Drugs and Leads from the Ocean Through Biotechnology References 725
Part F | 29
29.13
A.B. Malmberg, T.L. Yaksh: Effect of continuous intrathecal infusion of !-conopeptides, Ntype calcium-channel blockers, on behavior and
antinociception in the formalin and hot-plate
tests in rats, Pain 60, 83–90 (1995)
29.14
B.M. Olivera: Conus peptides: Biodiversity-based
discovery and exogenomics, J. Biol. Chem. 281,
31173–31177 (2006)
29.15
B.M. Olivera, R.W. Teichert: Diversity of the neurotoxic conus peptides: A model for concerted
pharmacologic discovery, Mol. Interv. 7, 251–260
(2007)
29.16
B.M. Olivera: !-Conotoxin MVIIA: From marine
snail venom to analgesic drug. In: Drugs from the
Sea, ed. by N. Fusetani (Karger, Basel 2000) pp.
75–85
29.17
J.P. Bingham, E. Mitsunaga, Z.L. Bergeron: Drugs
from slugs past, present and future perspectives
of omega-conotoxin research, Chem. Biol. Interact. 183, 1–18 (2010)
29.18
D. Chung, S. Gaur, J.R. Bell, J. Ramachandran,
L. Nadasdi: Determination of disulfide bridge
pattern in !-conopeptides, Int. J. Pept. Protein
Res. 46, 320–325 (1995)
29.19
A. Schmidtko, J. Lötsch, R. Freynhagen,
G. Geisslinger: Ziconotide for treatment of
severe chronic pain, Lancet 375, 1569–1577 (2010)
29.20
P.S. Staats, Y. Thomas, G.S. Charapata,
R.W. Presley, M.S. Wallace, M. Byas-Smith,
R. Fisher, D.A. Bryce, E.A. Mangieri, R.R. Luther,
M.M. Pharm, D. McGuire, D. Ellis: Intrathecal
ziconotide in the treatment of refractory pain
in patients with cancer or AIDS A randomized
controlled trial, J. Am. Med. Assoc. 291, 63–70
(2004)
29.21
Y.X. Wang, D. Gao, M. Pettus, C. Phillips, S.S. Bowersox: Interactions of intrathecally administered
ziconotide, a selective blocker of neuronal N-type
voltage-sensitive calcium channels, with morphine on nociception in rats, Pain 84, 271–281
(2000)
29.22
R.J. Lewis, K.J. Nielsen, D.J. Craik, M.L. Loughnan,
D.A. Adams, I.A. Sharpe, T. Luchian, D.J. Adams,
T. Bond, L. Thomas, A. Jones, J.L. Matheson, R. Drinkwater, P.R. Andrew, P.F. Alewood:
Novel !-conotoxins from Conus catus discriminate among neuronal calcium channel subtypes,
J. Biol. Chem. 275, 35335–35344 (2000)
29.23
D.A. Scott, C.E. Wright, J.A. Angus: Actions of
intrathecal !-conotoxins CVID, GVIA, MVIIA, and
morphine in acute and neuropathic pain in the
rat, Eur. J. Pharmacol. 451, 279–286 (2002)
29.24
R.L. Rauck, M.S. Wallace, A.W. Burton, L. Kapural,
J.M. North: Intrathecal ziconotide for neuropathic
pain: A review, Pain Pract. 9, 327–337 (2009)
29.25
K. Garber: Peptide leads new class of chronic pain
drugs, Nat. Biotech. 23, 399 (2005)
29.26
K.L. Rinehart, T.G. Holt, N.L. Fregeau, J.G. Stroh,
P.A. Keifer, F. Sun, L.H. Li, D.G. Martin: Ecteinascidin-729, Ecteinascidin-743, Ecteinascidin745, Ecteinascidin-759a, Ecteinascidin-759b, and
Ecteinascidin-770 potent antitumor agents from
the Caribbean tunicate Ecteinascidiaturbinata,
J. Org. Chem. 55, 4512–4515 (1990)
29.27
A.E. Wright, D.A. Forleo, G.P. Gunawardana,
S.P. Gunasekera, F.E. Koehn, O.J. McConnell: Antitumortetrahydroisoquinoline alkaloids from the
colonial ascidian Ecteinascidiaturbinata, J. Org.
Chem. 55, 4508–4512 (1990)
29.28
C. van Kesteren, M.M. de Vooght, L. LópezLázaro, R.A. Mathôt, J.H. Schellens, J.M. Jimeno, J.H. Beijnen: Yondelis (trabectedin, ET743): The development of an anticancer agent of
marine origin., Anticancer Drugs 14(7), 487–502
(2003)
29.29
M. Zewail-Foote, V.S. Li, K.H. Bearss, M. Guzman, L.H. Hurley: The inefficiency of incisions of
ecteinascidin 743-DNA adducts by the UvrABC nuclease and the unique structural feature of the
DNA adducts can be used to explain the repairdependent toxicities of this antitumor agent,
Chem. Biol. 8, 1033–1049 (2001)
29.30
D.G. Soares, A.E. Escargueil, V. Poindessous,
A. Sarasin, A. de Gramont, D. Bonatto, J.A. Pêgas, A.K. Larsen: Replication and homologous
recombination repair regulate DNA-double strand
break formation by antitumor alkyl for eiteinascidin 743, Proc. Natl. Acad. Sci. 10, 13062–
13067 (2007)
29.31
A.B. Herrero, C. Martin-Castellanos, E. Marco,
F. Gago, S. Moreno: Cross-talk between nucleotide excision and homologous recombination
DNA repair pathways in the mechanism of action
of antitumor trabectedin, Cancer Res. 66, 8155–
8162 (2006)
29.32
C. Sessa, A. Perotti, C. Noberasco, F. De Braud,
E. Gallerani, S. Cresta, M. Zucchetti, L. Viganò, A. Locatelli, J. Jimeno, J.W. Feilchenfeldt,
M. D’Incalci, G. Capri, N. Ielmini, L. Gianni: Phase I
clinical and pharmacokinetic study of trabectedin
and doxorubicin in advanced soft tissue sarcoma
and breast cancer, Eur. J. Cancer 45(7), 1153–1161
(2009)
29.33
I. Bhatnagar, S.-K. Kim: Marine antitumor drugs:
Status, shortfalls and strategies, Mar. Drugs 8,
2702–2720 (2010)
29.34
D.J. Newman, G.M. Cragg: Marine natural products and related compounds in clinical and advanced pre-clinical trials, J. Nat. Prod. 67, 1216–
1238 (2004)
29.35
R. Montaser, H. Luesch: Marine natural products:
A new wave of drugs?, Future Med, Chem. 3(12),
1475–1489 (2011)
29.36
D. Cosco, F. Rocco, M. Ceruti, M. Vono, M. Fresta,
D. Paolino: Self-assembled squalenoyl-cytarabine nanostructures as a potent nanomedicine
for treatment of leukemic diseases, Int.
J. Nanomed. 7, 2535–2546 (2012)
Part F | 29
29.13
A.B. Malmberg, T.L. Yaksh: Effect of continuous intrathecal infusion of !-conopeptides, Ntype calcium-channel blockers, on behavior and
antinociception in the formalin and hot-plate
tests in rats, Pain 60, 83–90 (1995)
29.14
B.M. Olivera: Conus peptides: Biodiversity-based
discovery and exogenomics, J. Biol. Chem. 281,
31173–31177 (2006)
29.15
B.M. Olivera, R.W. Teichert: Diversity of the neurotoxic conus peptides: A model for concerted
pharmacologic discovery, Mol. Interv. 7, 251–260
(2007)
29.16
B.M. Olivera: !-Conotoxin MVIIA: From marine
snail venom to analgesic drug. In: Drugs from the
Sea, ed. by N. Fusetani (Karger, Basel 2000) pp.
75–85
29.17
J.P. Bingham, E. Mitsunaga, Z.L. Bergeron: Drugs
from slugs past, present and future perspectives
of omega-conotoxin research, Chem. Biol. Interact. 183, 1–18 (2010)
29.18
D. Chung, S. Gaur, J.R. Bell, J. Ramachandran,
L. Nadasdi: Determination of disulfide bridge
pattern in !-conopeptides, Int. J. Pept. Protein
Res. 46, 320–325 (1995)
29.19
A. Schmidtko, J. Lötsch, R. Freynhagen,
G. Geisslinger: Ziconotide for treatment of
severe chronic pain, Lancet 375, 1569–1577 (2010)
29.20
P.S. Staats, Y. Thomas, G.S. Charapata,
R.W. Presley, M.S. Wallace, M. Byas-Smith,
R. Fisher, D.A. Bryce, E.A. Mangieri, R.R. Luther,
M.M. Pharm, D. McGuire, D. Ellis: Intrathecal
ziconotide in the treatment of refractory pain
in patients with cancer or AIDS A randomized
controlled trial, J. Am. Med. Assoc. 291, 63–70
(2004)
29.21
Y.X. Wang, D. Gao, M. Pettus, C. Phillips, S.S. Bowersox: Interactions of intrathecally administered
ziconotide, a selective blocker of neuronal N-type
voltage-sensitive calcium channels, with morphine on nociception in rats, Pain 84, 271–281
(2000)
29.22
R.J. Lewis, K.J. Nielsen, D.J. Craik, M.L. Loughnan,
D.A. Adams, I.A. Sharpe, T. Luchian, D.J. Adams,
T. Bond, L. Thomas, A. Jones, J.L. Matheson, R. Drinkwater, P.R. Andrew, P.F. Alewood:
Novel !-conotoxins from Conus catus discriminate among neuronal calcium channel subtypes,
J. Biol. Chem. 275, 35335–35344 (2000)
29.23
D.A. Scott, C.E. Wright, J.A. Angus: Actions of
intrathecal !-conotoxins CVID, GVIA, MVIIA, and
morphine in acute and neuropathic pain in the
rat, Eur. J. Pharmacol. 451, 279–286 (2002)
29.24
R.L. Rauck, M.S. Wallace, A.W. Burton, L. Kapural,
J.M. North: Intrathecal ziconotide for neuropathic
pain: A review, Pain Pract. 9, 327–337 (2009)
29.25
K. Garber: Peptide leads new class of chronic pain
drugs, Nat. Biotech. 23, 399 (2005)
29.26
K.L. Rinehart, T.G. Holt, N.L. Fregeau, J.G. Stroh,
P.A. Keifer, F. Sun, L.H. Li, D.G. Martin: Ecteinascidin-729, Ecteinascidin-743, Ecteinascidin745, Ecteinascidin-759a, Ecteinascidin-759b, and
Ecteinascidin-770 potent antitumor agents from
the Caribbean tunicate Ecteinascidiaturbinata,
J. Org. Chem. 55, 4512–4515 (1990)
29.27
A.E. Wright, D.A. Forleo, G.P. Gunawardana,
S.P. Gunasekera, F.E. Koehn, O.J. McConnell: Antitumortetrahydroisoquinoline alkaloids from the
colonial ascidian Ecteinascidiaturbinata, J. Org.
Chem. 55, 4508–4512 (1990)
29.28
C. van Kesteren, M.M. de Vooght, L. LópezLázaro, R.A. Mathôt, J.H. Schellens, J.M. Jimeno, J.H. Beijnen: Yondelis (trabectedin, ET743): The development of an anticancer agent of
marine origin., Anticancer Drugs 14(7), 487–502
(2003)
29.29
M. Zewail-Foote, V.S. Li, K.H. Bearss, M. Guzman, L.H. Hurley: The inefficiency of incisions of
ecteinascidin 743-DNA adducts by the UvrABC nuclease and the unique structural feature of the
DNA adducts can be used to explain the repairdependent toxicities of this antitumor agent,
Chem. Biol. 8, 1033–1049 (2001)
29.30
D.G. Soares, A.E. Escargueil, V. Poindessous,
A. Sarasin, A. de Gramont, D. Bonatto, J.A. Pêgas, A.K. Larsen: Replication and homologous
recombination repair regulate DNA-double strand
break formation by antitumor alkyl for eiteinascidin 743, Proc. Natl. Acad. Sci. 10, 13062–
13067 (2007)
29.31
A.B. Herrero, C. Martin-Castellanos, E. Marco,
F. Gago, S. Moreno: Cross-talk between nucleotide excision and homologous recombination
DNA repair pathways in the mechanism of action
of antitumor trabectedin, Cancer Res. 66, 8155–
8162 (2006)
29.32
C. Sessa, A. Perotti, C. Noberasco, F. De Braud,
E. Gallerani, S. Cresta, M. Zucchetti, L. Viganò, A. Locatelli, J. Jimeno, J.W. Feilchenfeldt,
M. D’Incalci, G. Capri, N. Ielmini, L. Gianni: Phase I
clinical and pharmacokinetic study of trabectedin
and doxorubicin in advanced soft tissue sarcoma
and breast cancer, Eur. J. Cancer 45(7), 1153–1161
(2009)
29.33
I. Bhatnagar, S.-K. Kim: Marine antitumor drugs:
Status, shortfalls and strategies, Mar. Drugs 8,
2702–2720 (2010)
29.34
D.J. Newman, G.M. Cragg: Marine natural products and related compounds in clinical and advanced pre-clinical trials, J. Nat. Prod. 67, 1216–
1238 (2004)
29.35
R. Montaser, H. Luesch: Marine natural products:
A new wave of drugs?, Future Med, Chem. 3(12),
1475–1489 (2011)
29.36
D. Cosco, F. Rocco, M. Ceruti, M. Vono, M. Fresta,
D. Paolino: Self-assembled squalenoyl-cytarabine nanostructures as a potent nanomedicine
for treatment of leukemic diseases, Int.
J. Nanomed. 7, 2535–2546 (2012)