Phys. Rev. -- Table of Contents (October 2004, 84, (4))

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Contents: Volume 84, Issue 4; October, 2004. [Index by Author] [Editorial Board]

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Articles

Joseph W. Lynch: Molecular Structure and Function of the Glycine Receptor Chloride Channel
Physiol. Rev. 84: 1051-1095, 2004; doi:10.1152/physrev.00042.2003 [Abstract] [Full Text] [PDF]

Popi Syntichaki and Nektarios Tavernarakis: Genetic Models of Mechanotransduction: The Nematode Caenorhabditis elegans
Physiol. Rev. 84: 1097-1153, 2004; doi:10.1152/physrev.00043.2003 [Abstract] [Full Text] [PDF]

Andrzej Slominski, Desmond J. Tobin, Shigeki Shibahara, and Jacobo Wortsman: Melanin Pigmentation in Mammalian Skin and Its Hormonal Regulation
Physiol. Rev. 84: 1155-1228, 2004; doi:10.1152/physrev.00044.2003 [Abstract] [Full Text] [PDF]

M. Cereijido, R. G. Contreras, and L. Shoshani: Cell Adhesion, Polarity, and Epithelia in the Dawn of Metazoans
Physiol. Rev. 84: 1229-1262, 2004; doi:10.1152/physrev.00001.2004 [Abstract] [Full Text] [PDF]

Carsten A. Wagner, Karin E. Finberg, Sylvie Breton, Vladimir Marshansky, Dennis Brown, and John P. Geibel: Renal Vacuolar H⁺-ATPase
Physiol. Rev. 84: 1263-1314, 2004; doi:10.1152/physrev.00045.2003 [Abstract] [Full Text] [PDF]

Michael C. Brown and Christopher E. Turner: Paxillin: Adapting to Change
Physiol. Rev. 84: 1315-1339, 2004; doi:10.1152/physrev.00002.2004 [Abstract] [Full Text] [PDF]

Alex W. Cohen, Robert Hnasko, William Schubert, and Michael P. Lisanti: Role of Caveolae and Caveolins in Health and Disease
Physiol. Rev. 84: 1341-1379, 2004; doi:10.1152/physrev.00046.2003 [Abstract] [Full Text] [PDF]

Roland Stocker and John F. Keaney, Jr.: Role of Oxidative Modifications in Atherosclerosis
Physiol. Rev. 84: 1381-1478, 2004; doi:10.1152/physrev.00047.2003 [Abstract] [Full Text] [PDF]

Corrigenda

: Corrigendum for vol. 83, p. 475
Physiol. Rev. 84: 1479, 2004; doi:10.1152/physrev.00010.2004 [Full Text] [PDF]

Cover

Cover: The glycine receptor chloride channel is a member of the pentameric ligand-gated ion channel family. The cover figure shows a structural model of the inhibitory zinc binding site located at the interface between adjacent glycine receptor {alpha}1-subunits. The site is viewed radially outwards from the central water-filled cavity, and different subunits are denoted by different colors. The zinc atom, shown in pink, is coordinated primarily by His-107 from the positive (right) side of the interface and His-109 from the negative (left) side. In addition to the coordinating histidines, side chains of the nearby residues Glu-110 and Thr-112 are also shown. Dr. Brett Cromer and Prof. Michael Parker from St Vincent's Institute of Medical Research, Melbourne, Australia, are acknowledged for providing this unpublished image. See Lynch, Joseph W. Physiol Rev 84: 1051-1095, 2004.