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Volumn 26, Issue 6 SPEC. ISS., 2005, Pages 1035-1043

A new paradigm for hormone recognition and allosteric receptor activation revealed from structural studies of NPR-C

Author keywords

Crystallography; Protein protein interaction; Receptor; Signaling; Structure

Indexed keywords

GUANYLATE CYCLASE; NATRIURETIC FACTOR; NATRIURETIC PEPTIDE RECEPTOR A; NATRIURETIC PEPTIDE RECEPTOR B; NATRIURETIC PEPTIDE RECEPTOR C; RECEPTOR; UNCLASSIFIED DRUG;

EID: 19444371985     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2004.08.035     Document Type: Article
Times cited : (12)

References (65)
  • 1
    • 0034732942 scopus 로고    scopus 로고
    • Downregulation of atrial natriuretic peptide ANP-C receptor is associated with alterations in G-protein expression in A10 smooth muscle cells
    • M.B. Anand-Srivastava Downregulation of atrial natriuretic peptide ANP-C receptor is associated with alterations in G-protein expression in A10 smooth muscle cells Biochemistry 39 2000 6503 6513
    • (2000) Biochemistry , vol.39 , pp. 6503-6513
    • Anand-Srivastava, M.B.1
  • 2
    • 0029741022 scopus 로고    scopus 로고
    • Cytoplasmic domain of natriuretic peptide receptor-C inhibits adenylyl cyclase. Involvement of a pertussis toxin-sensitive G protein
    • M.B. Anand-Srivastava, P.D. Sehl, and D.G. Lowe Cytoplasmic domain of natriuretic peptide receptor-C inhibits adenylyl cyclase. Involvement of a pertussis toxin-sensitive G protein J Biol Chem 271 1996 19324 19329
    • (1996) J Biol Chem , vol.271 , pp. 19324-19329
    • Anand-Srivastava, M.B.1    Sehl, P.D.2    Lowe, D.G.3
  • 4
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: Implications for TNF receptor activation
    • D.W. Banner, A. D'Arcy, W. Janes, R. Gentz, H.J. Schoenfeld, and C. Broger Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation Cell 73 1993 431 445
    • (1993) Cell , vol.73 , pp. 431-445
    • Banner, D.W.1    D'Arcy, A.2    Janes, W.3    Gentz, R.4    Schoenfeld, H.J.5    Broger, C.6
  • 5
    • 0026317979 scopus 로고
    • Extracellular domain-IgG fusion proteins for three human natriuretic peptide receptors. Hormone pharmacology and application to solid phase screening of synthetic peptide antisera
    • B.D. Bennett, G.L. Bennett, R.V. Vitangcol, J.R. Jewett, J. Burnier, and W. Henzel Extracellular domain-IgG fusion proteins for three human natriuretic peptide receptors. Hormone pharmacology and application to solid phase screening of synthetic peptide antisera J Biol Chem 266 1991 23060 23067
    • (1991) J Biol Chem , vol.266 , pp. 23060-23067
    • Bennett, B.D.1    Bennett, G.L.2    Vitangcol, R.V.3    Jewett, J.R.4    Burnier, J.5    Henzel, W.6
  • 6
    • 0026725829 scopus 로고
    • Ligand-independent oligomerization of natriuretic peptide receptors. Identification of heteromeric receptors and a dominant negative mutant
    • M. Chinkers, and E.M. Wilson Ligand-independent oligomerization of natriuretic peptide receptors. Identification of heteromeric receptors and a dominant negative mutant J Biol Chem 267 1992 18589 18597
    • (1992) J Biol Chem , vol.267 , pp. 18589-18597
    • Chinkers, M.1    Wilson, E.M.2
  • 7
    • 0038175431 scopus 로고    scopus 로고
    • Natriuretic peptide receptor a activation stabilizes a membrane-distal dimer interface
    • A. De Lean, N. McNicoll, and J. Labrecque Natriuretic peptide receptor A activation stabilizes a membrane-distal dimer interface J Biol Chem 278 2003 11159 11166
    • (2003) J Biol Chem , vol.278 , pp. 11159-11166
    • De Lean, A.1    McNicoll, N.2    Labrecque, J.3
  • 8
    • 0026744565 scopus 로고
    • Characterization of the recombinant human receptor for Escherichia coli heat-stable enterotoxin
    • F.J. de Sauvage, R. Horuk, G. Bennett, C. Quan, J.P. Burnier, and D.V. Goeddel Characterization of the recombinant human receptor for Escherichia coli heat-stable enterotoxin J Biol Chem 267 1992 6479 6482
    • (1992) J Biol Chem , vol.267 , pp. 6479-6482
    • De Sauvage, F.J.1    Horuk, R.2    Bennett, G.3    Quan, C.4    Burnier, J.P.5    Goeddel, D.V.6
  • 9
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • A.M. de Vos, M. Ultsch, and A.A. Kossiakoff Human growth hormone and extracellular domain of its receptor: crystal structure of the complex Science 255 1992 306 312
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 11
    • 0028331705 scopus 로고
    • The family of guanylyl cyclase receptors and their ligands
    • J.G. Drewett, and D.L. Garbers The family of guanylyl cyclase receptors and their ligands Endocr Rev 15 1994 135 162
    • (1994) Endocr Rev , vol.15 , pp. 135-162
    • Drewett, J.G.1    Garbers, D.L.2
  • 12
    • 0029090914 scopus 로고
    • Single amino acid residue-linked signaling shifts in the transduction activities of atrial and type C natriuretic factor receptor guanylate cyclases
    • T. Duda, R.M. Goraczniak, and R.K. Sharma Single amino acid residue-linked signaling shifts in the transduction activities of atrial and type C natriuretic factor receptor guanylate cyclases Biochem Biophys Res Commun 212 1995 1046 1053
    • (1995) Biochem Biophys Res Commun , vol.212 , pp. 1046-1053
    • Duda, T.1    Goraczniak, R.M.2    Sharma, R.K.3
  • 13
    • 0028910483 scopus 로고
    • Characterization of the hormone binding site of natriuretic peptide receptor-C
    • A.M. Engel, and D.G. Lowe Characterization of the hormone binding site of natriuretic peptide receptor-C FEBS Lett 360 1995 169 172
    • (1995) FEBS Lett , vol.360 , pp. 169-172
    • Engel, A.M.1    Lowe, D.G.2
  • 14
    • 0028229051 scopus 로고
    • A single residue determines the distinct pharmacology of rat and human natriuretic peptide receptor-C
    • A.M. Engel, J.R. Schoenfeld, and D.G. Lowe A single residue determines the distinct pharmacology of rat and human natriuretic peptide receptor-C J Biol Chem 269 1994 17005 17008
    • (1994) J Biol Chem , vol.269 , pp. 17005-17008
    • Engel, A.M.1    Schoenfeld, J.R.2    Lowe, D.G.3
  • 15
    • 0028169737 scopus 로고
    • Solution conformation of an atrial natriuretic peptide variant selective for the type a receptor
    • W.J. Fairbrother, R.S. McDowell, and B.C. Cunningham Solution conformation of an atrial natriuretic peptide variant selective for the type A receptor Biochemistry 33 1994 8897 8904
    • (1994) Biochemistry , vol.33 , pp. 8897-8904
    • Fairbrother, W.J.1    McDowell, R.S.2    Cunningham, B.C.3
  • 16
    • 0035312774 scopus 로고    scopus 로고
    • Transmembrane signaling in bacterial chemoreceptors
    • J.J. Falke, and G.L. Hazelbauer Transmembrane signaling in bacterial chemoreceptors Trends Biochem Sci 26 2001 257 265
    • (2001) Trends Biochem Sci , vol.26 , pp. 257-265
    • Falke, J.J.1    Hazelbauer, G.L.2
  • 17
    • 0029773198 scopus 로고    scopus 로고
    • Glycosylation is critical for natriuretic peptide receptor-B function
    • R. Fenrick, N. McNicoll, and A. De Lean Glycosylation is critical for natriuretic peptide receptor-B function Mol Cell Biochem 165 1996 103 109
    • (1996) Mol Cell Biochem , vol.165 , pp. 103-109
    • Fenrick, R.1    McNicoll, N.2    De Lean, A.3
  • 18
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization
    • K.M. Ferguson, M.B. Berger, J.M. Mendrola, H.S. Cho, D.J. Leahy, and M.A. Lemmon EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization Mol Cell 11 2003 507 517
    • (2003) Mol Cell , vol.11 , pp. 507-517
    • Ferguson, K.M.1    Berger, M.B.2    Mendrola, J.M.3    Cho, H.S.4    Leahy, D.J.5    Lemmon, M.A.6
  • 19
    • 0035105355 scopus 로고    scopus 로고
    • Three-dimensional structure of human follicle-stimulating hormone
    • K.M. Fox, J.A. Dias, and P. Van Roey Three-dimensional structure of human follicle-stimulating hormone Mol Endocrinol 15 2001 378 389
    • (2001) Mol Endocrinol , vol.15 , pp. 378-389
    • Fox, K.M.1    Dias, J.A.2    Van Roey, P.3
  • 20
    • 0032415294 scopus 로고    scopus 로고
    • Focus on: "g protein-dependent activation of smooth muscle eNOS via natriuretic peptide clearance receptor"
    • J.J. Galligan Focus on: "G protein-dependent activation of smooth muscle eNOS via natriuretic peptide clearance receptor" Am J Physiol 275 1998 1407 1408
    • (1998) Am J Physiol , vol.275 , pp. 1407-1408
    • Galligan, J.J.1
  • 21
    • 0028034529 scopus 로고
    • Guanylyl cyclase receptors
    • D.L. Garbers, and D.G. Lowe Guanylyl cyclase receptors J Biol Chem 269 1994 30741 30744
    • (1994) J Biol Chem , vol.269 , pp. 30741-30744
    • Garbers, D.L.1    Lowe, D.G.2
  • 22
    • 0029662223 scopus 로고    scopus 로고
    • An alphabeta T cell receptor structure at 2.5 a and its orientation in the TCR-MHC complex
    • K.C. Garcia, M. Degano, R.L. Stanfield, A. Brunmark, M.R. Jackson, and P.A. Peterson An alphabeta T cell receptor structure at 2.5 A and its orientation in the TCR-MHC complex Science 274 1996 209 219
    • (1996) Science , vol.274 , pp. 209-219
    • Garcia, K.C.1    Degano, M.2    Stanfield, R.L.3    Brunmark, A.4    Jackson, M.R.5    Peterson, P.A.6
  • 23
    • 0033565368 scopus 로고    scopus 로고
    • The relevance of N-linked glycosylation to the binding of a ligand to guanylate cyclase C
    • M. Hasegawa, Y. Hidaka, A. Wada, T. Hirayama, and Y. Shimonishi The relevance of N-linked glycosylation to the binding of a ligand to guanylate cyclase C Eur J Biochem 263 1999 338 346
    • (1999) Eur J Biochem , vol.263 , pp. 338-346
    • Hasegawa, M.1    Hidaka, Y.2    Wada, A.3    Hirayama, T.4    Shimonishi, Y.5
  • 24
    • 0033117567 scopus 로고    scopus 로고
    • Expression and characterization of the extracellular domain of guanylyl cyclase C from a baculovirus and Sf21 insect cells
    • M. Hasegawa, Y. Kawano, Y. Matsumoto, Y. Hidaka, J. Fujii, and N. Taniguchi Expression and characterization of the extracellular domain of guanylyl cyclase C from a baculovirus and Sf21 insect cells Protein Expr Purif 15 1999 271 281
    • (1999) Protein Expr Purif , vol.15 , pp. 271-281
    • Hasegawa, M.1    Kawano, Y.2    Matsumoto, Y.3    Hidaka, Y.4    Fujii, J.5    Taniguchi, N.6
  • 25
    • 0035979721 scopus 로고    scopus 로고
    • Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone
    • X. He, D. Chow, M.M. Martick, and K.C. Garcia Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone Science 293 2001 1657 1662
    • (2001) Science , vol.293 , pp. 1657-1662
    • He, X.1    Chow, D.2    Martick, M.M.3    Garcia, K.C.4
  • 26
    • 18044399782 scopus 로고    scopus 로고
    • Picture story. a hormone receptor springs into action
    • J. Hollien Picture story. A hormone receptor springs into action Nat Struct Biol 8 2001 832
    • (2001) Nat Struct Biol , vol.8 , pp. 832
    • Hollien, J.1
  • 27
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking
    • W.L. Hubbell, C. Altenbach, C.M. Hubbell, and H.G. Khorana Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking Adv Protein Chem 63 2003 243 290
    • (2003) Adv Protein Chem , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 28
    • 0033592859 scopus 로고    scopus 로고
    • Ligand binding-dependent limited proteolysis of the atrial natriuretic peptide receptor: Juxtamembrane hinge structure essential for transmembrane signal transduction
    • X. Huo, T. Abe, and K.S. Misono Ligand binding-dependent limited proteolysis of the atrial natriuretic peptide receptor: juxtamembrane hinge structure essential for transmembrane signal transduction Biochemistry 38 1999 16941 16951
    • (1999) Biochemistry , vol.38 , pp. 16941-16951
    • Huo, X.1    Abe, T.2    Misono, K.S.3
  • 29
    • 0031052779 scopus 로고    scopus 로고
    • Structural analysis of natriuretic peptide receptor-C by truncation and site-directed mutagenesis
    • M. Itakura, H. Suzuki, and S. Hirose Structural analysis of natriuretic peptide receptor-C by truncation and site-directed mutagenesis Biochem J 322 1997 585 590
    • (1997) Biochem J , vol.322 , pp. 585-590
    • Itakura, M.1    Suzuki, H.2    Hirose, S.3
  • 30
    • 0032936037 scopus 로고    scopus 로고
    • Intracellular fragments of the natriuretic peptide receptor-C (NPR-C) attenuate dopamine efflux
    • S. Kanwal, D.G. Lowe, and G.J. Trachte Intracellular fragments of the natriuretic peptide receptor-C (NPR-C) attenuate dopamine efflux Endocrinology 140 1999 1118 1124
    • (1999) Endocrinology , vol.140 , pp. 1118-1124
    • Kanwal, S.1    Lowe, D.G.2    Trachte, G.J.3
  • 31
    • 0031739144 scopus 로고    scopus 로고
    • Structural basis for cytokine hormone-receptor recognition and receptor activation
    • A.A. Kossiakoff, and A.M. De Vos Structural basis for cytokine hormone-receptor recognition and receptor activation Adv Protein Chem 52 1998 67 108
    • (1998) Adv Protein Chem , vol.52 , pp. 67-108
    • Kossiakoff, A.A.1    De Vos, A.M.2
  • 32
    • 0040736351 scopus 로고    scopus 로고
    • A disulfide-bridged mutant of natriuretic peptide receptor-A displays constitutive activity. Role of receptor dimerization in signal transduction
    • J. Labrecque, N. Mc Nicoll, M. Marquis, and A. De Lean A disulfide-bridged mutant of natriuretic peptide receptor-A displays constitutive activity. Role of receptor dimerization in signal transduction J Biol Chem 274 1999 9752 9759
    • (1999) J Biol Chem , vol.274 , pp. 9752-9759
    • Labrecque, J.1    Mc Nicoll, N.2    Marquis, M.3    De Lean, A.4
  • 33
    • 0027502763 scopus 로고
    • Natriuretic peptide C-receptor: More than a clearance receptor
    • E.R. Levin Natriuretic peptide C-receptor: more than a clearance receptor Am J Physiol 264 1993 483 489
    • (1993) Am J Physiol , vol.264 , pp. 483-489
    • Levin, E.R.1
  • 34
    • 0031766635 scopus 로고    scopus 로고
    • An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation
    • O. Livnah, D.L. Johnson, E.A. Stura, F.X. Farrell, F.P. Barbone, and Y. You An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation Nat Struct Biol 5 1998 993 1004
    • (1998) Nat Struct Biol , vol.5 , pp. 993-1004
    • Livnah, O.1    Johnson, D.L.2    Stura, E.A.3    Farrell, F.X.4    Barbone, F.P.5    You, Y.6
  • 35
    • 0026446633 scopus 로고
    • Human natriuretic peptide receptor-A guanylyl cyclase is self-associated prior to hormone binding
    • D.G. Lowe Human natriuretic peptide receptor-A guanylyl cyclase is self-associated prior to hormone binding Biochemistry 31 1992 10421 10425
    • (1992) Biochemistry , vol.31 , pp. 10421-10425
    • Lowe, D.G.1
  • 36
    • 0024376353 scopus 로고
    • Human atrial natriuretic peptide receptor defines a new paradigm for second messenger signal transduction
    • D.G. Lowe, M.S. Chang, R. Hellmiss, E. Chen, S. Singh, and D.L. Garbers Human atrial natriuretic peptide receptor defines a new paradigm for second messenger signal transduction EMBO J 8 1989 1377 1384
    • (1989) EMBO J , vol.8 , pp. 1377-1384
    • Lowe, D.G.1    Chang, M.S.2    Hellmiss, R.3    Chen, E.4    Singh, S.5    Garbers, D.L.6
  • 37
    • 0026786403 scopus 로고
    • Human natriuretic peptide receptor-A guanylyl cyclase. Hormone cross-linking and antibody reactivity distinguish receptor glycoforms
    • D.G. Lowe, and B.M. Fendly Human natriuretic peptide receptor-A guanylyl cyclase. Hormone cross-linking and antibody reactivity distinguish receptor glycoforms J Biol Chem 267 1992 21691 21697
    • (1992) J Biol Chem , vol.267 , pp. 21691-21697
    • Lowe, D.G.1    Fendly, B.M.2
  • 39
    • 13044312090 scopus 로고    scopus 로고
    • The natriuretic peptide clearance receptor locally modulates the physiological effects of the natriuretic peptide system
    • N. Matsukawa, W.J. Grzesik, N. Takahashi, K.N. Pandey, S. Pang, and M. Yamauchi The natriuretic peptide clearance receptor locally modulates the physiological effects of the natriuretic peptide system Proc Natl Acad Sci USA 96 1999 7403 7408
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7403-7408
    • Matsukawa, N.1    Grzesik, W.J.2    Takahashi, N.3    Pandey, K.N.4    Pang, S.5    Yamauchi, M.6
  • 40
    • 0026728457 scopus 로고
    • Emerging principles for the recognition of peptide antigens by MHC class I molecules
    • M. Matsumura, D.H. Fremont, P.A. Peterson, and I.A. Wilson Emerging principles for the recognition of peptide antigens by MHC class I molecules Science 257 1992 927 934
    • (1992) Science , vol.257 , pp. 927-934
    • Matsumura, M.1    Fremont, D.H.2    Peterson, P.A.3    Wilson, I.A.4
  • 41
    • 0029815026 scopus 로고    scopus 로고
    • Localization by photoaffinity labeling of natriuretic peptide receptor-A binding domain
    • N. McNicoll, J. Gagnon, J.J. Rondeau, H. Ong, and A. De Lean Localization by photoaffinity labeling of natriuretic peptide receptor-A binding domain Biochemistry 35 1996 12950 12956
    • (1996) Biochemistry , vol.35 , pp. 12950-12956
    • McNicoll, N.1    Gagnon, J.2    Rondeau, J.J.3    Ong, H.4    De Lean, A.5
  • 42
    • 0028941516 scopus 로고
    • Evaluation of conformational and binding characteristics of various natriuretic peptides and related analogs
    • M. Mimeault, A. De Lean, M. Lafleur, D. Bonenfant, and A. Fournier Evaluation of conformational and binding characteristics of various natriuretic peptides and related analogs Biochemistry 34 1995 955 964
    • (1995) Biochemistry , vol.34 , pp. 955-964
    • Mimeault, M.1    De Lean, A.2    Lafleur, M.3    Bonenfant, D.4    Fournier, A.5
  • 43
    • 0034625734 scopus 로고    scopus 로고
    • Atrial natriuretic factor binding to its receptor is dependent on chloride concentration: A possible feedback-control mechanism in renal salt regulation
    • K.S. Misono Atrial natriuretic factor binding to its receptor is dependent on chloride concentration: a possible feedback-control mechanism in renal salt regulation Circ Res 86 2000 1135 1139
    • (2000) Circ Res , vol.86 , pp. 1135-1139
    • Misono, K.S.1
  • 44
    • 0036199366 scopus 로고    scopus 로고
    • Natriuretic peptide receptor: Structure and signaling
    • K.S. Misono Natriuretic peptide receptor: structure and signaling Mol Cell Biochem 230 2002 49 60
    • (2002) Mol Cell Biochem , vol.230 , pp. 49-60
    • Misono, K.S.1
  • 45
    • 0033547811 scopus 로고    scopus 로고
    • Expression and purification of the extracellular ligand-binding domain of the atrial natriuretic peptide (ANP) receptor: Monovalent binding with ANP induces 2:2 complexes
    • K.S. Misono, N. Sivasubramanian, K. Berkner, and X. Zhang Expression and purification of the extracellular ligand-binding domain of the atrial natriuretic peptide (ANP) receptor: monovalent binding with ANP induces 2:2 complexes Biochemistry 38 1999 516 523
    • (1999) Biochemistry , vol.38 , pp. 516-523
    • Misono, K.S.1    Sivasubramanian, N.2    Berkner, K.3    Zhang, X.4
  • 46
    • 0033825365 scopus 로고    scopus 로고
    • Glycosylation sites in the atrial natriuretic peptide receptor: Oligosaccharide structures are not required for hormone binding
    • M. Miyagi, X. Zhang, and K.S. Misono Glycosylation sites in the atrial natriuretic peptide receptor: oligosaccharide structures are not required for hormone binding Eur J Biochem 267 2000 5758 5768
    • (2000) Eur J Biochem , vol.267 , pp. 5758-5768
    • Miyagi, M.1    Zhang, X.2    Misono, K.S.3
  • 47
    • 0033580998 scopus 로고    scopus 로고
    • Identification of the G protein-activating domain of the natriuretic peptide clearance receptor (NPR-C)
    • K.S. Murthy, and G.M. Makhlouf Identification of the G protein-activating domain of the natriuretic peptide clearance receptor (NPR-C) J Biol Chem 274 1999 17587 17592
    • (1999) J Biol Chem , vol.274 , pp. 17587-17592
    • Murthy, K.S.1    Makhlouf, G.M.2
  • 49
    • 3142582002 scopus 로고    scopus 로고
    • Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: Rotation mechanism for transmembrane signal transduction
    • H. Ogawa, Y. Qiu, C.M. Ogata, and K.S. Misono Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: rotation mechanism for transmembrane signal transduction J Biol Chem 279 2004 28625 28631
    • (2004) J Biol Chem , vol.279 , pp. 28625-28631
    • Ogawa, H.1    Qiu, Y.2    Ogata, C.M.3    Misono, K.S.4
  • 50
    • 0033543590 scopus 로고    scopus 로고
    • A piston model for transmembrane signaling of the aspartate receptor
    • K.M. Ottemann, W. Xiao, Y.K. Shin, and D.E. Koshland Jr. A piston model for transmembrane signaling of the aspartate receptor Science 285 1999 1751 1754
    • (1999) Science , vol.285 , pp. 1751-1754
    • Ottemann, K.M.1    Xiao, W.2    Shin, Y.K.3    Koshland Jr., D.E.4
  • 51
    • 0035046326 scopus 로고    scopus 로고
    • Natriuretic peptides suppress vascular endothelial cell growth factor signaling to angiogenesis
    • A. Pedram, M. Razandi, and E.R. Levin Natriuretic peptides suppress vascular endothelial cell growth factor signaling to angiogenesis Endocrinology 142 2001 1578 1586
    • (2001) Endocrinology , vol.142 , pp. 1578-1586
    • Pedram, A.1    Razandi, M.2    Levin, E.R.3
  • 52
    • 0031935846 scopus 로고    scopus 로고
    • Characterization of the phosphorylation state of natriuretic peptide receptor-C
    • L. Pedro, R. Fenrick, M. Marquis, N. McNicoll, and A. De Lean Characterization of the phosphorylation state of natriuretic peptide receptor-C Mol Cell Biochem 178 1998 95 101
    • (1998) Mol Cell Biochem , vol.178 , pp. 95-101
    • Pedro, L.1    Fenrick, R.2    Marquis, M.3    McNicoll, N.4    De Lean, A.5
  • 53
    • 0035794170 scopus 로고    scopus 로고
    • Guanylyl cyclase-linked natriuretic peptide receptors: Structure and regulation
    • L.R. Potter, and T. Hunter Guanylyl cyclase-linked natriuretic peptide receptors: structure and regulation J Biol Chem 276 2001 6057 6060
    • (2001) J Biol Chem , vol.276 , pp. 6057-6060
    • Potter, L.R.1    Hunter, T.2
  • 54
    • 0028965963 scopus 로고
    • Stoichiometry of the atrial natriuretic factor-R1 receptor complex in the bovine zona glomerulosa
    • J.J. Rondeau, N. McNicoll, J. Gagnon, N. Bouchard, H. Ong, and A. De Lean Stoichiometry of the atrial natriuretic factor-R1 receptor complex in the bovine zona glomerulosa Biochemistry 34 1995 2130 2136
    • (1995) Biochemistry , vol.34 , pp. 2130-2136
    • Rondeau, J.J.1    McNicoll, N.2    Gagnon, J.3    Bouchard, N.4    Ong, H.5    De Lean, A.6
  • 55
    • 0037145061 scopus 로고    scopus 로고
    • Ligand-induced, receptor-mediated dimerization and activation of EGF receptor
    • J. Schlessinger Ligand-induced, receptor-mediated dimerization and activation of EGF receptor Cell 110 2002 669 672
    • (2002) Cell , vol.110 , pp. 669-672
    • Schlessinger, J.1
  • 56
    • 0031911816 scopus 로고    scopus 로고
    • Receptor-specific ligands distinguish natriuretic peptide receptors-A and -C in primate tissues
    • P. Sehl, J.Y. Tom, D. Oare, and D.G. Lowe Receptor-specific ligands distinguish natriuretic peptide receptors-A and -C in primate tissues Mol Cell Biochem 178 1998 317 324
    • (1998) Mol Cell Biochem , vol.178 , pp. 317-324
    • Sehl, P.1    Tom, J.Y.2    Oare, D.3    Lowe, D.G.4
  • 57
    • 0035069096 scopus 로고    scopus 로고
    • Natriuretic peptide signalling: Molecular and cellular pathways to growth regulation
    • M. Silberbach, and C.T. Roberts Jr. Natriuretic peptide signalling: molecular and cellular pathways to growth regulation Cell Signal 13 2001 221 231
    • (2001) Cell Signal , vol.13 , pp. 221-231
    • Silberbach, M.1    Roberts Jr., C.T.2
  • 59
    • 0032917236 scopus 로고    scopus 로고
    • C-type natriuretic peptide attenuates evoked dopamine efflux by influencing Goalpha
    • S. Takida, B.J. Elmquist, and G.J. Trachte C-type natriuretic peptide attenuates evoked dopamine efflux by influencing Goalpha Hypertension 33 1999 124 129
    • (1999) Hypertension , vol.33 , pp. 124-129
    • Takida, S.1    Elmquist, B.J.2    Trachte, G.J.3
  • 60
    • 0028876903 scopus 로고
    • Dominant negative mutations of the guanylyl cyclase-A receptor. Extracellular domain deletion and catalytic domain point mutations
    • D.K. Thompson, and D.L. Garbers Dominant negative mutations of the guanylyl cyclase-A receptor. Extracellular domain deletion and catalytic domain point mutations J Biol Chem 270 1995 425 430
    • (1995) J Biol Chem , vol.270 , pp. 425-430
    • Thompson, D.K.1    Garbers, D.L.2
  • 61
    • 0028913363 scopus 로고
    • C-type natriuretic peptide neuromodulates via "clearance" receptors
    • G.J. Trachte, S. Kanwal, B.J. Elmquist, and R.J. Ziegler C-type natriuretic peptide neuromodulates via "clearance" receptors Am J Physiol 268 1995 978 984
    • (1995) Am J Physiol , vol.268 , pp. 978-984
    • Trachte, G.J.1    Kanwal, S.2    Elmquist, B.J.3    Ziegler, R.J.4
  • 62
    • 0034612573 scopus 로고    scopus 로고
    • Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor
    • F. van den Akker, X. Zhang, M. Miyagi, X. Huo, K.S. Misono, and V.C. Yee Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor Nature 406 2000 101 104
    • (2000) Nature , vol.406 , pp. 101-104
    • Van Den Akker, F.1    Zhang, X.2    Miyagi, M.3    Huo, X.4    Misono, K.S.5    Yee, V.C.6
  • 63
    • 0029807129 scopus 로고    scopus 로고
    • Identification of ligand recognition sites in heat-stable enterotoxin receptor, membrane-associated guanylyl cyclase C by site-directed mutational analysis
    • A. Wada, T. Hirayama, H. Kitaura, J. Fujisawa, M. Hasegawa, and Y. Hidaka Identification of ligand recognition sites in heat-stable enterotoxin receptor, membrane-associated guanylyl cyclase C by site-directed mutational analysis Infect Immun 64 1996 5144 5150
    • (1996) Infect Immun , vol.64 , pp. 5144-5150
    • Wada, A.1    Hirayama, T.2    Kitaura, H.3    Fujisawa, J.4    Hasegawa, M.5    Hidaka, Y.6
  • 64
    • 0030050701 scopus 로고    scopus 로고
    • Binding in the growth hormone receptor complex
    • J.A. Wells Binding in the growth hormone receptor complex Proc Natl Acad Sci USA 93 1996 1 6
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1-6
    • Wells, J.A.1
  • 65
    • 0037405126 scopus 로고    scopus 로고
    • Identification of the G protein-activating sequence of the single-transmembrane natriuretic peptide receptor C (NPR-C)
    • H. Zhou, and K.S. Murthy Identification of the G protein-activating sequence of the single-transmembrane natriuretic peptide receptor C (NPR-C) Am J Physiol Cell Physiol 284 2003 1255 1261
    • (2003) Am J Physiol Cell Physiol , vol.284 , pp. 1255-1261
    • Zhou, H.1    Murthy, K.S.2


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