Viewpoints:

Dispatches from the Frontlines of Research - edited by John W. Nelson

Isabelle M. Mansuy

STEPping into Position: A New Player in the NMDA Receptor Game
Mol. Interv. 2002 2: 282-284. [Summary] [Full Text] [PDF]  

Stephen R. Cronin

I’ll Simply Die Without My Calcium: Ca²⁺ Signaling and Surviving Cellular Stress
Mol. Interv. 2002 2: 284-285. [Summary] [Full Text] [PDF]  

Erik Sahai

p53 Moves Into Control of Cell Morphology
Mol. Interv. 2002 2: 286-289. [Summary] [Full Text] [PDF]  

Tooraj Mirshahi and Diomedes E. Logothetis

GIRK Channel Trafficking: Different Paths for Different Family Members
Mol. Interv. 2002 2: 289-291. [Summary] [Full Text] [PDF]  

R E V I E W S:

Jason M. Haugh

Localization of Receptor-Mediated Signal Transduction Pathways: The Inside Story
Mol. Interv. 2002 2: 292-307. [Summary] [Full Text] [PDF]  

The old conventional wisdom stated that internalized growth factor receptors were incapable of transmitting signals; however, new research indicates that internalized receptors can still send signals, but that the quality and quantity of those signals are likely to differ from those of their plasma-membrane-bound brethren. The maintenance of active pathways in concert with the deactivation of others allows for fine-tuning cellular responses to external stimuli. These findings have implications for cell motility, metabolism, and cell cycling.

P. Michael Conn, Alfredo Leaños-Miranda, and Jo Ann Janovick

Protein Origami: Therapeutic Rescue of Misfolded Gene Products
Mol. Interv. 2002 2: 308-316. [Summary] [Full Text] [PDF]  

Not only must proteins be synthesized, folded, and modified—processes that may all be related—but they must also be trafficked to appropriate subcellular destinations. Thus, the regulation of trafficking of any given protein may represent a means for the regulation of its function. The development of therapeutics that affect protein localization—either by nudging the reluctant protein on to a desired location or by stranding the overeager protein mid route—could become a specific way of targeting certain disease states.

Sergio E. Martinez, Joseph A. Beavo, and Wim G.J. Hol

GAF Domains: Two–Billion–Year–Old Molecular Switches that Bind Cyclic Nucleotides
Mol. Interv. 2002 2: 317-323. [Summary] [Full Text] [PDF]  

The cyclic nucleotides cAMP and cGMP bind to and regulate a vast variety of proteins including phosphodiesterases (PDEs), which act to terminate signaling. PDEs are thus important drug targets, a fact underscored by the success of Viagra(R). A key to the design of new PDE-targeting drugs may lie in an age-old trick—about two billion years old, to be precise. Specific protein motifs—the GAF domains—have evolved in mammals as well as cyanobacteria, and bind cyclic nucleotides to regulate a broad array of proteins. A newly described crystallographic structure gives us the first glimpse into the binding of a cyclic nucleotide to a GAF motif from a PDE, and provides important insights regarding the regulatory binding (as opposed to substrate binding) of cGMP.

D E P A R T M E N T S:

Speaking of Pharmacology:

Peter C. Preusch

What IS training in the Pharmacological Sciences?
Mol. Interv. 2002 2: 270-275. [Full Text] [PDF]  

CrossTalk:

Interviews with people in the world of pharmacology

40 Years as a Chemist at the NIH
Mol. Interv. 2002 2: 276-281. [Summary] [Full Text] [PDF]  

Beyond the Bench:

Representations of pharmacology and science in the media

Christine K. Carrico

Culinary Chemistry
Mol. Interv. 2002 2: 324-325. [Full Text] [PDF]  

Net Results:

Sites of interest on the World Wide Web

Sites of interest on the World Wide Web–edited by Rick Neubig
Mol. Interv. 2002 2: 326. [Full Text] [PDF]  

Outliers:

Cartoon

Mol. Interv. 2002 2: 334. [Full Text] [PDF]  

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