Substitution of the side-chain-constrained amino acids β-methyl-2',6'- dimethyl-4'-methoxytyrosine in position 2 of a bicyclic oxytocin analogue provides unique insights into the bioactive topography of oxytocin antagonists [24]

S. Liao; M. D. Shenderovich; Z. Zhang; L. Maletinska; J. Slaninova; V. J. Hruby

doi:10.1021/ja980848b

Substitution of the side-chain-constrained amino acids β-methyl-2',6'- dimethyl-4'-methoxytyrosine in position 2 of a bicyclic oxytocin analogue provides unique insights into the bioactive topography of oxytocin antagonists [24]

S. Liao
, M. D. Shenderovich
, Z. Zhang
, L. Maletinska
, J. Slaninova
, V. J. Hruby

Research output: Contribution to journal › Letter › peer-review

Original language	English (US)
Pages (from-to)	7393-7394
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	120
Issue number	29
DOIs	https://doi.org/10.1021/ja980848b
State	Published - Jul 29 1998
Externally published	Yes

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja980848b

Cite this

Liao, S., Shenderovich, M. D., Zhang, Z., Maletinska, L., Slaninova, J., & Hruby, V. J. (1998). Substitution of the side-chain-constrained amino acids β-methyl-2',6'- dimethyl-4'-methoxytyrosine in position 2 of a bicyclic oxytocin analogue provides unique insights into the bioactive topography of oxytocin antagonists [24]. Journal of the American Chemical Society, 120(29), 7393-7394. https://doi.org/10.1021/ja980848b

Substitution of the side-chain-constrained amino acids β-methyl-2',6'- dimethyl-4'-methoxytyrosine in position 2 of a bicyclic oxytocin analogue provides unique insights into the bioactive topography of oxytocin antagonists [24]. / Liao, S.; Shenderovich, M. D.; Zhang, Z. et al.
In: Journal of the American Chemical Society, Vol. 120, No. 29, 29.07.1998, p. 7393-7394.

Research output: Contribution to journal › Letter › peer-review

Liao, S, Shenderovich, MD, Zhang, Z, Maletinska, L, Slaninova, J & Hruby, VJ 1998, 'Substitution of the side-chain-constrained amino acids β-methyl-2',6'- dimethyl-4'-methoxytyrosine in position 2 of a bicyclic oxytocin analogue provides unique insights into the bioactive topography of oxytocin antagonists [24]', Journal of the American Chemical Society, vol. 120, no. 29, pp. 7393-7394. https://doi.org/10.1021/ja980848b

Liao S, Shenderovich MD, Zhang Z, Maletinska L, Slaninova J, Hruby VJ. Substitution of the side-chain-constrained amino acids β-methyl-2',6'- dimethyl-4'-methoxytyrosine in position 2 of a bicyclic oxytocin analogue provides unique insights into the bioactive topography of oxytocin antagonists [24]. Journal of the American Chemical Society. 1998 Jul 29;120(29):7393-7394. doi: 10.1021/ja980848b

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author = "S. Liao and Shenderovich, \{M. D.\} and Z. Zhang and L. Maletinska and J. Slaninova and Hruby, \{V. J.\}",

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AU - Slaninova, J.

AU - Hruby, V. J.

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Substitution of the side-chain-constrained amino acids β-methyl-2',6'- dimethyl-4'-methoxytyrosine in position 2 of a bicyclic oxytocin analogue provides unique insights into the bioactive topography of oxytocin antagonists [24]

ASJC Scopus subject areas

Access to Document

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