-
1
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0029156967
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Direct stereological estimation of three-dimensional connectivity in rat vertebrae: effect of estrogen, etidronate and risedronate following ovariectomy
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PID: 7756049, COI: 1:CAS:528:DyaK2MXltlCrtLY%3D
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Boyce RW, Wronski TJ, Ebert DC, et al.: Direct stereological estimation of three-dimensional connectivity in rat vertebrae: effect of estrogen, etidronate and risedronate following ovariectomy. Bone 1995, 16:209–213. DOI: 10.1016/8756-3282(94)00031-T
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Bone
, vol.16
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Boyce, R.W.1
Wronski, T.J.2
Ebert, D.C.3
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2
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-
0030678552
-
Bone mineral density reflects bone mass but also the degree of mineralization of bone: therapeutic implications
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PID: 9356729, COI: 1:STN:280:DyaK1c%2FhvFGktw%3D%3D
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Meunier PJ, Boivin G: Bone mineral density reflects bone mass but also the degree of mineralization of bone: therapeutic implications. Bone 1997, 21:373–377. DOI: 10.1016/S8756-3282(97)00170-1
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(1997)
Bone
, vol.21
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Meunier, P.J.1
Boivin, G.2
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3
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0033755981
-
Alendronate increases bone strength by increasing the mean degree of mineralization of bone tissue in osteoporotic women
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PID: 11062357, COI: 1:CAS:528:DC%2BD3cXosFygtL8%3D, This clinical study demonstrates enhanced bone mineralization biopsies of patients treated with alendronate for 2 to 3 years, provides mechanistic insight into the relationship between reduced turnover and prolonged secondary mineralization, leading to greater mean degree of mineralization, and provides a link between tissue-level mechanism on bone and anti-fracture efficacy
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Boivin GY, Chavassieux PM, Santora AC, et al.: Alendronate increases bone strength by increasing the mean degree of mineralization of bone tissue in osteoporotic women. Bone 2000, 27:687–694. This clinical study demonstrates enhanced bone mineralization in biopsies of patients treated with alendronate for 2 to 3 years, provides mechanistic insight into the relationship between reduced turnover and prolonged secondary mineralization, leading to greater mean degree of mineralization, and provides a link between tissue-level mechanism on bone and anti-fracture efficacy. DOI: 10.1016/S8756-3282(00)00376-8
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(2000)
Bone
, vol.27
, pp. 687-694
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Boivin, G.Y.1
Chavassieux, P.M.2
Santora, A.C.3
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4
-
-
0034906270
-
Alendronate increases degree and uniformity of mineralization in cancellous bone and decreases the porosity in cortical bone of osteoporotic women
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PID: 11502482, COI: 1:CAS:528:DC%2BD3MXlvFWkurk%3D, This clinical study demonstrates enhanced mineralization and reduced porosity biopsies of patients treated with alendronate for 2 to 3 years. Study demonstrates more uniform mineralization treated bone, with maintenance of normal crystal structures
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Roschger P, Rinnerthaler S, Yates J, et al.: Alendronate increases degree and uniformity of mineralization in cancellous bone and decreases the porosity in cortical bone of osteoporotic women. Bone 2001, 29:185–191. This clinical study demonstrates enhanced mineralization and reduced porosity in biopsies of patients treated with alendronate for 2 to 3 years. Study demonstrates more uniform mineralization in treated bone, with maintenance of normal crystal structures. DOI: 10.1016/S8756-3282(01)00485-9
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(2001)
Bone
, vol.29
, pp. 185-191
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Roschger, P.1
Rinnerthaler, S.2
Yates, J.3
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5
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-
0033678399
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Skeletal benefits of alendronate: 7-year treatment of postmenopausal osteoporotic women. Phase III Osteoporosis Treatment Study Group
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PID: 10999794, COI: 1:CAS:528:DC%2BD3cXmsVKru70%3D
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Tonino RP, Meunier PJ, Emkey R, et al.: Skeletal benefits of alendronate: 7-year treatment of postmenopausal osteoporotic women. Phase III Osteoporosis Treatment Study Group. J Clin Endocrinol Metab 2000, 85:3109–3115. DOI: 10.1210/jc.85.9.3109
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J Clin Endocrinol Metab
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Tonino, R.P.1
Meunier, P.J.2
Emkey, R.3
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6
-
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0026320852
-
Bisphosphonate action: alendronate localization in rat bone and effects on osteoclast ultrastructure
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PID: 1661297, COI: 1:CAS:528:DyaK38XjsVGgtA%3D%3D
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Sato M, Grasser W, Endo N, et al.: Bisphosphonate action: alendronate localization in rat bone and effects on osteoclast ultrastructure. J Clin Invest 1991, 88:2095–2105.
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Sato, M.1
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Endo, N.3
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7
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0029164610
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Alendronate distributed on bone surfaces inhibits osteoclastic bone resorption in vitro and in experimental hypercalcemia models
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PID: 7756053, COI: 1:CAS:528:DyaK2MXltlCrtb8%3D
-
Azuma Y, Sato H, Oue Y, et al.: Alendronate distributed on bone surfaces inhibits osteoclastic bone resorption in vitro and in experimental hypercalcemia models. Bone 1995, 16:235–245. DOI: 10.1016/8756-3282(94)00035-X
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, vol.16
, pp. 235-245
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Azuma, Y.1
Sato, H.2
Oue, Y.3
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8
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0030227986
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Comparison of the distribution of 3H-alendronate and 3H-etidronate in rat and mouse bones
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Masarachia P, Weinreb M, Balena R, Rodan GA: Comparison of the distribution of 3H-alendronate and 3H-etidronate in rat and mouse bones. Bone 2003, 19:281–290. DOI: 10.1016/8756-3282(96)00182-2
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(2003)
Bone
, vol.19
, pp. 281-290
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Masarachia, P.1
Weinreb, M.2
Balena, R.3
Rodan, G.A.4
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9
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0009390724
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Protein-tyrosine phosphatase activity regulates osteoclast formation and function: inhibition by alendronate
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Schmidt A, Rutledge SJ, Endo N, et al.: Protein-tyrosine phosphatase activity regulates osteoclast formation and function: inhibition by alendronate. Proc Natl Acad Sci U S A 2003, 93:3068–3073. DOI: 10.1073/pnas.93.7.3068
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Proc Natl Acad Sci U S A
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, pp. 3068-3073
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Schmidt, A.1
Rutledge, S.J.2
Endo, N.3
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10
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0029873660
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Human protein tyrosine phosphatase-sigma: alternative splicing and inhibition by bisphosphonates
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Endo N, Rutledge SJ, Opas EE, et al.: Human protein tyrosine phosphatase-sigma: alternative splicing and inhibition by bisphosphonates. J Bone Miner Res 2003, 11:535–543.
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(2003)
J Bone Miner Res
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Endo, N.1
Rutledge, S.J.2
Opas, E.E.3
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11
-
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0030918039
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Tiludronate inhibits protein tyrosine phosphatase activity in osteoclasts
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PID: 9145236, COI: 1:CAS:528:DyaK2sXjsV2iuro%3D
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Murakami H, Takahashi N, Tanaka S, et al.: Tiludronate inhibits protein tyrosine phosphatase activity in osteoclasts. Bone 1997, 20:399–404. DOI: 10.1016/S8756-3282(97)00025-2
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(1997)
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, vol.20
, pp. 399-404
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Murakami, H.1
Takahashi, N.2
Tanaka, S.3
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12
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0030776772
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Alendronate inhibition of protein-tyrosine-phosphatase-meg1
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PID: 9310349, COI: 1:CAS:528:DyaK2sXmt1yjs7k%3D
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Opas EE, Rutledge SJ, Golub E, et al.: Alendronate inhibition of protein-tyrosine-phosphatase-meg1. Biochem Pharmacol 1997, 54:721–727. DOI: 10.1016/S0006-2952(97)00225-6
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, pp. 721-727
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Opas, E.E.1
Rutledge, S.J.2
Golub, E.3
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13
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0030931795
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How does alendronate inhibit protein-tyrosine phosphatases?
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PID: 9278398, COI: 1:CAS:528:DyaK2sXlvFGitro%3D
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Skorey K, Ly HD, Kelly J, et al.: How does alendronate inhibit protein-tyrosine phosphatases? J Biol Chem 1997, 272:22472–22480. DOI: 10.1074/jbc.272.36.22472
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Skorey, K.1
Ly, H.D.2
Kelly, J.3
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14
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0029782880
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The bisphosphonate tiludronate is a potent inhibitor of the osteoclast vacuolar H(+)-ATPase
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David P, Nguyen H, Barbier A, Baron R: The bisphosphonate tiludronate is a potent inhibitor of the osteoclast vacuolar H(+)-ATPase. J Bone Miner Res 2003, 11:1498–1507.
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J Bone Miner Res
, vol.11
, pp. 1498-1507
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David, P.1
Nguyen, H.2
Barbier, A.3
Baron, R.4
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15
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1842405434
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Clodronate and liposome-encapsulated clodronate are metabolized to a toxic ATP analog, adenosine 5’-(beta, gamma-dichloromethylene) triphosphate, by mammalian cells in vitro
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PID: 9286751, COI: 1:CAS:528:DyaK2sXmt1Wks7s%3D
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Frith JC, Monkkonen J, Blackburn GM, et al.: Clodronate and liposome-encapsulated clodronate are metabolized to a toxic ATP analog, adenosine 5’-(beta, gamma-dichloromethylene) triphosphate, by mammalian cells in vitro. J Bone Miner Res 1997, 12:1358–1367. DOI: 10.1359/jbmr.1997.12.9.1358
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J Bone Miner Res
, vol.12
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Frith, J.C.1
Monkkonen, J.2
Blackburn, G.M.3
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16
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0035460134
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The molecular mechanism of action of the antiresorptive and anti-inflammatory drug clodronate: evidence for the formation in vivo of a metabolite that inhibits bone resorption and causes osteoclast and macrophage apoptosis
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PID: 11592386, COI: 1:CAS:528:DC%2BD3MXpt12lt7g%3D, This study provides first vivo evidence for the formation of the active metabolite responsible for clodronate induction osteoclast apoptosis. The active metabolite is shown to induce osteoclast apoptosis and suppress bone resorption, linking its action to that of clodronate
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Frith JC, Monkkonen J, Auriola S, et al.: The molecular mechanism of action of the antiresorptive and anti-inflammatory drug clodronate: evidence for the formation in vivo of a metabolite that inhibits bone resorption and causes osteoclast and macrophage apoptosis. Arthritis Rheum 2001, 44:2201–2210. This study provides first in vivo evidence for the formation of the active metabolite responsible for clodronate induction osteoclast apoptosis. The active metabolite is shown to induce osteoclast apoptosis and suppress bone resorption, linking its action to that of clodronate. DOI: 10.1002/1529-0131(200109)44:9<2201::AID-ART374>3.0.CO;2-E
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(2001)
Arthritis Rheum
, vol.44
, pp. 2201-2210
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Frith, J.C.1
Monkkonen, J.2
Auriola, S.3
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17
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0036238837
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Further insight into mechanism of action of clodronate: inhibition of mitochondrial ADP/ATP translocase by a nonhydrolyzable, adenine-containing metabolite
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PID: 11961144, COI: 1:CAS:528:DC%2BD38XjtlGksr8%3D, This biochemical study identifies a likely candidate enzyme, mitochondrial ADT/ATP translocase, as a target for the clodronate metabolite. This provides a link between the moelcular target of clodronate action and the induction of osteoclast apoptosis
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Lehenkari PP, Kellinsalmi M, Napankangas JP, et al.: Further insight into mechanism of action of clodronate: inhibition of mitochondrial ADP/ATP translocase by a nonhydrolyzable, adenine-containing metabolite. Mol Pharmacol 2002, 61:1255–1262. This biochemical study identifies a likely candidate enzyme, mitochondrial ADT/ATP translocase, as a target for the clodronate metabolite. This provides a link between the moelcular target of clodronate action and the induction of osteoclast apoptosis. DOI: 10.1124/mol.61.5.1255
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Mol Pharmacol
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, pp. 1255-1262
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Lehenkari, P.P.1
Kellinsalmi, M.2
Napankangas, J.P.3
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18
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0023749462
-
Isoprenoid (phosphinylmethyl) phosphonates as inhibitors of squalene synthetase
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PID: 3172121, COI: 1:CAS:528:DyaL1cXlt12gsbc%3D
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Biller SA, Forster C, Gordon EM, et al.: Isoprenoid (phosphinylmethyl) phosphonates as inhibitors of squalene synthetase. J Med Chem 1988, 31:1869–1871. DOI: 10.1021/jm00118a001
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Biller, S.A.1
Forster, C.2
Gordon, E.M.3
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19
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0026486931
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Bisphosphonates used for the treatment of bone disorders inhibit squalene synthase and cholesterol biosynthesis
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PID: 1464749, COI: 1:CAS:528:DyaK3sXntlCktA%3D%3D
-
Amin D, Cornell SA, Gustafson SK, et al.: Bisphosphonates used for the treatment of bone disorders inhibit squalene synthase and cholesterol biosynthesis. J Lipid Res 1992, 33:1657–1663.
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Amin, D.1
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Gustafson, S.K.3
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20
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0027436434
-
Lipophilic 1,1-bisphosphonates are potent squalene synthase inhibitors and orally active cholesterol lowering agents in vivo
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PID: 8227045, COI: 1:CAS:528:DyaK3sXmtFOisr4%3D
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Ciosek CP, Jr, Magnin DR, Harrity TW, et al.: Lipophilic 1,1-bisphosphonates are potent squalene synthase inhibitors and orally active cholesterol lowering agents in vivo. J Biol Chem 1993, 268:24832–24837.
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Ciosek, C.P.1
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Harrity, T.W.4
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21
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0029011739
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1,1-Bisphosphonate squalene synthase inhibitors: interplay between the isoprenoid subunit and the diphosphate surrogate
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PID: 7629799, COI: 1:CAS:528:DyaK2MXms1Ojsrw%3D
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Magnin DR, Biller SA, Dickson JK, Jr, et al.: 1,1-Bisphosphonate squalene synthase inhibitors: interplay between the isoprenoid subunit and the diphosphate surrogate. J Med Chem 1995, 38:2596–2605. DOI: 10.1021/jm00014a012
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Magnin, D.R.1
Biller, S.A.2
Dickson, J.K.3
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22
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0029791778
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1-Hydroxy-3-(methylpentylamino)-propylidene-1,1-bisphosphonic acid as a potent inhibitor of squalene synthase
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Amin D, Cornell SA, Perrone MH, Bilder GE: 1-Hydroxy-3-(methylpentylamino)-propylidene-1,1-bisphosphonic acid as a potent inhibitor of squalene synthase. Arzneimittelforschung 2003, 46:759–762.
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Amin, D.1
Cornell, S.A.2
Perrone, M.H.3
Bilder, G.E.4
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23
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0030176408
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Time-dependent changes in biochemical bone markers and serum cholesterol in ovariectomized rats: effects of raloxifene HCl, tamoxifen, estrogen, and alendronate
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Frolik CA, Bryant HU, Black EC, et al.: Time-dependent changes in biochemical bone markers and serum cholesterol in ovariectomized rats: effects of raloxifene HCl, tamoxifen, estrogen, and alendronate. Bone 2003, 18:621–627. DOI: 10.1016/8756-3282(96)00085-3
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(2003)
Bone
, vol.18
, pp. 621-627
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Frolik, C.A.1
Bryant, H.U.2
Black, E.C.3
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24
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17044454321
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SR-12813 lowers plasma cholesterol in beagle dogs by decreasing cholesterol biosynthesis
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PID: 9298680, COI: 1:CAS:528:DyaK2sXlslent7s%3D
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Berkhout TA, Simon HM, Jackson B, et al.: SR-12813 lowers plasma cholesterol in beagle dogs by decreasing cholesterol biosynthesis. Atherosclerosis 1997, 133:203–212. DOI: 10.1016/S0021-9150(97)00131-7
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Berkhout, T.A.1
Simon, H.M.2
Jackson, B.3
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25
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15844402429
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The novel cholesterol- lowering drug SR-12813 inhibits cholesterol synthesis via an increased degradation of 3-hydroxy-3-methylglutarylcoenzyme A reductase
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Berkhout TA, Simon HM, Patel DD, et al.: The novel cholesterol- lowering drug SR-12813 inhibits cholesterol synthesis via an increased degradation of 3-hydroxy-3-methylglutarylcoenzyme A reductase. J Biol Chem 2003, 271:14376–14382.
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Berkhout, T.A.1
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Patel, D.D.3
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26
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0030859911
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An enzyme inhibition assay for the quantitative determination of the new bisphosphonate zoledronate in plasma
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PID: 9278893, COI: 1:CAS:528:DyaK2sXlvVejtbs%3D
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Risser F, Pfister CU, Degen PH: An enzyme inhibition assay for the quantitative determination of the new bisphosphonate zoledronate in plasma. J Pharm Biomed Anal 1997, 15:1877–1880. DOI: 10.1016/S0731-7085(96)02021-3
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Risser, F.1
Pfister, C.U.2
Degen, P.H.3
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27
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0033958778
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Alendronate is a specific, nanomolar inhibitor of farnesyl diphosphate synthase
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PID: 10620343, COI: 1:CAS:528:DC%2BD3cXosVWl, This biochemical study explains how farnesyl diphosphate synthase was first identified as the molecular target for N-BPs
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Bergstrom JD, Bostedor RG, Masarachia PJ, et al.: Alendronate is a specific, nanomolar inhibitor of farnesyl diphosphate synthase. Arch Biochem Biophys 2000, 373:231–241. This biochemical study explains how farnesyl diphosphate synthase was first identified as the molecular target for N-BPs. DOI: 10.1006/abbi.1999.1502
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Arch Biochem Biophys
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Bergstrom, J.D.1
Bostedor, R.G.2
Masarachia, P.J.3
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28
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0033573882
-
Nitrogen-containing bisphosphonates inhibit isopentenyl pyrophosphate isomerase/farnesyl pyrophosphate synthase activity with relative potencies corresponding to their antiresorptive potencies in vitro and in vivo
-
PID: 10049736
-
van Beek E, Pieterman E, Cohen L, et al.: Nitrogen-containing bisphosphonates inhibit isopentenyl pyrophosphate isomerase/farnesyl pyrophosphate synthase activity with relative potencies corresponding to their antiresorptive potencies in vitro and in vivo. Biochem Biophys Res Commun 1999, 255:491–494. DOI: 10.1006/bbrc.1999.0224
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van Beek, E.1
Pieterman, E.2
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29
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0033554651
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Farnesyl pyrophosphate synthase is the molecular target of nitrogen-containing bisphosphonates
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PID: 10527849
-
van Beek E, Pieterman E, Cohen L, et al.: Farnesyl pyrophosphate synthase is the molecular target of nitrogen-containing bisphosphonates. Biochem Biophys Res Commun 1999, 264:108–111. DOI: 10.1006/bbrc.1999.1499
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Biochem Biophys Res Commun
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van Beek, E.1
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30
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0035146537
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Structure-activity relationships for inhibition of farnesyl diphosphate synthase in vitro and inhibition of bone resorption in vivo by nitrogen-containing bisphosphonates
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PID: 11160603, COI: 1:CAS:528:DC%2BD3MXoslaluw%3D%3D, This biochemical study extends analysis of farnesyl diphosphate synthase inhibition to several N-BPs. It provides statistical evidence for a link between inhibition of this enzyme and vivo efficacy on bone
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Dunford JE, Thompson K, Coxon FP, et al.: Structure-activity relationships for inhibition of farnesyl diphosphate synthase in vitro and inhibition of bone resorption in vivo by nitrogen-containing bisphosphonates. J Pharmacol Exp Ther 2001, 296:235–242. This biochemical study extends analysis of farnesyl diphosphate synthase inhibition to several N-BPs. It provides statistical evidence for a link between inhibition of this enzyme and in vivo efficacy on bone.
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J Pharmacol Exp Ther
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Dunford, J.E.1
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Coxon, F.P.3
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31
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0033527417
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Nitrogen-containing bisphosphonates as carbocation transition state analogs for isoprenoid biosynthesis
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PID: 10512752, COI: 1:CAS:528:DyaK1MXmtlCrtrg%3D
-
Martin MB, Arnold W, Heath HT, et al.: Nitrogen-containing bisphosphonates as carbocation transition state analogs for isoprenoid biosynthesis. Biochem Biophys Res Commun 1999, 263:754–758. DOI: 10.1006/bbrc.1999.1404
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4344635757
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Modeling of bisphosphonate binding to farnesyl diphosphate synthase
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Ebetino FH, Rogers MJ, Dunford JE, et al.: Modeling of bisphosphonate binding to farnesyl diphosphate synthase. Bone 2002, 30:40S. DOI: 10.1016/S8756-3282(01)00637-8
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Bone
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The mechanism of inhibition of farnesyl diphosphate synthase by nitrogen-containing bisphosphonates
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Dunford JE, Ebetino FH, Rogers MJ: The mechanism of inhibition of farnesyl diphosphate synthase by nitrogen-containing bisphosphonates. Bone 2002, 30:40S. DOI: 10.1016/S8756-3282(01)00637-8
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34
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0035930612
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Identification of a novel phosphonocarboxylate inhibitor of Rab geranylgeranyl transferase that specifically prevents Rab prenylation in osteoclasts and macrophages
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PID: 11581260, COI: 1:CAS:528:DC%2BD38XltVei
-
Coxon FP, Helfrich MH, Larijani B, et al.: Identification of a novel phosphonocarboxylate inhibitor of Rab geranylgeranyl transferase that specifically prevents Rab prenylation in osteoclasts and macrophages. J Biol Chem 2001, 276:48213–48222.
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Coxon, F.P.1
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Larijani, B.3
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35
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0344074580
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Binding and antiresorptive properties of heterocycle-containing bisphosphonate analogs: structure-activity relationships
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PID: 9823450
-
van Beek ER, Lowik CW, Ebetino FH, Papapoulos SE: Binding and antiresorptive properties of heterocycle-containing bisphosphonate analogs: structure-activity relationships. Bone 1998, 23:437–442. DOI: 10.1016/S8756-3282(98)00120-3
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36
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0028202499
-
Preclinical pharmacology of CGP 42’446, a new, potent, heterocyclic bisphosphonate compound
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PID: 8053405, COI: 1:CAS:528:DyaK2cXlt1Gitro%3D
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Green JR, Muller K, Jaeggi KA: Preclinical pharmacology of CGP 42’446, a new, potent, heterocyclic bisphosphonate compound. J Bone Miner Res 1994, 9:745–751.
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37
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0035463593
-
Zoledronic acid versus pamidronate in the treatment of skeletal metastases in patients with breast cancer or osteolytic lesions of multiple myeloma: a phase III, double-blind, comparative trial
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