Orgel. A simpler nucleic acid (origin of life) Science.
290, pg 1306 (2000)
Lusis. Atherosclerosis (a review) Nature. 407. pg
233 (2000)
Mangelsdorf et al. New Ways to Lower Cholesterol .
Science. 289. pg 1446 (2000)
Garcia et al. The Cholesterol Quartet. Science.
292. pg 1310, 1394 (2001)
Fuentes-Prior et al. Structural basis for the
anticoagulant activity of the thrombin-thrombomodulin complex. Nature.
404, pg 449, 518 (2000)
Dennis et al. Peptide exosite inhibitors of factor VIIA
as anticoagulants. Nature. 404, pg 449, 465 (2000)
Okamoto et al. A cholesteryl ester transfer protein
inhibitor attenuates atherosclerosis in rabbits. Nature. 406, pg 203
(2000)
Kersten et al. Roles of PPAR;s in health and
disease. Nature. 405, pg 421 (2000)
The
Divine Cytokine (review of cytokine nomenclature) Scientist. pg 36 April
3, 2000.
HDL metabolism. Nature. 400, pg 816 (2000),
Science, 285, pg 814 (1999) (both about Tangier's disease and relationship
to HDL)
Older References
GENERAL INFORMATION
The Two Cultures: Chemistry and
Biology. Kornberg, Arthur (1987) Biochemistry
(Perspectives) 26, 6888-6891.
Basic Research: the Lifeline of
Medicine. Kornberg, Arthur (1992) News and Features of
unknown Journal 6, 3143-3145.
LIPIDS
LIposomes, Lasic, Danilo. (1992)
American Scientist. 80, 20-30.
Liposomes Revisited, Lasic and
Papahadjopoulos. (1995) Science. 267, 1275-1276.
Doxorubicin in Sterically Stabilized
Liposomes, Lasic. (1996) Nature. 380, 561-562.
PROTEIN
STRUCTURE/FOLDING
Measurement of the Beta Sheet Forming
Propensities of Amino Acids, Minor, D.L. & Kim, P.
(1994) Nature, 367, 660-663.
Structural Basis of Amino Acid -Helix
Propensity, Blaber, M. Zhang, X., & Matthews, B. (1993)
Science, 260, 1637-1640.
The "Bio" in Biochemistry: Protein
Folding Inside and Outside the Cell, Ellis, R. stapled with
Principles of Chaperone-Assisted Proein
Folding: Differences Between in Vitro and in Vivo
Mechanisms. (1996) Science, 272, 1448-9, and 1497-1501.
Moleculear Chaperones in Cellular
Protein Folding. Harti, F. Ulrich. (1996) Nature, 381,
571-580.
Folding Proteins Caught in the
Act, Service, C. (1996) Science, 273, 29-30.
Scientist Refine Understanding of
Protein Folding and Design, Borman, S. (1996) Chemical and
Engineering News, May 27, 29-34.
The Protein Folding Problem,
Chan, H, & Dill, K. (1993) PhysicsToday, 24-32.
The Protein Folding Problem,
Richards, F. (1991) Scientific American, January, 54-63.
A Kinetic Method to Evaluate the
Two-State Character of Solvent-Induced Protein
Denaturation, Micke. M. & Schmid, F. (1994)
Biochemistry, 33, 12930-12935.
The Prion Disease, Prusiner, S.
(1995) Scientific American, 48- 57.
Putting Prions to the Test,
Mestel, R. (1996) Science, 273, 184-185.
Missfolding the Way to Dieseae,
Taubes, G. (1996) Science, 271, 1493-1495.
Amyloid Fibrils: Mutations Make Enzymes
Polymerize, Perutz, M.F, stapled with Instability, Unfolding, And Aggregation of Human
Lysozyme Variants Underlying Amyloid Fibrillogenesis,
Booth, D. R. et. al. (1997) Nature, 385, 787-794.
CARBOHYDRATES
Carbohydrate's Complexities:
Glycobiochemists Attanin a More Detailed Understnading of the
Involvement of Carbohydrates in Intricate Life
Processes, Borman, S. (1996)
Chemistry and Engineering News, Sept. 30, 34-40.
Oligosaccharides Coming of
Age, Rouhi, A. (1996) Chemistry and
Engineering News, Sept. 23, 62-66.
DNA/PROTEIN INTERACTIONS;
TRANSCRIPTION
Protein-DNA Recognition: New Perspective and Underlying
Themes, von Hippel, P. (1994) Science, 263, 769-770.
Coupling of Local Folding to Site Specific Binding of Proteins
to DNA, Spolar, R. & Record, T. (1994) Science, 263, 777-784.
Mining Treasures From Junk DNA, Nowak, R. (1994) Science, 263,
608-610.
Transcriiptional Activation of Heat Shock Genes, Morimoto, R.
Cells in Stress: (1993) Science, 259, 1409-1410.
The Regulation of Transcription by Phosphorylation, Hunter, T.
& Karin, M. (1992) Cell, 70, 375-387.
Target Gene Replacement, Capecchi, M. (1994) Scientific
American, March, 52-61.
What Happens to Nucleosomes duringTranscription, van Holde et
al. (1992) J. Biol. Chem., 267, 2837-2840.
Toward more Measurement in Biology, Maddox, J. (1994) Nature,
368, 95.
Histones as Regulators of Genes, Grunstein, M. (1992)
Scientific American, October, 68-75.
Polymerase Chain Reaction, Amhein, N. & Levenson, C.
(1990) Chem. & Eng. News, October, 36-47.
OXYGEN AND FREE RADICAL
PACKET
Superoxide Dismutases, Fridovich, I. (1989) J. Biological
Chemistry, 7761-7764. 4/26/93
Protein Oxidation and Aging, Stadtman, E. (1992) Science,
1220-1223.
Oxidative Damage to Behavior During Aging, Floyd, R. (1991)
Science, (December) 1597. 4/26/93
Signs of Damage by Radicals: Smoking and Health, Csillag, C.
& Aldhous, P. (1992) Science, 258, 1875-76. 4/26/93
Mitochondrial Genetics: A Paradigm for Aging and Degenerative
Diseases?, Wallace, D. (1992) Science, 256, 628-632.
Did Radicals Strike Lou Gehrig?, McNamara, J. & Fridovich,
I. (1993) Nature, 362, 20-21.
CATALYSIS
The Interplay Between Chemistry and Biology in the Design of
Enzyme Catalyst, Schultz, P. (198) Science, 240, 426-433.
Hydrogen Tunneling in Enzyme Reaction, Cha, Y. (1989) Science,
243, 1325-1330.
How do Enzymes Work, Kraut, J. (1988) Science, 242, 533-540.
Catalysis: New Reaction Pathways, Not Just a Lowering of the
Activation Energy, Haim, A. (1989) J. Chem. Ed., 66, 935-937.
Enzyme Catalysis: Not Different, Just Better, Knowles, J.
(1991) Nature, 350, 121-124.
Enzyme Reactivity from an Organic Perspective, Menger, F.
(1993) Acc. Chem. Res., 26, 206-212.
Understanding the Rates of Certain Enzyme-Catalyzed
Reactions:Protein Abstraction from Carbon Acids,
Acyl-TransferReactions, and Displacement Reactions of
Phosphoidesters, Gerlt, J. & Gassman, P. (1993) Biochemistry,
32, 11943-11952.
Remarkable (1013) Rate Enhancement in Phosphonate Ester
Hydrolysis Catalyzed by Two Metal Ions, Tsubouchi & Bruice
(1994) J. Am. Chem. Soc., 116, 11614.
Our Primary Source of ATP, Cross, R. (1994) Nature, 370,
594-596
A Structural Explanation for Enzyme Memory in Nonaqueous
Solvents, Yennawar, H. et al. (1995) J. Am. Chem. Soc., 117,
577-585.
Why Nature Chose Phosphate, Westheimer, F. (1987) Science,
235, 1173-1178
Why Calcium?, Ochiai, E. (1991) J. Chem. Ed., 68, 10-12.
A Proficient Enzyme, Radzicka & Wolfenden, (1995) Science,
267, 90-93.