Lingering mysteries of ubiquitin-chain assembly.

@article{citeulike:562956, abstract = {The small protein ubiquitin is often linked to substrates as a polymer. Such polymers vary in both linkage and length, which has important consequences for their function. Surprisingly, the mechanisms of ubiquitin-chain assembly are still not known. Deciphering them will shed light on why substrates differ in the extent and timing of polyubiquitin modification and how ancillary ubiquitination factors function.}, address = {Yale University, Department of Molecular Biophysics \& Biochemistry, New Haven, CT 06520, USA. mark.hochstrasser@yale.edu}, author = {Hochstrasser, M. }, citeulike-article-id = {562956}, doi = {http://dx.doi.org/10.1016/j.cell.2005.12.025}, issn = {0092-8674}, journal = {Cell}, month = {January}, number = {1}, pages = {27--34}, posted-at = {2006-03-25 11:37:43}, priority = {2}, title = {Lingering mysteries of ubiquitin-chain assembly.}, url = {http://dx.doi.org/10.1016/j.cell.2005.12.025}, volume = {124}, year = {2006} }

TY - JOUR ID - citeulike:562956 L3 - citeulike-article-id:562956 TI - Lingering mysteries of ubiquitin-chain assembly. JF - Cell VL - 124 IS - 1 SP - 27 EP - 34 AD - Yale University, Department of Molecular Biophysics & Biochemistry, New Haven, CT 06520, USA. mark.hochstrasser@yale.edu SN - 0092-8674 N2 - The small protein ubiquitin is often linked to substrates as a polymer. Such polymers vary in both linkage and length, which has important consequences for their function. Surprisingly, the mechanisms of ubiquitin-chain assembly are still not known. Deciphering them will shed light on why substrates differ in the extent and timing of polyubiquitin modification and how ancillary ubiquitination factors function. AU - Hochstrasser, M PY - 2006/01/13/ UR - http://dx.doi.org/10.1016/j.cell.2005.12.025 ER -