.L. Control of EGF receptor signaling by clathrin-mediated endocytosis. Science 274, 2086-2089 (1996).
    • (1996) Science , vol.274 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 50
    • 13444263549 scopus 로고    scopus 로고
    • Clathrin-and non-clathrin-mediated endocytic regulation of cell signalling
    • Le Roy, C. & Wrana, J.L. Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling. Nat. Rev. Mol. Cell Biol. 6, 112-126 (2005).
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 112-126
    • Le Roy, C.1    Wrana, J.L.2
  • 51
    • 84879793105 scopus 로고    scopus 로고
    • Structure of the repulsive guidance molecule (RGM)-neogenin signaling hub
    • Bell, C.H. et al. Structure of the repulsive guidance molecule (RGM)-neogenin signaling hub. Science 341, 77-80 (2013).
    • (2013) Science , vol.341 , pp. 77-80
    • Bell, C.H.1
  • 52
    • 33745912405 scopus 로고    scopus 로고
    • A time- and cost-effcient system for high-level protein production in mammalian cells
    • Aricescu, A.R., Lu, W. & Jones, E.Y. A time- and cost-effcient system for high-level protein production in mammalian cells. Acta Crystallogr. D Biol. Crystallogr. 62, 1243-1250 (2006).
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1243-1250
    • Aricescu, A.R.1    Lu, W.2    Jones, E.Y.3
  • 53
    • 79959935033 scopus 로고    scopus 로고
    • Automation of large scale transient protein expression in mammalian cells
    • Zhao, Y. et al. Automation of large scale transient protein expression in mammalian cells. J. Struct. Biol. 175, 209-215 (2011).
    • (2011) J. Struct. Biol. , vol.175 , pp. 209-215
    • Zhao, Y.1
  • 54
    • 33847653747 scopus 로고    scopus 로고
    • Glycoprotein structural genomics: Solving the glycosylation problem
    • Chang, V.T. et al. Glycoprotein structural genomics: solving the glycosylation problem. Structure 15, 267-273 (2007).
    • (2007) Structure , vol.15 , pp. 267-273
    • Chang, V.T.1
  • 55
    • 77955429857 scopus 로고    scopus 로고
    • A novel TWO-STEP renaturation procedure for effcient production of recombinant BMP-2
    • von Einem, S., Schwarz, E. & Rudolph, R. A novel TWO-STEP renaturation procedure for effcient production of recombinant BMP-2. Protein Expr. Purif. 73, 65-69 (2010).
    • (2010) Protein Expr. Purif. , vol.73 , pp. 65-69
    • Von Einem, S.1    Schwarz, E.2    Rudolph, R.3
  • 56
    • 0344393021 scopus 로고    scopus 로고
    • Quality control and protein folding in the secretory pathway
    • Trombetta, E.S. & Parodi, A.J. Quality control and protein folding in the secretory pathway. Annu. Rev. Cell Dev. Biol. 19, 649-676 (2003).
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 649-676
    • Trombetta, E.S.1    Parodi, A.J.2
  • 57
    • 23844515485 scopus 로고    scopus 로고
    • A procedure for setting up high-throughput nanolitre crystallization experiments: Crystallization workfow for initial screening, automated storage, imaging and optimization
    • Walter, T.S. et al. A procedure for setting up high-throughput nanolitre crystallization experiments: crystallization workfow for initial screening, automated storage, imaging and optimization. Acta Crystallogr. D Biol. Crystallogr. 61, 651-657 (2005).
    • (2005) Acta Crystallogr. D Biol. Crystallogr. , vol.61 , pp. 651-657
    • Walter, T.S.1
  • 58
    • 13844266400 scopus 로고    scopus 로고
    • Benefts of automated crystallization plate tracking, imaging, and analysis
    • Mayo, C.J. et al. Benefts of automated crystallization plate tracking, imaging, and analysis. Structure 13, 175-182 (2005).
    • (2005) Structure , vol.13 , pp. 175-182
    • Mayo, C.J.1
  • 59
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 61
    • 85027632383 scopus 로고
    • Automatic indexing of rotation diffraction patterns
    • Kabsch, W. Automatic indexing of rotation diffraction patterns. J. Appl. Crystallogr. 21, 67-72 (1988).
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 67-72
    • Kabsch, W.1
  • 62
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 63
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie, A.G.W. The integration of macromolecular diffraction data. Acta Crystallogr. D Biol. Crystallogr. 62, 48-57 (2006).
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 48-57
    • Leslie, A.G.W.1
  • 65
    • 33645160257 scopus 로고    scopus 로고
    • Automated diffraction image analysis and spot searching for high-throughput crystal screening
    • Zhang, Z., Sauter, N.K., van den Bedem, H., Snell, G. & Deacon, A.M. Automated diffraction image analysis and spot searching for high-throughput crystal screening. J. Appl. Crystallogr. 39, 112-119 (2006).
    • (2006) J. Appl. Crystallogr. , vol.39 , pp. 112-119
    • Zhang, Z.1    Sauter, N.K.2    Van Den Bedem, H.3    Snell, G.4    Deacon, A.M.5
  • 66
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A.J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 67
    • 0033582942 scopus 로고    scopus 로고
    • Crystal structure of human bone morphogenetic protein-2 at 2.7 A resolution
    • Scheufer, C., Sebald, W. & Hulsmeyer, M. Crystal structure of human bone morphogenetic protein-2 at 2.7 A resolution. J. Mol. Biol. 287, 103-115 (1999).
    • (1999) J. Mol. Biol. , vol.287 , pp. 103-115
    • Scheufer, C.1    Sebald, W.2    Hulsmeyer, M.3
  • 68
    • 77950798648 scopus 로고    scopus 로고
    • Recent developments in classical density modifcation
    • Cowtan, K. Recent developments in classical density modifcation. Acta Crystallogr. D Biol. Crystallogr. 66, 470-478 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 470-478
    • Cowtan, K.1
  • 69
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan, K. The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. D Biol. Crystallogr. 62, 1002-1011 (2006).
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 71
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 72
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis, I.W. et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35, W375-W383 (2007).
    • (2007) Nucleic Acids Res. , vol.35 , pp. W375-W383
    • Davis, I.W.1
  • 74
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (2007).
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 75
    • 84879169814 scopus 로고    scopus 로고
    • Upgraded ESRF BM29 beamline for SAXS on macromolecules in solution
    • Pernot, P. et al. Upgraded ESRF BM29 beamline for SAXS on macromolecules in solution. J. Synchrotron Radiat. 20, 660-664 (2013).
    • (2013) J. Synchrotron Radiat. , vol.20 , pp. 660-664
    • Pernot, P.1
  • 76
    • 84859782518 scopus 로고    scopus 로고
    • New developments in the ATSAS program package for small-angle scattering data analysis
    • Petoukhov, M.V. et al. New developments in the ATSAS program package for small-angle scattering data analysis. J. Appl. Crystallogr. 45, 342-350 (2012).
    • (2012) J. Appl. Crystallogr. , vol.45 , pp. 342-350
    • Petoukhov, M.V.1
  • 77
    • 84876800465 scopus 로고    scopus 로고
    • Accurate assessment of mass, models and resolution by small-angle scattering
    • Rambo, R.P. & Tainer, J.A. Accurate assessment of mass, models and resolution by small-angle scattering. Nature 496, 477-481 (2013).
    • (2013) Nature , vol.496 , pp. 477-481
    • Rambo, R.P.1    Tainer, J.A.2
  • 78
    • 78650905964 scopus 로고    scopus 로고
    • ROSETTA3: An object-oriented software suite for the simulation and design of macromolecules
    • Leaver-Fay, A. et al. ROSETTA3: an object-oriented software suite for the simulation and design of macromolecules. Methods Enzymol. 487, 545-574 (2011).
    • (2011) Methods Enzymol. , vol.487 , pp. 545-574
    • Leaver-Fay, A.1
  • 79
    • 0043123167 scopus 로고    scopus 로고
    • Tools for comparative protein structure modeling and analysis
    • Eswar, N. et al. Tools for comparative protein structure modeling and analysis. Nucleic Acids Res. 31, 3375-3380 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3375-3380
    • Eswar, N.1
  • 80
    • 84859455527 scopus 로고    scopus 로고
    • Structure-based model of allostery predicts coupling between distant sites
    • Weinkam, P. , Pons, J. & Sali, A. Structure-based model of allostery predicts coupling between distant sites. Proc. Natl. Acad. Sci. USA 109, 4875-4880 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 4875-4880
    • Weinkam, P.1    Pons, J.2    Sali, A.3
  • 81
    • 67650992092 scopus 로고    scopus 로고
    • Structure and fexibility within proteins as identifed through small angle X-ray scattering
    • Pelikan, M., Hura, G.L. & Hammel, M. Structure and fexibility within proteins as identifed through small angle X-ray scattering. Gen. Physiol. Biophys. 28, 174-189 (2009).
    • (2009) Gen. Physiol. Biophys. , vol.28 , pp. 174-189
    • Pelikan, M.1    Hura, G.L.2    Hammel, M.3
  • 82
    • 84882940564 scopus 로고    scopus 로고
    • Accurate SAXS profle computation and its assessment by contrast variation experiments
    • Schneidman-Duhovny, D., Hammel, M., Tainer, J.A. & Sali, A. Accurate SAXS profle computation and its assessment by contrast variation experiments. Biophys. J. 105, 962-974 (2013).
    • (2013) Biophys. J. , vol.105 , pp. 962-974
    • Schneidman-Duhovny, D.1    Hammel, M.2    Tainer, J.A.3    Sali, A.4
  • 83
    • 84874855471 scopus 로고    scopus 로고
    • All-atom ensemble modeling to analyze small-angle x-ray scattering of glycosylated proteins
    • Guttman, M., Weinkam, P., Sali, A. & Lee, K.K. All-atom ensemble modeling to analyze small-angle x-ray scattering of glycosylated proteins. Structure 21, 321-331 (2013).
    • (2013) Structure , vol.21 , pp. 321-331
    • Guttman, M.1    Weinkam, P.2    Sali, A.3    Lee, K.K.4
  • 84
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran-modifed gold surface for biospecifc interaction analysis in surface plasmon resonance sensors
    • Johnsson, B., Löfås, S. & Lindquist, G. Immobilization of proteins to a carboxymethyldextran-modifed gold surface for biospecifc interaction analysis in surface plasmon resonance sensors. Anal. Biochem. 198, 268-277 (1991).
    • (1991) Anal. Biochem. , vol.198 , pp. 268-277
    • Johnsson, B.1    Löfås, S.2    Lindquist, G.3
  • 85
    • 64049114344 scopus 로고    scopus 로고
    • A rapid and sensitive bioassay for the simultaneous measurement of multiple bone morphogenetic proteins: Identifcation and quantifcation of BMP4 BMP6 and BMP9 in bovine and human serum
    • Herrera, B. & Inman, G.J. A rapid and sensitive bioassay for the simultaneous measurement of multiple bone morphogenetic proteins: identifcation and quantifcation of BMP4, BMP6 and BMP9 in bovine and human serum. BMC Cell Biol. 10, 20 (2009).
    • (2009) BMC Cell Biol. , vol.10 , pp. 20
    • Herrera, B.1    Inman, G.J.2
  • 86
    • 0037085441 scopus 로고    scopus 로고
    • Identifcation and functional characterization of distinct critically important bone morphogenetic protein-specifc response elements in the Id1 promoter
    • Korchynskyi, O. & ten Dijke, P. Identifcation and functional characterization of distinct critically important bone morphogenetic protein-specifc response elements in the Id1 promoter. J. Biol. Chem. 277, 4883-4891 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 4883-4891
    • Korchynskyi, O.1    Ten Dijke, P.2
  • 87
    • 1642300769 scopus 로고    scopus 로고
    • SpPack: Spatial point pattern analysis in Excel using Visual Basic for Applications (VBA)
    • Perry, G.L.W. SpPack: spatial point pattern analysis in Excel using Visual Basic for Applications (VBA). Environ. Model. Softw. 19, 559-569 (2004).
    • (2004) Environ. Model. Softw. , vol.19 , pp. 559-569
    • Perry, G.L.W.1
  • 88
    • 84871201282 scopus 로고    scopus 로고
    • Conformational states of the kinase Lck regulate clustering in early T cell signaling
    • Rossy, J., Owen, D.M., Williamson, D.J., Yang, Z. & Gaus, K. Conformational states of the kinase Lck regulate clustering in early T cell signaling. Nat. Immunol. 14, 82-89 (2013).
    • (2013) Nat. Immunol. , vol.14 , pp. 82-89
    • Rossy, J.1    Owen, D.M.2    Williamson, D.J.3    Yang, Z.4    Gaus, K.5
  • 89
    • 77954630046 scopus 로고    scopus 로고
    • PALM imaging and cluster analysis of protein heterogeneity at the cell surface
    • Owen, D.M. et al. PALM imaging and cluster analysis of protein heterogeneity at the cell surface. J Biophotonics 3, 446-454 (2010).
    • (2010) J Biophotonics , vol.3 , pp. 446-454
    • Owen, D.M.1
  • 90
    • 84855965214 scopus 로고    scopus 로고
    • Optical techniques for imaging membrane domains in live cells (live-cell palm of protein clustering)
    • Owen, D.M., Williamson, D., Magenau, A. & Gaus, K. Optical techniques for imaging membrane domains in live cells (live-cell palm of protein clustering). Methods Enzymol. 504, 221-235 (2012).
    • (2012) Methods Enzymol. , vol.504 , pp. 221-235
    • Owen, D.M.1    Williamson, D.2    Magenau, A.3    Gaus, K.4
  • 91
    • 79959373064 scopus 로고    scopus 로고
    • Pre-existing clusters of the adaptor Lat do not participate in early T cell signaling events
    • Williamson, D.J. et al. Pre-existing clusters of the adaptor Lat do not participate in early T cell signaling events. Nat. Immunol. 12, 655-662 (2011).
    • (2011) Nat. Immunol. , vol.12 , pp. 655-662
    • Williamson, D.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.