Structural biology: Actin in a twist Export

@article{citeulike:3921987, abstract = {How monomers of the cytoskeletal protein actin join to form the stable polymers crucial to muscle contraction and cellular motility has been a long-standing question. A state-of-the-art approach provides an answer. The actin protein is abundant in all eukaryotic cells (those characterized by a membrane-bound nucleus), and is particularly prevalent in muscle, where it comprises about 20\% of the total mass. Actin comes in two forms: monomeric, globular G-actin; and polymeric, filamentous F-actin.}, author = {Holmes, Kenneth C.}, citeulike-article-id = {3921987}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/457389a}, citeulike-linkout-1 = {http://dx.doi.org/10.1038/457389a}, day = {21}, doi = {10.1038/457389a}, issn = {0028-0836}, journal = {Nature}, keywords = {actin, commentary, structure}, month = {January}, number = {7228}, pages = {389--390}, posted-at = {2009-01-21 22:16:46}, priority = {0}, publisher = {Nature Publishing Group}, title = {Structural biology: Actin in a twist}, url = {http://dx.doi.org/10.1038/457389a}, volume = {457}, year = {2009} }

TY - JOUR ID - citeulike:3921987 L3 - citeulike-article-id:3921987 N2 - How monomers of the cytoskeletal protein actin join to form the stable polymers crucial to muscle contraction and cellular motility has been a long-standing question. A state-of-the-art approach provides an answer. The actin protein is abundant in all eukaryotic cells (those characterized by a membrane-bound nucleus), and is particularly prevalent in muscle, where it comprises about 20% of the total mass. Actin comes in two forms: monomeric, globular G-actin; and polymeric, filamentous F-actin. IS - 7228 JF - Nature SN - 0028-0836 EP - 390 TI - Structural biology: Actin in a twist PB - Nature Publishing Group VL - 457 SP - 389 KW - actin KW - commentary KW - structure AU - Holmes, Kenneth PY - 2009/01/21/ UR - http://dx.doi.org/10.1038/457389a ER -