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Volumn 35, Issue 6, 2013, Pages 825-832

Altered peptidase activities in thyroid neoplasia and hyperplasia

Author keywords

[No Author keywords available]

Indexed keywords

5 OXOPROLYL PEPTIDASE; AMINOPEPTIDASE B; ASPARTYL AMINOPEPTIDASE; DIPEPTIDYL PEPTIDASE IV; MICROSOMAL AMINOPEPTIDASE; PEPTIDASE; PROLYL ENDOPEPTIDASE;

EID: 84896944734     PISSN: 02780240     EISSN: 18758630     Source Type: Journal    
DOI: 10.1155/2013/970736     Document Type: Article
Times cited : (11)

References (54)
  • 1
    • 79955675599 scopus 로고    scopus 로고
    • Approach to the patient with nontoxic multinodular goiter
    • 2-s2.0-79955675599 10.1210/jc.2010-2583
    • Bahn R. S., Castro M. R., Approach to the patient with nontoxic multinodular goiter. Journal of Clinical Endocrinology and Metabolism 2011 96 5 1202 1212 2-s2.0-79955675599 10.1210/jc.2010-2583
    • (2011) Journal of Clinical Endocrinology and Metabolism , vol.96 , Issue.5 , pp. 1202-1212
    • Bahn, R.S.1    Castro, M.R.2
  • 3
    • 84867965390 scopus 로고    scopus 로고
    • Pitfalls in the diagnosis of follicular epithelial proliferations of the thyroid
    • 10.1097/PAP.0b013e318271a5ac
    • Mete O., Asa S. L., Pitfalls in the diagnosis of follicular epithelial proliferations of the thyroid. Advances in Anatomic Pathology 2012 19 6 363 373 10.1097/PAP.0b013e318271a5ac
    • (2012) Advances in Anatomic Pathology , vol.19 , Issue.6 , pp. 363-373
    • Mete, O.1    Asa, S.L.2
  • 4
    • 84896987685 scopus 로고    scopus 로고
    • Histological diagnosis of the thyroid disease using ultrasound-guided core biopsies
    • López J. I., Zabala R., del Cura J. L., Histological diagnosis of the thyroid disease using ultrasound-guided core biopsies. European Thyroid Journal 2013 2 29 36
    • (2013) European Thyroid Journal , vol.2 , pp. 29-36
    • López, J.I.1    Zabala, R.2    Del Cura, J.L.3
  • 5
    • 79951513849 scopus 로고    scopus 로고
    • Papillary thyroid carcinoma variants
    • 2-s2.0-79951513849 10.1007/s12105-010-0236-9
    • Lloyd R. V., Buehler D., Khanafshar E., Papillary thyroid carcinoma variants. Head and Neck Pathology 2011 5 1 51 56 2-s2.0-79951513849 10.1007/s12105-010-0236-9
    • (2011) Head and Neck Pathology , vol.5 , Issue.1 , pp. 51-56
    • Lloyd, R.V.1    Buehler, D.2    Khanafshar, E.3
  • 6
    • 79953293940 scopus 로고    scopus 로고
    • Papillary thyroid carcinoma: An update
    • supplement 2 10.1038/modpathol.2010.129
    • LiVolsi V. A., Papillary thyroid carcinoma: an update. Modern Pathology 2011 24 supplement 2 S1 S9 10.1038/modpathol.2010.129
    • (2011) Modern Pathology , vol.24
    • Livolsi, V.A.1
  • 8
    • 4544273167 scopus 로고    scopus 로고
    • Regulatory role of membrane-bound peptidases in the progression of gynecologic malignancies
    • 2-s2.0-4544273167 10.1515/BC.2004.084
    • Ino K., Shibata K., Kajiyama H., Kikkawa F., Mizutani S., Regulatory role of membrane-bound peptidases in the progression of gynecologic malignancies. Biological Chemistry 2004 385 8 683 690 2-s2.0-4544273167 10.1515/BC.2004.084
    • (2004) Biological Chemistry , vol.385 , Issue.8 , pp. 683-690
    • Ino, K.1    Shibata, K.2    Kajiyama, H.3    Kikkawa, F.4    Mizutani, S.5
  • 10
    • 0035118889 scopus 로고    scopus 로고
    • Ectopeptidases in pathophysiology
    • Antczak C., De Meester I., Bauvois B., Ectopeptidases in pathophysiology. Bioessays 2001 23 3 251 260
    • (2001) Bioessays , vol.23 , Issue.3 , pp. 251-260
    • Antczak, C.1    De Meester, I.2    Bauvois, B.3
  • 11
    • 33749188873 scopus 로고    scopus 로고
    • Inverse relationships between the expression of MMP-7 and MMP-11 and predictors of poor prognosis of papillary thyroid carcinoma
    • 2-s2.0-33749188873 10.1080/00313020600922496
    • Ito Y., Yoshida H., Kakudo K., Nakamura Y., Kuma K., Miyauchi A., Inverse relationships between the expression of MMP-7 and MMP-11 and predictors of poor prognosis of papillary thyroid carcinoma. Pathology 2006 38 5 421 425 2-s2.0-33749188873 10.1080/00313020600922496
    • (2006) Pathology , vol.38 , Issue.5 , pp. 421-425
    • Ito, Y.1    Yoshida, H.2    Kakudo, K.3    Nakamura, Y.4    Kuma, K.5    Miyauchi, A.6
  • 12
    • 0034501336 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the thyroid
    • 2-s2.0-0034501336
    • Kraiem Z., Korem S., Matrix metalloproteinases and the thyroid. Thyroid 2000 10 12 1061 1069 2-s2.0-0034501336
    • (2000) Thyroid , vol.10 , Issue.12 , pp. 1061-1069
    • Kraiem, Z.1    Korem, S.2
  • 14
    • 0035115332 scopus 로고    scopus 로고
    • Protein expression of matrix metalloproteinases 2 and 9 and tissue inhibitors of metalloproteinase 1 and 2 in papillary thyroid carcinomas
    • 2-s2.0-0035115332 10.1007/s004280000286
    • Maeta H., Ohgi S., Terada T., Protein expression of matrix metalloproteinases 2 and 9 and tissue inhibitors of metalloproteinase 1 and 2 in papillary thyroid carcinomas. Virchows Archiv 2001 438 2 121 128 2-s2.0-0035115332 10.1007/s004280000286
    • (2001) Virchows Archiv , vol.438 , Issue.2 , pp. 121-128
    • Maeta, H.1    Ohgi, S.2    Terada, T.3
  • 15
    • 84864479766 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase-2 and its tissue inhibitor-2 in fetal and neoplastic thyroid tissue and their significance as diagnostic and prognostic markers in papillary carcinoma
    • Marecko I., Cvejic D., Tatic S., Dragutinovic V., Paunovic I., Savin S., Expression of matrix metalloproteinase-2 and its tissue inhibitor-2 in fetal and neoplastic thyroid tissue and their significance as diagnostic and prognostic markers in papillary carcinoma. Cancer Biomark 2011-2012 11 1 49 58
    • (2011) Cancer Biomark , vol.11 , Issue.1 , pp. 49-58
    • Marecko, I.1    Cvejic, D.2    Tatic, S.3    Dragutinovic, V.4    Paunovic, I.5    Savin, S.6
  • 16
    • 39449100808 scopus 로고    scopus 로고
    • Utility of malignancy markers in fine-needle aspiration cytology of thyroid nodules: Comparison of Hector Battifora mesothelial antigen-1, thyroid peroxidase and dipeptidyl aminopeptidase IV
    • 2-s2.0-39449100808 10.1038/sj.bjc.6604194
    • De Micco C., Savchenko V., Giorgi R., Sebag F., Henry J.-F., Utility of malignancy markers in fine-needle aspiration cytology of thyroid nodules: comparison of Hector Battifora mesothelial antigen-1, thyroid peroxidase and dipeptidyl aminopeptidase IV. British Journal of Cancer 2008 98 4 818 823 2-s2.0-39449100808 10.1038/sj.bjc.6604194
    • (2008) British Journal of Cancer , vol.98 , Issue.4 , pp. 818-823
    • De Micco, C.1    Savchenko, V.2    Giorgi, R.3    Sebag, F.4    Henry, J.-F.5
  • 18
    • 0029872324 scopus 로고    scopus 로고
    • Differential expression of dipeptidyl peptidase IV (CD26) and thyroid peroxidase in neoplastic thyroid tissues
    • 2-s2.0-0029872324
    • Umeki K., Tanaka T., Yamamoto I., Aratake Y., Kotani T., Sakamoto F., Noguchi S., Ohtaki S., Differential expression of dipeptidyl peptidase IV (CD26) and thyroid peroxidase in neoplastic thyroid tissues. Endocrine Journal 1996 43 1 53 60 2-s2.0-0029872324
    • (1996) Endocrine Journal , vol.43 , Issue.1 , pp. 53-60
    • Umeki, K.1    Tanaka, T.2    Yamamoto, I.3    Aratake, Y.4    Kotani, T.5    Sakamoto, F.6    Noguchi, S.7    Ohtaki, S.8
  • 19
    • 44949168668 scopus 로고    scopus 로고
    • Acid, basic, and neutral peptidases present different profiles in chromophobe renal cell carcinoma and in oncocytoma
    • 2-s2.0-44949168668 10.1152/ajprenal.00469.2007
    • Blanco L., Larrinaga G., Pérez I., López J. I., Gil J., Agirregoitia E., Varona A., Acid, basic, and neutral peptidases present different profiles in chromophobe renal cell carcinoma and in oncocytoma. American Journal of Physiology 2008 294 4 F850 F858 2-s2.0-44949168668 10.1152/ajprenal.00469.2007
    • (2008) American Journal of Physiology , vol.294 , Issue.4
    • Blanco, L.1    Larrinaga, G.2    Pérez, I.3    López, J.I.4    Gil, J.5    Agirregoitia, E.6    Varona, A.7
  • 20
    • 70349331392 scopus 로고    scopus 로고
    • Increased APN/CD13 and acid aminopeptidase activities in head and neck squamous cell carcinoma
    • 2-s2.0-70349331392 10.1002/hed.21099
    • Pérez I., Varona A., Blanco L., Gil J., Santaolalla F., Zabala A., Ibarguen A. M., Irazusta J., Larrinaga G., Increased APN/CD13 and acid aminopeptidase activities in head and neck squamous cell carcinoma. Head and Neck 2009 31 10 1335 1340 2-s2.0-70349331392 10.1002/hed.21099
    • (2009) Head and Neck , vol.31 , Issue.10 , pp. 1335-1340
    • Pérez, I.1    Varona, A.2    Blanco, L.3    Gil, J.4    Santaolalla, F.5    Zabala, A.6    Ibarguen, A.M.7    Irazusta, J.8    Larrinaga, G.9
  • 21
    • 33846864246 scopus 로고    scopus 로고
    • Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma
    • 2-s2.0-33846864246 10.1152/ajprenal.00148.2006
    • Varona A., Blanco L., López J. I., Gil J., Agirregoitia E., Irazusta J., Larrinaga G., Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma. American Journal of Physiology 2007 292 2 F780 F788 2-s2.0-33846864246 10.1152/ajprenal.00148.2006
    • (2007) American Journal of Physiology , vol.292 , Issue.2
    • Varona, A.1    Blanco, L.2    López, J.I.3    Gil, J.4    Agirregoitia, E.5    Irazusta, J.6    Larrinaga, G.7
  • 25
    • 34548481975 scopus 로고    scopus 로고
    • Aspartyl, arginyl and alanyl aminopeptidase activities in the hippocampus and hypothalamus of streptozotocin-induced diabetic rats
    • 2-s2.0-34548481975 10.1016/j.brainres.2007.07.026
    • Zambotti-Villela L., Yamasaki S. C., Villarroel J. S., Alponti R. F., Silveira P. F., Aspartyl, arginyl and alanyl aminopeptidase activities in the hippocampus and hypothalamus of streptozotocin-induced diabetic rats. Brain Research 2007 1170 112 118 2-s2.0-34548481975 10.1016/j.brainres.2007.07.026
    • (2007) Brain Research , vol.1170 , pp. 112-118
    • Zambotti-Villela, L.1    Yamasaki, S.C.2    Villarroel, J.S.3    Alponti, R.F.4    Silveira, P.F.5
  • 26
    • 0018750650 scopus 로고
    • Post-proline cleaving enzyme. Synthesis of a new fluorogenic substrate and distribution of the endopeptidase in rat tissues and body fluids of man
    • 2-s2.0-0018750650
    • Yoshimoto T., Ogita K., Walter R., Post-proline cleaving enzyme. Synthesis of a new fluorogenic substrate and distribution of the endopeptidase in rat tissues and body fluids of man. Biochimica et Biophysica Acta 1979 569 2 184 192 2-s2.0-0018750650
    • (1979) Biochimica et Biophysica Acta , vol.569 , Issue.2 , pp. 184-192
    • Yoshimoto, T.1    Ogita, K.2    Walter, R.3
  • 27
    • 0025008623 scopus 로고
    • Characterization of aminopeptidases in human kidney soluble fraction
    • 2-s2.0-0025008623 10.1016/0009-8981(90)90336-Q
    • Mantle D., Lauffat B., McDermott J., Gibson A., Characterization of aminopeptidases in human kidney soluble fraction. Clinica Chimica Acta 1990 187 2 105 113 2-s2.0-0025008623 10.1016/0009-8981(90)90336-Q
    • (1990) Clinica Chimica Acta , vol.187 , Issue.2 , pp. 105-113
    • Mantle, D.1    Lauffat, B.2    McDermott, J.3    Gibson, A.4
  • 28
    • 0035755738 scopus 로고    scopus 로고
    • Interactions among challenges of hydromineral balance, angiotensin-converting enzyme, and cystine aminopeptidase
    • 2-s2.0-0035755738
    • Silveira P. F., Irazusta J., Gil J., Agirregoitia N., Casis L., Interactions among challenges of hydromineral balance, angiotensin-converting enzyme, and cystine aminopeptidase. Peptides 2001 22 12 2137 2144 2-s2.0-0035755738
    • (2001) Peptides , vol.22 , Issue.12 , pp. 2137-2144
    • Silveira, P.F.1    Irazusta, J.2    Gil, J.3    Agirregoitia, N.4    Casis, L.5
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • 2-s2.0-0017184389
    • Bradford M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Analytical Biochemistry 1976 72 1-2 248 254 2-s2.0-0017184389
    • (1976) Analytical Biochemistry , vol.72 , Issue.1-2 , pp. 248-254
    • Bradford, M.M.1
  • 32
    • 0025872297 scopus 로고
    • Dipeptidyl peptidase IV, prolyl endopeptidase and cathepsin B activities in primary human lung tumours and lung parenchyma
    • 2-s2.0-0025872297
    • Sedo A., Krepela E., Kasafirek E., Dipeptidyl peptidase IV, prolyl endopeptidase and cathepsin B activities in primary human lung tumours and lung parenchyma. Journal of Cancer Research and Clinical Oncology 1991 117 3 249 253 2-s2.0-0025872297
    • (1991) Journal of Cancer Research and Clinical Oncology , vol.117 , Issue.3 , pp. 249-253
    • Sedo, A.1    Krepela, E.2    Kasafirek, E.3
  • 33
    • 17144404555 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV and related enzymes in cell biology and liver disorders
    • 2-s2.0-17144404555 10.1042/CS20040302
    • Gorrell M. D., Dipeptidyl peptidase IV and related enzymes in cell biology and liver disorders. Clinical Science 2005 108 4 277 292 2-s2.0-17144404555 10.1042/CS20040302
    • (2005) Clinical Science , vol.108 , Issue.4 , pp. 277-292
    • Gorrell, M.D.1
  • 34
    • 0346219110 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV activity and/or structure homologues (DASH) and their substrates in cancer
    • 2-s2.0-0346219110 10.1016/S1357-2725(03)00262-0
    • Bušek P., Malík R., Šedo A., Dipeptidyl peptidase IV activity and/or structure homologues (DASH) and their substrates in cancer. International Journal of Biochemistry and Cell Biology 2004 36 3 408 421 2-s2.0-0346219110 10.1016/S1357-2725(03)00262-0
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , Issue.3 , pp. 408-421
    • Bušek, P.1    Malík, R.2    Šedo, A.3
  • 35
    • 0037190118 scopus 로고    scopus 로고
    • Aminopeptidase inhibitors bestatin and actinonin inhibit cell proliferation of myeloma cells predominantly by intracellular interactions
    • 2-s2.0-0037190118 10.1016/S0304-3835(02)00086-1
    • Grujić M., Renko M., Aminopeptidase inhibitors bestatin and actinonin inhibit cell proliferation of myeloma cells predominantly by intracellular interactions. Cancer Letters 2002 182 2 113 119 2-s2.0-0037190118 10.1016/S0304-3835(02)00086-1
    • (2002) Cancer Letters , vol.182 , Issue.2 , pp. 113-119
    • Grujić, M.1    Renko, M.2
  • 37
    • 0347594161 scopus 로고    scopus 로고
    • Of peptides and peptidases: The role of cell surface peptidases in cancer
    • 2-s2.0-0347594161
    • Nanus D. M., Of peptides and peptidases: the role of cell surface peptidases in cancer. Clinical Cancer Research 2003 9 17 6307 6309 2-s2.0-0347594161
    • (2003) Clinical Cancer Research , vol.9 , Issue.17 , pp. 6307-6309
    • Nanus, D.M.1
  • 38
    • 33846887537 scopus 로고    scopus 로고
    • The puromycin-sensitive aminopeptidase. Role in neurological, reproductive, inmunological and proliferative disorders
    • New York, NY, USA Kluwer Academic/Plenum Press
    • Thompson M. W., Hersh L. B., Hooper N. M., Lendeckel U., The puromycin-sensitive aminopeptidase. Role in neurological, reproductive, inmunological and proliferative disorders. Aminopeptidases in Biology and Disease 2004 New York, NY, USA Kluwer Academic/Plenum Press 1 15
    • (2004) Aminopeptidases in Biology and Disease , pp. 1-15
    • Thompson, M.W.1    Hersh, L.B.2    Hooper, N.M.3    Lendeckel, U.4
  • 39
    • 0031913776 scopus 로고    scopus 로고
    • CDNA cloning of mouse prolyl endopeptidase and its involvement in DNA synthesis by Swiss 3T3 cells
    • 2-s2.0-0031913776
    • Ishino T., Ohtsuki S., Homma K., Natori S., cDNA cloning of mouse prolyl endopeptidase and its involvement in DNA synthesis by Swiss 3T3 cells. Journal of Biochemistry 1998 123 3 540 545 2-s2.0-0031913776
    • (1998) Journal of Biochemistry , vol.123 , Issue.3 , pp. 540-545
    • Ishino, T.1    Ohtsuki, S.2    Homma, K.3    Natori, S.4
  • 40
    • 53249090063 scopus 로고    scopus 로고
    • Expression and traffic of cellular prolyl oligopeptidase are regulated during cerebellar granule cell differentiation, maturation, and aging
    • 2-s2.0-53249090063 10.1016/j.neuroscience.2008.06.072
    • Moreno-Baylach M. J., Felipo V., Männistö P. T., García-Horsman J. A., Expression and traffic of cellular prolyl oligopeptidase are regulated during cerebellar granule cell differentiation, maturation, and aging. Neuroscience 2008 156 3 580 585 2-s2.0-53249090063 10.1016/j.neuroscience.2008.06.072
    • (2008) Neuroscience , vol.156 , Issue.3 , pp. 580-585
    • Moreno-Baylach, M.J.1    Felipo, V.2    Männistö, P.T.3    García-Horsman, J.A.4
  • 42
    • 84860871900 scopus 로고    scopus 로고
    • Sequential expression, activity and nuclear localization of prolyl oligopeptidase protein in the developing rat brain
    • 10.1111/j.1476-5381.2012.01846.x
    • Hannula M. J., Männistö P. T., Myöhänen T. T., Sequential expression, activity and nuclear localization of prolyl oligopeptidase protein in the developing rat brain. British Journal of Pharmacology 2012 166 3 1097 1113 10.1111/j.1476-5381.2012.01846.x
    • (2012) British Journal of Pharmacology , vol.166 , Issue.3 , pp. 1097-1113
    • Hannula, M.J.1    Männistö, P.T.2    Myöhänen, T.T.3
  • 44
    • 0042266355 scopus 로고    scopus 로고
    • Leukotriene A4 signaling, inflammation, and cancer
    • 2-s2.0-0042266355
    • DuBois R. N., Leukotriene A4 signaling, inflammation, and cancer. Journal of the National Cancer Institute 2003 95 14 1028 1029 2-s2.0-0042266355
    • (2003) Journal of the National Cancer Institute , vol.95 , Issue.14 , pp. 1028-1029
    • Dubois, R.N.1
  • 45
    • 0043095584 scopus 로고    scopus 로고
    • Leukotriene A4 hydrolase in rat and human esophageal adenocarcinomas and inhibitory effects of bestatin
    • 2-s2.0-0043095584
    • Chen X., Li N., Wang S., Hong J., Jiao X., Krasna M. J., Beer D. G., Yang C. S., Leukotriene A4 hydrolase in rat and human esophageal adenocarcinomas and inhibitory effects of bestatin. Journal of the National Cancer Institute 2003 95 14 1053 1061 2-s2.0-0043095584
    • (2003) Journal of the National Cancer Institute , vol.95 , Issue.14 , pp. 1053-1061
    • Chen, X.1    Li, N.2    Wang, S.3    Hong, J.4    Jiao, X.5    Krasna, M.J.6    Beer, D.G.7    Yang, C.S.8
  • 46
    • 51849135397 scopus 로고    scopus 로고
    • The renin-angiotensin system and malignancy
    • 2-s2.0-51849135397 10.1093/carcin/bgn171
    • Ager E. I., Neo J., Christophi C., The renin-angiotensin system and malignancy. Carcinogenesis 2008 29 9 1675 1684 2-s2.0-51849135397 10.1093/carcin/bgn171
    • (2008) Carcinogenesis , vol.29 , Issue.9 , pp. 1675-1684
    • Ager, E.I.1    Neo, J.2    Christophi, C.3
  • 48
    • 0036125025 scopus 로고    scopus 로고
    • The biology of the opioid growth factor receptor (OGFr)
    • 2-s2.0-0036125025 10.1016/S0165-0173(01)00160-6
    • Zagon I. S., Verderame M. F., McLaughlin P. J., The biology of the opioid growth factor receptor (OGFr). Brain Research Reviews 2002 38 3 351 376 2-s2.0-0036125025 10.1016/S0165-0173(01)00160-6
    • (2002) Brain Research Reviews , vol.38 , Issue.3 , pp. 351-376
    • Zagon, I.S.1    Verderame, M.F.2    McLaughlin, P.J.3
  • 49
    • 0031884518 scopus 로고    scopus 로고
    • Aminopeptidase B: A processing enzyme secreted and associated with the plasma membrane of rat pheochromocytoma (PC12) cells
    • 2-s2.0-0031884518
    • Balogh A., Cadel S., Foulon T., Picart R., Garabedian A. D., Rousselet A., Tougard C., Cohen P., Aminopeptidase B: a processing enzyme secreted and associated with the plasma membrane of rat pheochromocytoma (PC12) cells. Journal of Cell Science 1998 111 2 161 169 2-s2.0-0031884518
    • (1998) Journal of Cell Science , vol.111 , Issue.2 , pp. 161-169
    • Balogh, A.1    Cadel, S.2    Foulon, T.3    Picart, R.4    Garabedian, A.D.5    Rousselet, A.6    Tougard, C.7    Cohen, P.8
  • 50
    • 33846203261 scopus 로고    scopus 로고
    • On the role of prolyl oligopeptidase in health and disease
    • 10.1016/j.npep.2006.10.004
    • García-Hornsman J. A., Männistö P. T., Venäläinen J. I., On the role of prolyl oligopeptidase in health and disease. Neuropeptides 2007 41 1 1 24 10.1016/j.npep.2006.10.004
    • (2007) Neuropeptides , vol.41 , Issue.1 , pp. 1-24
    • García-Hornsman, J.A.1    Männistö, P.T.2    Venäläinen, J.I.3
  • 51
    • 0036799813 scopus 로고    scopus 로고
    • Soluble metalloendopeptidases and neuroendocrine signaling
    • 2-s2.0-0036799813 10.1210/er.2001-0032
    • Shrimpton C. N., Smith A. I., Lew R. A., Soluble metalloendopeptidases and neuroendocrine signaling. Endocrine Reviews 2002 23 5 647 664 2-s2.0-0036799813 10.1210/er.2001-0032
    • (2002) Endocrine Reviews , vol.23 , Issue.5 , pp. 647-664
    • Shrimpton, C.N.1    Smith, A.I.2    Lew, R.A.3
  • 52
    • 33748925956 scopus 로고    scopus 로고
    • An intracrine view of angiogenesis
    • 2-s2.0-33748925956 10.1002/bies.20459
    • Re R. N., Cook J. L., An intracrine view of angiogenesis. BioEssays 2006 28 9 943 953 2-s2.0-33748925956 10.1002/bies.20459
    • (2006) BioEssays , vol.28 , Issue.9 , pp. 943-953
    • Re, R.N.1    Cook, J.L.2
  • 53
    • 29244463006 scopus 로고    scopus 로고
    • The intracrine hypothesis: An update
    • 2-s2.0-29244463006 10.1016/j.regpep.2005.09.012
    • Re R. N., Cook J. L., The intracrine hypothesis: an update. Regulatory Peptides 2006 133 1-3 1 9 2-s2.0-29244463006 10.1016/j.regpep.2005.09.012
    • (2006) Regulatory Peptides , vol.133 , Issue.1-3 , pp. 1-9
    • Re, R.N.1    Cook, J.L.2
  • 54
    • 81255157608 scopus 로고    scopus 로고
    • Noncanonical intracrine action
    • 2-s2.0-81255157608 10.1016/j.jash.2011.07.001
    • Re R. N., Cook J. L., Noncanonical intracrine action. Journal of the American Society of Hypertension 2011 5 6 435 448 2-s2.0-81255157608 10.1016/j.jash.2011.07.001
    • (2011) Journal of the American Society of Hypertension , vol.5 , Issue.6 , pp. 435-448
    • Re, R.N.1    Cook, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.