This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.More than half of the proteins in mammals, specifically in humans, are glycosylated through linkages to asparagine (N-linked glycans) or serine/threonine (O-linked glycans) and ocassionally other sites as well. The absence or diminished expression of glycosidases and glycosyl transfereases that are involved in the assembly of glycans can lead to severe disease, now generically referred to as 'congenital disorders of glycosylation (CDGs). The aberrant pathways in some CDGs have been defined, but numerous new cases are being recognized. It is sometimes difficult to determine the specific structures of the resulting glycans, especially when the modification or presence of multiple pathways or incomplete penetrance of the disorder leads to the production of glycosylation mixtures. The Resource collaborated with Prof. Freeze and his colleagues to unravel the glycan structures and thereby to deduce the genetic aberration in a recent case that resulted in the definintion of a new congenital disorder of glycosylation, type IIh, that involves a deficiency of COG8.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR010888-11
Application #
7602059
Study Section
Special Emphasis Panel (ZRG1-BCMB-H (40))
Project Start
2007-08-03
Project End
2008-05-31
Budget Start
2007-08-03
Budget End
2008-05-31
Support Year
11
Fiscal Year
2007
Total Cost
$16,160
Indirect Cost
Name
Boston University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
604483045
City
Boston
State
MA
Country
United States
Zip Code
02118
Lu, Yanyan; Jiang, Yan; Prokaeva, Tatiana et al. (2017) Oxidative Post-Translational Modifications of an Amyloidogenic Immunoglobulin Light Chain Protein. Int J Mass Spectrom 416:71-79
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Steinhorn, Benjamin S; Loscalzo, Joseph; Michel, Thomas (2015) Nitroglycerin and Nitric Oxide--A Rondo of Themes in Cardiovascular Therapeutics. N Engl J Med 373:277-80

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