Medicinal Chemistry

(Jacob Rumans) #1

to be balanced against the risk of breast cancer and other shortcomings associated with
chronic estrogen replacement.


Selected References


Proteins as Drug Design Targets: Enzymes


D. C. Evans, D. P. Hartley, R. Evers (2001). Enzyme induction—Mechanisms, assays, and
relevance to drug discovery and development. Ann. Rep. Med. Chem. 38: 315.
A. Fersht (1985). Enzyme Structure and Mechanism,2nd ed. San Francisco: Freeman.
M. Garcia-Viloca, J. Gao, M. Karplus, D. Truhlar (2004). How enzymes work: analysis by modern
rate theory and computer simulations. Science 303: 186–195.
M. J. Jung (1978). Selective enzyme inhibitors in medicinal chemistry. Annu. Rep. Med. Chem.
13 : 249–260.
R. N. Lindquist (1975). The design of enzyme inhibitors: Transition state analogs. In: E. J. Ariëns
(Ed.).Drug Design, vol. 5. New York: Academic Press, pp. 23–80.
T. M. Penning (1983). Design of suicide substrates. Trends Pharmacol. Sci. 4: 212–217.
R. R. Rando (1974). Mechanism based irreversible enzyme inhibitors. Annu. Rep. Med. Chem. 9:
234–243.
M. Sandler (Ed.) (1980). Enzyme Inhibitors as Drugs. London: Macmillan.
C. T. Walsh (1984). Suicide substrates, mechanism-based enzyme inactivators: recent develop-
ments.Annu. Rev. Biochem. 53: 493–535.
R. Wolfenden (1976). Transition state analog inhibitors and enzyme catalysis. Annu. Rev.
Biophys. Bioeng. 5 : 271–306.


Enzyme Targets: Acetylcholinesterase


A. Khalid, Zaheer-uls-Haq, S. Anjum, M. Riaz Khan, Atta-ur-Rahman, M. Iqbal Choudhary
(2004). Kinetics and structure–activity relationship studies on pregnane-type steroidal alka-
loids that inhibit cholinesterases. Bioorg. Med. Chem. 12: 1995–2003.
J. Lindstrom (1986). Acetylcholine receptors: structure, function, synthesis, destruction and
antigenicity. In: A. G. Engel, B. Q. Banker (Eds.). Myology.New York: McGraw-Hill,
pp. 769–790.
P. Taylor, M. Schumacher, K. MacPhee-Quigley, T. Friedman, S. Taylor (1987). The structure of
acetylcholinesterase: relationships to its function and cellular disposition. Trends Neurosci.
10 : 92–96.


Enzyme Targets: Adenosine Triphosphatase


J. A. Bristol, D. B. Evans (1981). Cardiotonic agents for the treatment of heart failure. Annu. Rep.
Med. Chem. 16: 91–102.
S. F. Campbell, J. C. Danilewicz (1978). Agents for the treatment of heart failure. Annu. Rep.
Med. Chem. 13: 92–102.
L. Cantley (1986). Ion transport systems sequenced. Trends Neurosci. 9: 1–3.
P. Chene (2002). ATPases as drug targets: learning from their structure. Nat. Rev. Drug Discov.
1 : 665–673.
P. Chene (2003). The ATPases: a new family for a family-based drug design approach. Expert
Opin. Ther. Targ. 7: 453–461.


538 MEDICINAL CHEMISTRY

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