@article {1437,
	title = {Expanding the thioglycoligase strategy to the synthesis of alpha-linked thioglycosides allows structural investigation of the parent enzyme/substrate complex},
	journal = {Journal of the American Chemical Society},
	volume = {128},
	number = {7},
	year = {2006},
	note = {ISI Document Delivery No.: 015PITimes Cited: 21Cited Reference Count: 12},
	month = {Feb},
	pages = {2202-2203},
	type = {Article},
	keywords = {ARCHAEON, DISEASE TYPE-II, IDENTIFICATION, MOLECULAR CHARACTERIZATION, MUTATIONS, PHENOTYPE},
	isbn = {0002-7863},
	url = {<Go to ISI>://000235562900024},
	author = {Kim, Y. W. and Lovering, A. L. and Chen, H. M. and Kantner, T. and McIntosh, L. P. and Strynadka, N. C. J. and Withers, S. G.}
}
@article {1301,
	title = {RS1, a discoidin domain-containing retinal cell adhesion protein associated with X-linked retinoschisis, exists as a novel disulfide-linked octamer},
	journal = {Journal of Biological Chemistry},
	volume = {280},
	number = {11},
	year = {2005},
	note = {ISI Document Delivery No.: 905HQTimes Cited: 33Cited Reference Count: 25},
	month = {Mar},
	pages = {10721-10730},
	type = {Article},
	abstract = {RS1, also known as retinoschisin, is an extracellular protein that plays a crucial role in the cellular organization of the retina. Mutations in RS1 are responsible for X-linked retinoschisis, a common, early-onset macular degeneration in males that results in a splitting of the inner layers of the retina and severe loss in vision. RS1 is assembled and secreted from photoreceptors and bipolar cells as a homo-oligomeric protein complex. Each subunit consists of a 157-amino acid discoidin domain flanked by two small segments of 39 and 5 amino acids. To begin to understand how the structure of RS1 relates to its role in retinal cell adhesion and X-linked retinoschisis, we have determined the subunit organization and disulfide bonding pattern of RS1 by SDS gel electrophoresis, velocity sedimentation, and mass spectrometry. Our results indicate that RS1 exists as a novel octamer in which the eight subunits are joined together by Cys(59)-Cys(223) intermolecular disulfide bonds. Subunits within the octamer are further organized into dimers mediated by Cys(40)-Cys(40) bonds. These cysteines lie just outside the discoidin domain indicating that these flanking segments primarily function in the octamerization of RS1. Within the discoidin domain, two cysteine pairs (Cys(63)-Cys(219) and Cys(110)-Cys(142)) form intramolecular disulfide bonds that are important in protein folding, and one cysteine (Cys(83)) exists in its reduced state. Because mutations that disrupt subunit assembly cause X-linked retinoschisis, the assembly of RS1 into a disulfide-linked homo-octamer appears to be critical for its function as a retinal cell adhesion protein.},
	keywords = {C2 DOMAIN, COAGULATION-FACTOR-V, CRYSTAL-STRUCTURES, EXPRESSION, FACTOR-VIII, GENE, JUVENILE RETINOSCHISIS, MUTATIONS, PHOTORECEPTOR, RESOLUTION},
	isbn = {0021-9258},
	url = {<Go to ISI>://000227559600118},
	author = {Wu, W. W. H. and Wong, J. P. and Kast, J. and Molday, R. S.}
}
@article {4273,
	title = {Covalent adduct formation with a mutated enzyme: Evidence for a thioester intermediate in the reaction catalyzed by UDP-glucose dehydrogenase},
	journal = {Journal of the American Chemical Society},
	volume = {120},
	number = {26},
	year = {1998},
	note = {ISI Document Delivery No.: ZZ420Times Cited: 15Cited Reference Count: 23},
	month = {Jul},
	pages = {6613-6614},
	type = {Article},
	keywords = {ALDEHYDE DEHYDROGENASE, biosynthesis, GENE, GROUP-A, HYALURONIC-ACID SYNTHESIS, INSERTION, MOLECULAR CHARACTERIZATION, MUTATIONS, PNEUMONIAE, STREPTOCOCCI, TYPE-3 CAPSULAR POLYSACCHARIDE},
	isbn = {0002-7863},
	url = {<Go to ISI>://000074727600028},
	author = {Ge, X. and Campbell, R. E. and van de Rijn, I. and Tanner, M. E.}
}
