The interactions of adenylate cyclases with P-site inhibitors

Carmen W. Dessauer; John J G Tesmer; Stephen R. Sprang; Alfred G. Gilman

doi:10.1016/S0165-6147(99)01310-3

The interactions of adenylate cyclases with P-site inhibitors

Carmen W. Dessauer, John J G Tesmer, Stephen R. Sprang, Alfred G. Gilman

Pharmacology

Research output: Contribution to journal › Review article › peer-review

84 Scopus citations

Abstract

Recent kinetic, binding and crystallographic studies using P-site inhibitors of mammalian adenylate cyclases provide new insights into the catalytic mechanism of these highly regulated enzymes. Here, Carmen Dessauer and colleagues discuss the conformational states of adenylate cyclase, the structural determinants of inhibitor binding and the potential uses of these inhibitors as pharmacological agents.

Original language	English (US)
Pages (from-to)	205-210
Number of pages	6
Journal	Trends in Pharmacological Sciences
Volume	20
Issue number	5
DOIs	https://doi.org/10.1016/S0165-6147(99)01310-3
State	Published - May 1 1999

ASJC Scopus subject areas

Toxicology
Pharmacology

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10.1016/S0165-6147(99)01310-3

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title = "The interactions of adenylate cyclases with P-site inhibitors",

abstract = "Recent kinetic, binding and crystallographic studies using P-site inhibitors of mammalian adenylate cyclases provide new insights into the catalytic mechanism of these highly regulated enzymes. Here, Carmen Dessauer and colleagues discuss the conformational states of adenylate cyclase, the structural determinants of inhibitor binding and the potential uses of these inhibitors as pharmacological agents.",

author = "Dessauer, {Carmen W.} and Tesmer, {John J G} and Sprang, {Stephen R.} and Gilman, {Alfred G.}",

note = "Funding Information: Work from the authors' laboratories was supported by NIH grants DK46371 and GM34497, Welch Foundation Grants I-1229 and I-1271 and the Raymond and Ellen Willie Distinguished Chair in Molecular Neuropharmacology.",

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AU - Dessauer, Carmen W.

AU - Tesmer, John J G

AU - Sprang, Stephen R.

AU - Gilman, Alfred G.

N1 - Funding Information: Work from the authors' laboratories was supported by NIH grants DK46371 and GM34497, Welch Foundation Grants I-1229 and I-1271 and the Raymond and Ellen Willie Distinguished Chair in Molecular Neuropharmacology.

PY - 1999/5/1

Y1 - 1999/5/1

N2 - Recent kinetic, binding and crystallographic studies using P-site inhibitors of mammalian adenylate cyclases provide new insights into the catalytic mechanism of these highly regulated enzymes. Here, Carmen Dessauer and colleagues discuss the conformational states of adenylate cyclase, the structural determinants of inhibitor binding and the potential uses of these inhibitors as pharmacological agents.

AB - Recent kinetic, binding and crystallographic studies using P-site inhibitors of mammalian adenylate cyclases provide new insights into the catalytic mechanism of these highly regulated enzymes. Here, Carmen Dessauer and colleagues discuss the conformational states of adenylate cyclase, the structural determinants of inhibitor binding and the potential uses of these inhibitors as pharmacological agents.

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JO - Trends in Pharmacological Sciences

JF - Trends in Pharmacological Sciences

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The interactions of adenylate cyclases with P-site inhibitors

Abstract

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