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Volumn 37, Issue 6, 2016, Pages 485-497

Antifibrotic Actions of Serelaxin - New Roles for an Old Player

Author keywords

collagen; fibrosis; relaxin; serelaxin; signal transduction; TGF 1

Indexed keywords

SERELAXIN; TRANSFORMING GROWTH FACTOR BETA1; RECOMBINANT PROTEIN; RELAXIN; SERELAXIN PROTEIN, HUMAN;

EID: 84961230915     PISSN: 01656147     EISSN: 18733735     Source Type: Journal    
DOI: 10.1016/j.tips.2016.02.007     Document Type: Review
Times cited : (29)

References (114)
  • 1
    • 33847350691 scopus 로고    scopus 로고
    • Common and unique mechanisms regulate fibrosis in various fibroproliferative diseases
    • T.A. Wynn Common and unique mechanisms regulate fibrosis in various fibroproliferative diseases J. Clin. Invest. 117 2007 524 529
    • (2007) J. Clin. Invest. , vol.117 , pp. 524-529
    • Wynn, T.A.1
  • 2
    • 0034922841 scopus 로고    scopus 로고
    • Impaired angiogenesis in the remnant kidney model: I. Potential role of vascular endothelial growth factor and thrombospondin-1
    • D.H. Kang, and et al. Impaired angiogenesis in the remnant kidney model: I. Potential role of vascular endothelial growth factor and thrombospondin-1 J. Am. Soc. Nephrol. 12 2001 1434 1447
    • (2001) J. Am. Soc. Nephrol. , vol.12 , pp. 1434-1447
    • Kang, D.H.1
  • 3
    • 63449105614 scopus 로고    scopus 로고
    • Effect of extracellular matrix composition on airway epithelial cell and fibroblast structure: Implications for airway remodeling in asthma
    • S.G. Royce, and et al. Effect of extracellular matrix composition on airway epithelial cell and fibroblast structure: implications for airway remodeling in asthma Ann. Allergy Asthma Immunol. 102 2009 238 246
    • (2009) Ann. Allergy Asthma Immunol. , vol.102 , pp. 238-246
    • Royce, S.G.1
  • 4
    • 33846573898 scopus 로고    scopus 로고
    • Fibroblast differentiation in wound healing and fibrosis
    • I.A. Darby, and T.D. Hewitson Fibroblast differentiation in wound healing and fibrosis Int. Rev. Cytol. 257 2007 143 179
    • (2007) Int. Rev. Cytol. , vol.257 , pp. 143-179
    • Darby, I.A.1    Hewitson, T.D.2
  • 5
    • 77952174830 scopus 로고    scopus 로고
    • Epithelial cell cycle arrest in G2/M mediates kidney fibrosis after injury
    • L. Yang, and et al. Epithelial cell cycle arrest in G2/M mediates kidney fibrosis after injury Nat. Med. 16 2010 535 543
    • (2010) Nat. Med. , vol.16 , pp. 535-543
    • Yang, L.1
  • 6
    • 0032724757 scopus 로고    scopus 로고
    • High glucose increases growth and collagen synthesis in cultured human tubulointerstitial cells
    • S.C. Jones, and et al. High glucose increases growth and collagen synthesis in cultured human tubulointerstitial cells Diabetic Med. 16 2000 932 938
    • (2000) Diabetic Med. , vol.16 , pp. 932-938
    • Jones, S.C.1
  • 7
    • 0031452519 scopus 로고    scopus 로고
    • Angiotensin II modulates cell growth-related events and synthesis of matrix proteins in renal interstitial fibroblasts
    • M. Ruiz-Ortega, and J. Egido Angiotensin II modulates cell growth-related events and synthesis of matrix proteins in renal interstitial fibroblasts Kidney Int. 52 1997 1497 1510
    • (1997) Kidney Int. , vol.52 , pp. 1497-1510
    • Ruiz-Ortega, M.1    Egido, J.2
  • 8
    • 84930764947 scopus 로고    scopus 로고
    • Matrix remodeling by MMPs during wound repair
    • M.G. Rohani, and W.C. Parks Matrix remodeling by MMPs during wound repair Matrix Biol. 44-46 2015 113 121
    • (2015) Matrix Biol. , vol.44-46 , pp. 113-121
    • Rohani, M.G.1    Parks, W.C.2
  • 9
    • 3042610399 scopus 로고    scopus 로고
    • Relaxin's physiological roles and other diverse actions
    • O.D. Sherwood Relaxin's physiological roles and other diverse actions Endocr. Rev. 25 2004 205 234
    • (2004) Endocr. Rev. , vol.25 , pp. 205-234
    • Sherwood, O.D.1
  • 10
    • 84872314588 scopus 로고    scopus 로고
    • Relaxin family peptides and their receptors
    • R.A. Bathgate, and et al. Relaxin family peptides and their receptors Physiol. Rev. 93 2013 405 480
    • (2013) Physiol. Rev. , vol.93 , pp. 405-480
    • Bathgate, R.A.1
  • 11
    • 0003412980 scopus 로고
    • Experimental relaxation of the pubic ligament of the Guinea pig
    • F. Hisaw Experimental relaxation of the pubic ligament of the guinea pig Proc. Soc. Exp. Biol. Med. 23 1926 661 663
    • (1926) Proc. Soc. Exp. Biol. Med. , vol.23 , pp. 661-663
    • Hisaw, F.1
  • 12
    • 77953810500 scopus 로고    scopus 로고
    • Unveiling the vasodilatory actions and mechanisms of relaxin
    • K.P. Conrad Unveiling the vasodilatory actions and mechanisms of relaxin Hypertension 56 2010 2 9
    • (2010) Hypertension , vol.56 , pp. 2-9
    • Conrad, K.P.1
  • 13
    • 79961057515 scopus 로고    scopus 로고
    • Maternal vasodilation in pregnancy: The emerging role of relaxin
    • K.P. Conrad Maternal vasodilation in pregnancy: the emerging role of relaxin Am. J. Physiol. Regul. Integr. Comp. Physiol. 301 2011 R267 R275
    • (2011) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.301 , pp. R267-R275
    • Conrad, K.P.1
  • 14
    • 84902324106 scopus 로고    scopus 로고
    • Serelaxin: A potential new drug for the treatment of acute heart failure
    • N. Neverova, and J.R. Teerlink Serelaxin: a potential new drug for the treatment of acute heart failure Expert Opin. Investig. Drugs 23 2014 1017 1026
    • (2014) Expert Opin. Investig. Drugs , vol.23 , pp. 1017-1026
    • Neverova, N.1    Teerlink, J.R.2
  • 15
    • 84871986523 scopus 로고    scopus 로고
    • Serelaxin, recombinant human relaxin-2, for treatment of acute heart failure (RELAX-AHF): A randomised, placebo-controlled trial
    • J.R. Teerlink, and et al. Serelaxin, recombinant human relaxin-2, for treatment of acute heart failure (RELAX-AHF): a randomised, placebo-controlled trial Lancet 381 2013 29 39
    • (2013) Lancet , vol.381 , pp. 29-39
    • Teerlink, J.R.1
  • 16
    • 84871927704 scopus 로고    scopus 로고
    • Effect of serelaxin on cardiac, renal, and hepatic biomarkers in the Relaxin in Acute Heart Failure (RELAX-AHF) development program: Correlation with outcomes
    • M. Metra, and et al. Effect of serelaxin on cardiac, renal, and hepatic biomarkers in the Relaxin in Acute Heart Failure (RELAX-AHF) development program: correlation with outcomes J. Am. Coll. Cardiol. 61 2013 196 206
    • (2013) J. Am. Coll. Cardiol. , vol.61 , pp. 196-206
    • Metra, M.1
  • 17
    • 33646522213 scopus 로고    scopus 로고
    • Relaxin in cardiovascular and renal disease
    • C.S. Samuel, and T.D. Hewitson Relaxin in cardiovascular and renal disease Kidney Int. 69 2006 1498 1502
    • (2006) Kidney Int. , vol.69 , pp. 1498-1502
    • Samuel, C.S.1    Hewitson, T.D.2
  • 18
    • 34250739893 scopus 로고    scopus 로고
    • Drugs of the future: The hormone relaxin
    • C.S. Samuel, and et al. Drugs of the future: the hormone relaxin Cell. Mol. Life Sci. 64 2007 1539 1557
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1539-1557
    • Samuel, C.S.1
  • 19
    • 23644459249 scopus 로고    scopus 로고
    • Relaxin regulates endometrial structure and function in the rhesus monkey
    • L.T. Goldsmith, and G. Weiss Relaxin regulates endometrial structure and function in the rhesus monkey Ann. N. Y. Acad. Sci. 1041 2005 110 117
    • (2005) Ann. N. Y. Acad. Sci. , vol.1041 , pp. 110-117
    • Goldsmith, L.T.1    Weiss, G.2
  • 20
    • 0347986674 scopus 로고    scopus 로고
    • Impaired nipple development and parturition in LGR7 knockout mice
    • M.A. Krajnc-Franken, and et al. Impaired nipple development and parturition in LGR7 knockout mice Mol. Cell. Biol. 24 2004 687 696
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 687-696
    • Krajnc-Franken, M.A.1
  • 21
    • 4644313216 scopus 로고    scopus 로고
    • Genetic targeting of relaxin and Insl3 receptors in mice
    • A.A. Kamat, and et al. Genetic targeting of relaxin and Insl3 receptors in mice Endocrinology 145 2004 4712 4720
    • (2004) Endocrinology , vol.145 , pp. 4712-4720
    • Kamat, A.A.1
  • 22
    • 65349122390 scopus 로고    scopus 로고
    • Relaxin inhibits renal myofibroblast differentiation via RXFP1, the nitric oxide pathway, and Smad2
    • I. Mookerjee, and et al. Relaxin inhibits renal myofibroblast differentiation via RXFP1, the nitric oxide pathway, and Smad2 FASEB J. 23 2009 1219 1229
    • (2009) FASEB J. , vol.23 , pp. 1219-1229
    • Mookerjee, I.1
  • 23
    • 62749129843 scopus 로고    scopus 로고
    • Relaxin family peptide receptor-1 protects against airway fibrosis during homeostasis but not against fibrosis associated with chronic allergic airways disease
    • C.S. Samuel, and et al. Relaxin family peptide receptor-1 protects against airway fibrosis during homeostasis but not against fibrosis associated with chronic allergic airways disease Endocrinology 150 2009 1495 1502
    • (2009) Endocrinology , vol.150 , pp. 1495-1502
    • Samuel, C.S.1
  • 24
    • 34247639085 scopus 로고    scopus 로고
    • Relaxin as a cardiovascular hormone: Physiology, pathophysiology and therapeutic promises
    • S. Nistri, and et al. Relaxin as a cardiovascular hormone: physiology, pathophysiology and therapeutic promises Cardiovasc. Hematol. Agents Med. Chem. 5 2007 101 108
    • (2007) Cardiovasc. Hematol. Agents Med. Chem. , vol.5 , pp. 101-108
    • Nistri, S.1
  • 25
    • 66949114470 scopus 로고    scopus 로고
    • Relaxin and its role in the development and treatment of fibrosis
    • R.G. Bennett Relaxin and its role in the development and treatment of fibrosis Transl. Res. 154 2009 1 6
    • (2009) Transl. Res. , vol.154 , pp. 1-6
    • Bennett, R.G.1
  • 26
    • 76849113368 scopus 로고    scopus 로고
    • Cardiovascular effects of relaxin: From basic science to clinical therapy
    • X.J. Du, and et al. Cardiovascular effects of relaxin: from basic science to clinical therapy Nat. Rev. Cardiol. 7 2010 48 58
    • (2010) Nat. Rev. Cardiol. , vol.7 , pp. 48-58
    • Du, X.J.1
  • 27
    • 84884398620 scopus 로고    scopus 로고
    • The emerging role of relaxin as a novel therapeutic pathway in the treatment of chronic kidney disease
    • J.M. Sasser The emerging role of relaxin as a novel therapeutic pathway in the treatment of chronic kidney disease Am. J. Physiol. Regul. Integr. Comp. Physiol. 305 2013 R559 R565
    • (2013) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.305 , pp. R559-R565
    • Sasser, J.M.1
  • 28
    • 84892165173 scopus 로고    scopus 로고
    • Relaxin: New pathophysiological aspects and pharmacological perspectives for an old protein
    • V. Cernaro, and et al. Relaxin: new pathophysiological aspects and pharmacological perspectives for an old protein Med. Res. Rev. 34 2014 77 105
    • (2014) Med. Res. Rev. , vol.34 , pp. 77-105
    • Cernaro, V.1
  • 29
    • 84894492958 scopus 로고    scopus 로고
    • Therapeutic effects of serelaxin in acute heart failure
    • X.J. Du, and et al. Therapeutic effects of serelaxin in acute heart failure Circ. J. 78 2014 542 552
    • (2014) Circ. J. , vol.78 , pp. 542-552
    • Du, X.J.1
  • 30
    • 84932182940 scopus 로고    scopus 로고
    • Intranasally administered serelaxin abrogates airway remodelling and attenuates airway hyperresponsiveness in allergic airways disease
    • S.G. Royce, and et al. Intranasally administered serelaxin abrogates airway remodelling and attenuates airway hyperresponsiveness in allergic airways disease Clin. Exp. Allergy 44 2014 1399 1408
    • (2014) Clin. Exp. Allergy , vol.44 , pp. 1399-1408
    • Royce, S.G.1
  • 32
    • 0034612234 scopus 로고    scopus 로고
    • Recombinant human relaxin in the treatment of scleroderma. A randomized, double-blind, placebo-controlled trial
    • J.R. Seibold, and et al. Recombinant human relaxin in the treatment of scleroderma. A randomized, double-blind, placebo-controlled trial Ann. Intern. Med. 132 2000 871 879
    • (2000) Ann. Intern. Med. , vol.132 , pp. 871-879
    • Seibold, J.R.1
  • 33
    • 65249109216 scopus 로고    scopus 로고
    • Recombinant human relaxin in the treatment of systemic sclerosis with diffuse cutaneous involvement: A randomized, double-blind, placebo-controlled trial
    • D. Khanna, and et al. Recombinant human relaxin in the treatment of systemic sclerosis with diffuse cutaneous involvement: a randomized, double-blind, placebo-controlled trial Arthritis Rheum. 60 2009 1102 1111
    • (2009) Arthritis Rheum. , vol.60 , pp. 1102-1111
    • Khanna, D.1
  • 34
    • 4344606223 scopus 로고    scopus 로고
    • Relaxin modulates cardiac fibroblast proliferation, differentiation and collagen production and reverses cardiac fibrosis in vivo
    • C.S. Samuel, and et al. Relaxin modulates cardiac fibroblast proliferation, differentiation and collagen production and reverses cardiac fibrosis in vivo Endocrinology 145 2004 4125 4133
    • (2004) Endocrinology , vol.145 , pp. 4125-4133
    • Samuel, C.S.1
  • 35
    • 80051472751 scopus 로고    scopus 로고
    • ω-nitro-l-Arginine methyl ester hypertensive rats
    • ω-nitro-l-Arginine methyl ester hypertensive rats Hypertension 58 2011 197 204
    • (2011) Hypertension , vol.58 , pp. 197-204
    • Sasser, J.M.1
  • 36
    • 0025302162 scopus 로고
    • Relaxin modulates synthesis and secretion of procollagenase and collagen by human dermal fibroblasts
    • E.N. Unemori, and E.P. Amento Relaxin modulates synthesis and secretion of procollagenase and collagen by human dermal fibroblasts J. Biol. Chem. 265 1990 10681 10685
    • (1990) J. Biol. Chem. , vol.265 , pp. 10681-10685
    • Unemori, E.N.1    Amento, E.P.2
  • 37
    • 0030453783 scopus 로고    scopus 로고
    • Relaxin induces an extracellular matrix-degrading phenotype in human lung fibroblasts in vitro and inhibits lung fibrosis in a murine model in vivo
    • E.N. Unemori, and et al. Relaxin induces an extracellular matrix-degrading phenotype in human lung fibroblasts in vitro and inhibits lung fibrosis in a murine model in vivo J. Clin. Invest. 98 1996 2739 2745
    • (1996) J. Clin. Invest. , vol.98 , pp. 2739-2745
    • Unemori, E.N.1
  • 38
    • 79955549454 scopus 로고    scopus 로고
    • Relaxin remodels fibrotic healing following myocardial infarction
    • C.S. Samuel, and et al. Relaxin remodels fibrotic healing following myocardial infarction Lab. Invest. 91 2011 675 690
    • (2011) Lab. Invest. , vol.91 , pp. 675-690
    • Samuel, C.S.1
  • 39
    • 24944542890 scopus 로고    scopus 로고
    • The antifibrotic effects of relaxin in human renal fibroblasts are mediated in part by inhibition of the Smad2 pathway
    • M.H. Heeg, and et al. The antifibrotic effects of relaxin in human renal fibroblasts are mediated in part by inhibition of the Smad2 pathway Kidney Int. 68 2005 96 109
    • (2005) Kidney Int. , vol.68 , pp. 96-109
    • Heeg, M.H.1
  • 40
    • 84893793330 scopus 로고    scopus 로고
    • Relaxin decreases the severity of established hepatic fibrosis in mice
    • R.G. Bennett, and et al. Relaxin decreases the severity of established hepatic fibrosis in mice Liver Int. 34 2014 416 426
    • (2014) Liver Int. , vol.34 , pp. 416-426
    • Bennett, R.G.1
  • 41
    • 77957281721 scopus 로고    scopus 로고
    • Antifibrotic properties of relaxin: In vivo mechanism of action in experimental renal tubulointerstitial fibrosis
    • T.D. Hewitson, and et al. Antifibrotic properties of relaxin: in vivo mechanism of action in experimental renal tubulointerstitial fibrosis Endocrinology 151 2010 4938 4948
    • (2010) Endocrinology , vol.151 , pp. 4938-4948
    • Hewitson, T.D.1
  • 42
    • 84877989995 scopus 로고    scopus 로고
    • Relaxin prevents cardiac fibroblast-myofibroblast transition via notch-1-mediated inhibition of TGF-β/Smad3 signaling
    • C. Sassoli, and et al. Relaxin prevents cardiac fibroblast-myofibroblast transition via notch-1-mediated inhibition of TGF-β/Smad3 signaling PLoS ONE 8 2013 e63896
    • (2013) PLoS ONE , vol.8 , pp. e63896
    • Sassoli, C.1
  • 43
    • 84939839224 scopus 로고    scopus 로고
    • Relaxin inhibits cardiac fibrosis and endothelial-mesenchymal transition via the Notch pathway
    • X. Zhou, and et al. Relaxin inhibits cardiac fibrosis and endothelial-mesenchymal transition via the Notch pathway Drug Des. Dev. Therap. 9 2015 4599 4611
    • (2015) Drug Des. Dev. Therap. , vol.9 , pp. 4599-4611
    • Zhou, X.1
  • 44
    • 84922309570 scopus 로고    scopus 로고
    • Role of sphingosine kinase/S1P axis in ECM remodeling of cardiac cells elicited by relaxin
    • A. Frati, and et al. Role of sphingosine kinase/S1P axis in ECM remodeling of cardiac cells elicited by relaxin Mol. Endocrinol. 29 2015 53 67
    • (2015) Mol. Endocrinol. , vol.29 , pp. 53-67
    • Frati, A.1
  • 45
    • 1342285008 scopus 로고    scopus 로고
    • Relaxin down-regulates renal fibroblast function and promotes matrix remodelling in vitro
    • R. Masterson, and et al. Relaxin down-regulates renal fibroblast function and promotes matrix remodelling in vitro Nephrol. Dial. Transplant. 19 2004 544 552
    • (2004) Nephrol. Dial. Transplant. , vol.19 , pp. 544-552
    • Masterson, R.1
  • 46
    • 84899460877 scopus 로고    scopus 로고
    • Relaxin does not improve angiotensin II-induced target-organ damage
    • N. Haase, and et al. Relaxin does not improve angiotensin II-induced target-organ damage PLoS ONE 9 2014 e93743
    • (2014) PLoS ONE , vol.9 , pp. e93743
    • Haase, N.1
  • 47
    • 84882374148 scopus 로고    scopus 로고
    • The anti-fibrotic hormone relaxin is not reno-protective, despite being active, in an experimental model of type 1 diabetes
    • S.E. Wong, and et al. The anti-fibrotic hormone relaxin is not reno-protective, despite being active, in an experimental model of type 1 diabetes Protein Pept. Lett. 20 2013 1029 1038
    • (2013) Protein Pept. Lett. , vol.20 , pp. 1029-1038
    • Wong, S.E.1
  • 48
    • 84865168929 scopus 로고    scopus 로고
    • Relaxin signals through a RXFP1-pERK-nNOS-NO-cGMP-dependent pathway to up-regulate matrix metalloproteinases: The additional involvement of iNOS
    • B.S. Chow, and et al. Relaxin signals through a RXFP1-pERK-nNOS-NO-cGMP-dependent pathway to up-regulate matrix metalloproteinases: the additional involvement of iNOS PLoS ONE 7 2012 e42714
    • (2012) PLoS ONE , vol.7 , pp. e42714
    • Chow, B.S.1
  • 49
    • 46349103257 scopus 로고    scopus 로고
    • Relaxin ameliorates fibrosis in experimental diabetic cardiomyopathy
    • C.S. Samuel, and et al. Relaxin ameliorates fibrosis in experimental diabetic cardiomyopathy Endocrinology 149 2008 3286 3293
    • (2008) Endocrinology , vol.149 , pp. 3286-3293
    • Samuel, C.S.1
  • 50
    • 0037428061 scopus 로고    scopus 로고
    • Relaxin, a pregnancy hormone, is a functional endothelin-1 antagonist: Attenuation of endothelin-1-mediated vasoconstriction by stimulation of endothelin type-B receptor expression via ERK-1/2 and nuclear factor-kappaB
    • T. Dschietzig, and et al. Relaxin, a pregnancy hormone, is a functional endothelin-1 antagonist: attenuation of endothelin-1-mediated vasoconstriction by stimulation of endothelin type-B receptor expression via ERK-1/2 and nuclear factor-kappaB Circ. Res. 92 2003 32 40
    • (2003) Circ. Res. , vol.92 , pp. 32-40
    • Dschietzig, T.1
  • 51
    • 34247884253 scopus 로고    scopus 로고
    • Relaxin-induced matrix metalloproteinase-9 expression is associated with activation of the NF-κB pathway in human THP-1 cells
    • T.Y. Ho, and et al. Relaxin-induced matrix metalloproteinase-9 expression is associated with activation of the NF-κB pathway in human THP-1 cells J. Leukoc. Biol. 81 2007 1303 1310
    • (2007) J. Leukoc. Biol. , vol.81 , pp. 1303-1310
    • Ho, T.Y.1
  • 52
    • 1442323685 scopus 로고    scopus 로고
    • Relaxin inhibits the activation of human neutrophils: Involvement of the nitric oxide pathway
    • E. Masini, and et al. Relaxin inhibits the activation of human neutrophils: involvement of the nitric oxide pathway Endocrinology 145 2004 1106 1112
    • (2004) Endocrinology , vol.145 , pp. 1106-1112
    • Masini, E.1
  • 53
    • 39149091073 scopus 로고    scopus 로고
    • Relaxin induces mast cell inhibition and reduces ventricular arrhythmias in a swine model of acute myocardial infarction
    • S. Nistri, and et al. Relaxin induces mast cell inhibition and reduces ventricular arrhythmias in a swine model of acute myocardial infarction Pharm. Res. 57 2008 43 48
    • (2008) Pharm. Res. , vol.57 , pp. 43-48
    • Nistri, S.1
  • 54
    • 78650175034 scopus 로고    scopus 로고
    • Relaxin inhibits early steps in vascular inflammation
    • A. Brecht, and et al. Relaxin inhibits early steps in vascular inflammation Regul. Pept. 166 2011 76 82
    • (2011) Regul. Pept. , vol.166 , pp. 76-82
    • Brecht, A.1
  • 55
    • 33947379636 scopus 로고    scopus 로고
    • Relaxin antagonizes hypertrophy and apoptosis in neonatal rat cardiomyocytes
    • X.L. Moore, and et al. Relaxin antagonizes hypertrophy and apoptosis in neonatal rat cardiomyocytes Endocrinology 148 2007 1582 1589
    • (2007) Endocrinology , vol.148 , pp. 1582-1589
    • Moore, X.L.1
  • 56
    • 23644444636 scopus 로고    scopus 로고
    • Myocardial relaxin counteracts hypertrophy in hypertensive rats
    • T. Dschietzig, and et al. Myocardial relaxin counteracts hypertrophy in hypertensive rats Ann. N. Y. Acad. Sci. 1041 2005 441 443
    • (2005) Ann. N. Y. Acad. Sci. , vol.1041 , pp. 441-443
    • Dschietzig, T.1
  • 57
    • 42449109125 scopus 로고    scopus 로고
    • Relaxin acts on stromal cells to promote epithelial and stromal proliferation and inhibit apoptosis in the mouse cervix and vagina
    • L. Yao, and et al. Relaxin acts on stromal cells to promote epithelial and stromal proliferation and inhibit apoptosis in the mouse cervix and vagina Endocrinology 149 2008 2072 2079
    • (2008) Endocrinology , vol.149 , pp. 2072-2079
    • Yao, L.1
  • 58
    • 84885627668 scopus 로고    scopus 로고
    • Relaxin protects against renal ischemia-reperfusion injury
    • T. Yoshida, and et al. Relaxin protects against renal ischemia-reperfusion injury Am. J. Physiol. Renal Physiol. 305 2013 F1169 F1176
    • (2013) Am. J. Physiol. Renal Physiol. , vol.305 , pp. F1169-F1176
    • Yoshida, T.1
  • 59
    • 0033673465 scopus 로고    scopus 로고
    • Relaxin induces vascular endothelial growth factor expression and angiogenesis selectively at wound sites
    • E.N. Unemori, and et al. Relaxin induces vascular endothelial growth factor expression and angiogenesis selectively at wound sites Wound Repair Regen. 8 2000 361 370
    • (2000) Wound Repair Regen. , vol.8 , pp. 361-370
    • Unemori, E.N.1
  • 60
    • 64549162386 scopus 로고    scopus 로고
    • Scar prevention and cosmetically enhanced wound healing using relaxin
    • D.R. Stewart Scar prevention and cosmetically enhanced wound healing using relaxin Ann. N. Y. Acad. Sci. 1160 2009 336 341
    • (2009) Ann. N. Y. Acad. Sci. , vol.1160 , pp. 336-341
    • Stewart, D.R.1
  • 61
    • 78149340412 scopus 로고    scopus 로고
    • Relaxin regulates MMP expression and promotes satellite cell mobilization during muscle healing in both young and aged mice
    • X. Mu, and et al. Relaxin regulates MMP expression and promotes satellite cell mobilization during muscle healing in both young and aged mice Am. J. Pathol. 177 2010 2399 2410
    • (2010) Am. J. Pathol. , vol.177 , pp. 2399-2410
    • Mu, X.1
  • 62
  • 64
    • 79751520982 scopus 로고    scopus 로고
    • Central arterial aging and angiotensin II signaling
    • M. Wang, and et al. Central arterial aging and angiotensin II signaling Curr. Hypertens. Rev. 6 2010 266 281
    • (2010) Curr. Hypertens. Rev. , vol.6 , pp. 266-281
    • Wang, M.1
  • 65
    • 33745226248 scopus 로고    scopus 로고
    • Relaxin family peptide receptors RXFP1 and RXFP2 modulate cAMP signaling by distinct mechanisms
    • M.L. Halls, and et al. Relaxin family peptide receptors RXFP1 and RXFP2 modulate cAMP signaling by distinct mechanisms Mol. Pharmacol. 70 2006 214 226
    • (2006) Mol. Pharmacol. , vol.70 , pp. 214-226
    • Halls, M.L.1
  • 66
    • 0034464024 scopus 로고    scopus 로고
    • The three subfamilies of leucine-rich repeat-containing G protein-coupled receptors (LGR): Identification of LGR6 and LGR7 and the signaling mechanism for LGR7
    • S.Y. Hsu, and et al. The three subfamilies of leucine-rich repeat-containing G protein-coupled receptors (LGR): identification of LGR6 and LGR7 and the signaling mechanism for LGR7 Mol. Endocrinol. 14 2000 1257 1271
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1257-1271
    • Hsu, S.Y.1
  • 67
    • 0037169071 scopus 로고    scopus 로고
    • Activation of orphan receptors by the hormone relaxin
    • S.Y. Hsu, and et al. Activation of orphan receptors by the hormone relaxin Science 295 2002 671 674
    • (2002) Science , vol.295 , pp. 671-674
    • Hsu, S.Y.1
  • 68
    • 0037503879 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase activity is required for biphasic stimulation of cyclic adenosine 3′,5′-monophosphate by relaxin
    • B.T. Nguyen, and et al. Phosphoinositide 3-kinase activity is required for biphasic stimulation of cyclic adenosine 3′,5′-monophosphate by relaxin Mol. Endocrinol. 17 2003 1075 1084
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1075-1084
    • Nguyen, B.T.1
  • 69
    • 15444366198 scopus 로고    scopus 로고
    • Relaxin stimulates protein kinase C zeta translocation: Requirement for cyclic adenosine 3′,5′-monophosphate production
    • B.T. Nguyen, and C.W. Dessauer Relaxin stimulates protein kinase C zeta translocation: requirement for cyclic adenosine 3′,5′-monophosphate production Mol. Endocrinol. 19 2005 1012 1023
    • (2005) Mol. Endocrinol. , vol.19 , pp. 1012-1023
    • Nguyen, B.T.1    Dessauer, C.W.2
  • 70
    • 59449108031 scopus 로고    scopus 로고
    • αi3 involves the C-terminal Arg752 and localization within membrane Raft microdomains
    • αi3 involves the C-terminal Arg752 and localization within membrane Raft microdomains Mol. Pharmacol. 75 2009 415 428
    • (2009) Mol. Pharmacol. , vol.75 , pp. 415-428
    • Halls, M.L.1
  • 71
    • 64549095557 scopus 로고    scopus 로고
    • Relaxin activates multiple cAMP signaling pathway profiles in different target cells
    • M.L. Halls, and et al. Relaxin activates multiple cAMP signaling pathway profiles in different target cells Ann. N.Y. Acad. Sci. 1160 2009 108 111
    • (2009) Ann. N.Y. Acad. Sci. , vol.1160 , pp. 108-111
    • Halls, M.L.1
  • 72
    • 0031771628 scopus 로고    scopus 로고
    • Demonstration of a relaxin receptor and relaxin-stimulated tyrosine phosphorylation in human lower uterine segment fibroblasts
    • S. Palejwala, and et al. Demonstration of a relaxin receptor and relaxin-stimulated tyrosine phosphorylation in human lower uterine segment fibroblasts Endocrinology 139 1998 1208 1212
    • (1998) Endocrinology , vol.139 , pp. 1208-1212
    • Palejwala, S.1
  • 73
    • 84862876898 scopus 로고    scopus 로고
    • Relaxin improves TNF-Alpha-induced endothelial dysfunction: The role of glucocorticoid receptor and phosphatidylinositol 3-kinase signalling
    • T. Dschietzig, and et al. Relaxin improves TNF-Alpha-induced endothelial dysfunction: the role of glucocorticoid receptor and phosphatidylinositol 3-kinase signalling Cardiovasc. Res. 95 2012 97 107
    • (2012) Cardiovasc. Res. , vol.95 , pp. 97-107
    • Dschietzig, T.1
  • 74
    • 34547630675 scopus 로고    scopus 로고
    • Reversal by relaxin of altered ileal spontaneous contractions in dystrophic (mdx) mice through a nitric oxide-mediated mechanism
    • M.C. Baccari, and et al. Reversal by relaxin of altered ileal spontaneous contractions in dystrophic (mdx) mice through a nitric oxide-mediated mechanism Am. J. Physiol. Regul. Integr. Comp. Physiol. 293 2007 R662 R668
    • (2007) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.293 , pp. R662-R668
    • Baccari, M.C.1
  • 75
    • 4544332842 scopus 로고    scopus 로고
    • Influence of relaxin on the neurally induced relaxant responses of the mouse gastric fundus
    • M.C. Baccari, and et al. Influence of relaxin on the neurally induced relaxant responses of the mouse gastric fundus Biol. Reprod. 71 2004 1325 1329
    • (2004) Biol. Reprod. , vol.71 , pp. 1325-1329
    • Baccari, M.C.1
  • 76
    • 0031810556 scopus 로고    scopus 로고
    • Relaxin activates the l-Arginine-nitric oxide pathway in vascular smooth muscle cells in culture
    • D. Bani, and et al. Relaxin activates the l-Arginine-nitric oxide pathway in vascular smooth muscle cells in culture Hypertension 31 1998 1240 1247
    • (1998) Hypertension , vol.31 , pp. 1240-1247
    • Bani, D.1
  • 77
    • 84884786369 scopus 로고    scopus 로고
    • Relaxin protects rat lungs from ischemia-reperfusion injury via inducible NO synthase: Role of ERK-1/2, PI3K, and forkhead transcription factor FKHRL1
    • K. Alexiou, and et al. Relaxin protects rat lungs from ischemia-reperfusion injury via inducible NO synthase: role of ERK-1/2, PI3K, and forkhead transcription factor FKHRL1 PLoS ONE 8 2013 e75592
    • (2013) PLoS ONE , vol.8 , pp. e75592
    • Alexiou, K.1
  • 78
    • 84921792573 scopus 로고    scopus 로고
    • Serelaxin-mediated signal transduction in human vascular cells: Bell-shaped concentration-response curves reflect differential coupling to G proteins
    • M. Sarwar, and et al. Serelaxin-mediated signal transduction in human vascular cells: bell-shaped concentration-response curves reflect differential coupling to G proteins Br. J. Pharmacol. 172 2015 1005 1019
    • (2015) Br. J. Pharmacol. , vol.172 , pp. 1005-1019
    • Sarwar, M.1
  • 79
    • 84866933093 scopus 로고    scopus 로고
    • Relaxin induces matrix-metalloproteinases-9 and -13 via RXFP1: Induction of MMP-9 involves the PI3K, ERK, Akt and PKC-zeta pathways
    • N. Ahmad, and et al. Relaxin induces matrix-metalloproteinases-9 and -13 via RXFP1: induction of MMP-9 involves the PI3K, ERK, Akt and PKC-zeta pathways Mol. Cell. Endocrinol. 363 2012 46 61
    • (2012) Mol. Cell. Endocrinol. , vol.363 , pp. 46-61
    • Ahmad, N.1
  • 80
    • 36448936383 scopus 로고    scopus 로고
    • TGFβ-SMAD signal transduction: Molecular specificity and functional flexibility
    • B. Schmierer, and C.S. Hill TGFβ-SMAD signal transduction: molecular specificity and functional flexibility Nat. Rev. Mol. Cell. Biol. 8 2007 970 982
    • (2007) Nat. Rev. Mol. Cell. Biol. , vol.8 , pp. 970-982
    • Schmierer, B.1    Hill, C.S.2
  • 81
    • 84863062546 scopus 로고    scopus 로고
    • Notch signaling may negatively regulate neonatal rat cardiac fibroblast-myofibroblast transformation
    • Y.H. Fan, and et al. Notch signaling may negatively regulate neonatal rat cardiac fibroblast-myofibroblast transformation Physiol. Res. 60 2011 739 748
    • (2011) Physiol. Res. , vol.60 , pp. 739-748
    • Fan, Y.H.1
  • 82
    • 84861995097 scopus 로고    scopus 로고
    • Notch receptor-ligand binding and activation: Insights from molecular studies
    • C.R. Chillakuri, and et al. Notch receptor-ligand binding and activation: insights from molecular studies Semin. Cell Dev. Biol. 23 2012 421 428
    • (2012) Semin. Cell Dev. Biol. , vol.23 , pp. 421-428
    • Chillakuri, C.R.1
  • 83
    • 40849096162 scopus 로고    scopus 로고
    • Cloning, expression, and functional characterization of relaxin receptor (leucine-rich repeat-containing G protein-coupled receptor 7) splice variants from human fetal membranes
    • A. Kern, and et al. Cloning, expression, and functional characterization of relaxin receptor (leucine-rich repeat-containing G protein-coupled receptor 7) splice variants from human fetal membranes Endocrinology 149 2008 1277 1294
    • (2008) Endocrinology , vol.149 , pp. 1277-1294
    • Kern, A.1
  • 84
    • 40849119953 scopus 로고    scopus 로고
    • Cooperative binding of insulin-like peptide 3 to a dimeric relaxin family peptide receptor 2
    • A.M. Svendsen, and et al. Cooperative binding of insulin-like peptide 3 to a dimeric relaxin family peptide receptor 2 Endocrinology 149 2008 1113 1120
    • (2008) Endocrinology , vol.149 , pp. 1113-1120
    • Svendsen, A.M.1
  • 85
    • 56049100923 scopus 로고    scopus 로고
    • Negative cooperativity in H2 relaxin binding to a dimeric relaxin family peptide receptor 1
    • A.M. Svendsen, and et al. Negative cooperativity in H2 relaxin binding to a dimeric relaxin family peptide receptor 1 Mol. Cell. Endocrinol. 296 2008 10 17
    • (2008) Mol. Cell. Endocrinol. , vol.296 , pp. 10-17
    • Svendsen, A.M.1
  • 86
    • 77949568522 scopus 로고    scopus 로고
    • Membrane receptors: Structure and function of the relaxin family peptide receptors
    • R.C. Kong, and et al. Membrane receptors: structure and function of the relaxin family peptide receptors Mol. Cell. Endocrinol. 320 2010 1 15
    • (2010) Mol. Cell. Endocrinol. , vol.320 , pp. 1-15
    • Kong, R.C.1
  • 87
    • 0030853563 scopus 로고    scopus 로고
    • Logical analysis of timing-dependent receptor signalling specificity: Application to the insulin receptor metabolic and mitogenic signalling pathways
    • R.M. Shymko, and et al. Logical analysis of timing-dependent receptor signalling specificity: application to the insulin receptor metabolic and mitogenic signalling pathways Biochem. J. 326 1997 463 469
    • (1997) Biochem. J. , vol.326 , pp. 463-469
    • Shymko, R.M.1
  • 88
    • 0141455506 scopus 로고    scopus 로고
    • Time course and dose response of relaxin-mediated renal vasodilation, hyperfiltration, and changes in plasma osmolality in conscious rats
    • L.A. Danielson, and K.P. Conrad Time course and dose response of relaxin-mediated renal vasodilation, hyperfiltration, and changes in plasma osmolality in conscious rats J. Appl. Physiol. 95 2003 1509 1514
    • (2003) J. Appl. Physiol. , vol.95 , pp. 1509-1514
    • Danielson, L.A.1    Conrad, K.P.2
  • 89
    • 14144250653 scopus 로고    scopus 로고
    • Effects of relaxin on systemic arterial hemodynamics and mechanical properties in conscious rats: Sex dependency and dose response
    • D.O. Debrah, and et al. Effects of relaxin on systemic arterial hemodynamics and mechanical properties in conscious rats: sex dependency and dose response J. Appl. Physiol. 98 2005 1013 1020
    • (2005) J. Appl. Physiol. , vol.98 , pp. 1013-1020
    • Debrah, D.O.1
  • 90
    • 65249190276 scopus 로고    scopus 로고
    • Relaxin for the treatment of patients with acute heart failure (Pre-RELAX-AHF): A multicentre, randomised, placebo-controlled, parallel-group, dose-finding Phase IIb study
    • J.R. Teerlink, and et al. Relaxin for the treatment of patients with acute heart failure (Pre-RELAX-AHF): a multicentre, randomised, placebo-controlled, parallel-group, dose-finding Phase IIb study Lancet 373 2009 1429 1439
    • (2009) Lancet , vol.373 , pp. 1429-1439
    • Teerlink, J.R.1
  • 91
    • 84903773477 scopus 로고    scopus 로고
    • Relaxin requires the angiotensin II type 2 receptor to abrogate renal interstitial fibrosis
    • B.S. Chow, and et al. Relaxin requires the angiotensin II type 2 receptor to abrogate renal interstitial fibrosis Kidney Int. 86 2014 75 85
    • (2014) Kidney Int. , vol.86 , pp. 75-85
    • Chow, B.S.1
  • 92
    • 18244407290 scopus 로고    scopus 로고
    • Cardiovascular and renal regulation by the angiotensin type 2 receptor: The AT2 receptor comes of age
    • R.M. Carey Cardiovascular and renal regulation by the angiotensin type 2 receptor: the AT2 receptor comes of age Hypertension 45 2005 840 844
    • (2005) Hypertension , vol.45 , pp. 840-844
    • Carey, R.M.1
  • 93
    • 56149096807 scopus 로고    scopus 로고
    • AT2 receptors: Functional relevance in cardiovascular disease
    • E.S. Jones, and et al. AT2 receptors: functional relevance in cardiovascular disease Pharmacol. Ther. 120 2008 292 316
    • (2008) Pharmacol. Ther. , vol.120 , pp. 292-316
    • Jones, E.S.1
  • 94
    • 84904514461 scopus 로고    scopus 로고
    • Serelaxin is a more efficacious antifibrotic than enalapril in an experimental model of heart disease
    • C.S. Samuel, and et al. Serelaxin is a more efficacious antifibrotic than enalapril in an experimental model of heart disease Hypertension 64 2014 315 322
    • (2014) Hypertension , vol.64 , pp. 315-322
    • Samuel, C.S.1
  • 95
    • 84871690183 scopus 로고    scopus 로고
    • Combination therapy with relaxin and methylprednisolone augments the effects of either treatment alone in inhibiting subepithelial fibrosis in an experimental model of allergic airways disease
    • S.G. Royce, and et al. Combination therapy with relaxin and methylprednisolone augments the effects of either treatment alone in inhibiting subepithelial fibrosis in an experimental model of allergic airways disease Clin. Sci. 124 2013 41 51
    • (2013) Clin. Sci. , vol.124 , pp. 41-51
    • Royce, S.G.1
  • 96
    • 84922479871 scopus 로고    scopus 로고
    • Characterization of a novel model incorporating airway epithelial damage and related fibrosis to the pathogenesis of asthma
    • S.G. Royce, and et al. Characterization of a novel model incorporating airway epithelial damage and related fibrosis to the pathogenesis of asthma Lab. Invest. 94 2014 1326 1339
    • (2014) Lab. Invest. , vol.94 , pp. 1326-1339
    • Royce, S.G.1
  • 97
    • 69149094362 scopus 로고    scopus 로고
    • Stem cell therapy for cardiac repair: Benefits and barriers
    • S.J. Joggerst, and A.K. Hatzopoulos Stem cell therapy for cardiac repair: benefits and barriers Expert Rev. Mol. Med. 11 2009 e20
    • (2009) Expert Rev. Mol. Med. , vol.11 , pp. e20
    • Joggerst, S.J.1    Hatzopoulos, A.K.2
  • 99
    • 84895069470 scopus 로고    scopus 로고
    • Cell-based therapies for the acute respiratory distress syndrome
    • T. Maron-Gutierrez, and et al. Cell-based therapies for the acute respiratory distress syndrome Curr. Opin. Crit. Care 20 2014 122 131
    • (2014) Curr. Opin. Crit. Care , vol.20 , pp. 122-131
    • Maron-Gutierrez, T.1
  • 100
    • 3042719731 scopus 로고    scopus 로고
    • Molecular and cellular events at the site of myocardial infarction: From the perspective of rebuilding myocardial tissue
    • L. Lu, and et al. Molecular and cellular events at the site of myocardial infarction: from the perspective of rebuilding myocardial tissue Biochem. Biophys. Res. Commun. 320 2004 907 913
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 907-913
    • Lu, L.1
  • 101
    • 35649009903 scopus 로고    scopus 로고
    • Paracrine effects of transplanted myoblasts and relaxin on post-infarction heart remodelling
    • L. Formigli, and et al. Paracrine effects of transplanted myoblasts and relaxin on post-infarction heart remodelling J. Cell. Mol. Med. 11 2007 1087 1100
    • (2007) J. Cell. Mol. Med. , vol.11 , pp. 1087-1100
    • Formigli, L.1
  • 102
    • 84937548277 scopus 로고    scopus 로고
    • Combination therapy of mesenchymal stem cells and serelaxin effectively attenuates renal fibrosis in obstructive nephropathy
    • B.M. Huuskes, and et al. Combination therapy of mesenchymal stem cells and serelaxin effectively attenuates renal fibrosis in obstructive nephropathy FASEB J. 29 2015 540 553
    • (2015) FASEB J. , vol.29 , pp. 540-553
    • Huuskes, B.M.1
  • 103
    • 84942617492 scopus 로고    scopus 로고
    • Mesenchymal stem cells and serelaxin synergistically abrogate established airway fibrosis in an experimental model of chronic allergic airways disease
    • S.G. Royce, and et al. Mesenchymal stem cells and serelaxin synergistically abrogate established airway fibrosis in an experimental model of chronic allergic airways disease Stem Cell Res. 15 2015 495 505
    • (2015) Stem Cell Res. , vol.15 , pp. 495-505
    • Royce, S.G.1
  • 104
    • 80054824082 scopus 로고    scopus 로고
    • The minimal active structure of human relaxin-2
    • M.A. Hossain, and et al. The minimal active structure of human relaxin-2 J. Biol. Chem. 286 2011 37555 37565
    • (2011) J. Biol. Chem. , vol.286 , pp. 37555-37565
    • Hossain, M.A.1
  • 105
    • 84879636804 scopus 로고    scopus 로고
    • Identification and optimization of small-molecule agonists of the human relaxin hormone receptor RXFP1
    • J. Xiao, and et al. Identification and optimization of small-molecule agonists of the human relaxin hormone receptor RXFP1 Nat. Commun. 4 2013 1953
    • (2013) Nat. Commun. , vol.4 , pp. 1953
    • Xiao, J.1
  • 106
    • 1442311168 scopus 로고    scopus 로고
    • Where is the evidence that animal research benefits humans?
    • P. Pound, and et al. Where is the evidence that animal research benefits humans? BMJ 328 2004 514 517
    • (2004) BMJ , vol.328 , pp. 514-517
    • Pound, P.1
  • 107
    • 62749199801 scopus 로고    scopus 로고
    • Why animal studies are often poor predictors of human reactions to exposure
    • M.B. Bracken Why animal studies are often poor predictors of human reactions to exposure J. R. Soc. Med. 102 2009 120 122
    • (2009) J. R. Soc. Med. , vol.102 , pp. 120-122
    • Bracken, M.B.1
  • 108
    • 27744469670 scopus 로고    scopus 로고
    • The relaxin gene knockout mouse: A model of progressive scleroderma
    • C.S. Samuel, and et al. The relaxin gene knockout mouse: a model of progressive scleroderma J. Invest. Dermatol. 125 2005 692 699
    • (2005) J. Invest. Dermatol. , vol.125 , pp. 692-699
    • Samuel, C.S.1
  • 109
    • 84856264568 scopus 로고    scopus 로고
    • A randomized, placebo-controlled clinical trial on the effects of recombinant human relaxin on tooth movement and short-term stability
    • S.P. McGorray, and et al. A randomized, placebo-controlled clinical trial on the effects of recombinant human relaxin on tooth movement and short-term stability Am. J. Orthod. Dentofacial Orthop. 141 2012 196 203
    • (2012) Am. J. Orthod. Dentofacial Orthop. , vol.141 , pp. 196-203
    • McGorray, S.P.1
  • 110
    • 23644442930 scopus 로고    scopus 로고
    • Use of relaxin in orthodontics
    • D.R. Stewart, and et al. Use of relaxin in orthodontics Ann. N. Y. Acad. Sci. 1041 2005 379 387
    • (2005) Ann. N. Y. Acad. Sci. , vol.1041 , pp. 379-387
    • Stewart, D.R.1
  • 111
    • 84860381967 scopus 로고    scopus 로고
    • Effects of relaxin on relapse and periodontal tissue remodeling after experimental tooth movement in rats
    • Y. Hirate, and et al. Effects of relaxin on relapse and periodontal tissue remodeling after experimental tooth movement in rats Connect. Tissue Res. 53 2012 207 219
    • (2012) Connect. Tissue Res. , vol.53 , pp. 207-219
    • Hirate, Y.1
  • 112
    • 64549133824 scopus 로고    scopus 로고
    • A randomized, double-blind, placebo-controlled trial of relaxin for cervical ripening in post-delivery date pregnancies
    • G. Weiss, and et al. A randomized, double-blind, placebo-controlled trial of relaxin for cervical ripening in post-delivery date pregnancies Ann. N. Y. Acad. Sci. 1160 2009 385 386
    • (2009) Ann. N. Y. Acad. Sci. , vol.1160 , pp. 385-386
    • Weiss, G.1
  • 113
    • 84922356169 scopus 로고    scopus 로고
    • Synthetic covalently linked dimeric form of H2 relaxin retains native RXFP1 activity and has improved in vitro serum stability
    • V.B. Nair, and et al. Synthetic covalently linked dimeric form of H2 relaxin retains native RXFP1 activity and has improved in vitro serum stability Biomed. Res. Int. 2015 2015 731852
    • (2015) Biomed. Res. Int. , vol.2015 , pp. 731852
    • Nair, V.B.1
  • 114
    • 80955127759 scopus 로고    scopus 로고
    • The chemically synthesized human relaxin-2 analog, B-R13/17K H2, is an RXFP1 antagonist
    • M.A. Hossain, and et al. The chemically synthesized human relaxin-2 analog, B-R13/17K H2, is an RXFP1 antagonist Amino Acids 39 2010 409 416
    • (2010) Amino Acids , vol.39 , pp. 409-416
    • Hossain, M.A.1


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