Glycan in the context of "Carolyn R. Bertozzi"

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👉 Glycan in the context of Carolyn R. Bertozzi

Carolyn Ruth Bertozzi (born October 10, 1966) is an American chemist and Nobel laureate, known for her wide-ranging work spanning both chemistry and biology. She coined the term "bioorthogonal chemistry" for chemical reactions compatible with living systems. Her recent efforts include synthesis of chemical tools to study cell surface sugars called glycans and how they affect diseases such as cancer, inflammation, and viral infections like COVID-19. At Stanford University, she holds the Anne T. and Robert M. Bass Professorship in the School of Humanities and Sciences. Bertozzi is also an Investigator at the Howard Hughes Medical Institute (HHMI) and is the former director of the Molecular Foundry, a nanoscience research center at Lawrence Berkeley National Laboratory. Since 2024, she has served as a scientific advisory board member of Arc Institute.

She received the MacArthur "genius" award at age 33. In 2010, she was the first woman to receive the prestigious Lemelson–MIT Prize faculty award. She is a member of the National Academy of Sciences (2005), the Institute of Medicine (2011), and the National Academy of Inventors (2013). In 2014, it was announced that Bertozzi would lead ACS Central Science, the American Chemical Society's first peer-reviewed open access journal, which offers all content free to the public. Since 2021 she has been a member of the Accademia dei Lincei.

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Glycan in the context of Glycosylation

Glycosylation is the reaction in which a carbohydrate (or 'glycan'), i.e. a glycosyl donor, is attached to a hydroxyl or other functional group of another molecule (a glycosyl acceptor) in order to form a glycoconjugate. In biology (but not always in chemistry), glycosylation usually refers to an enzyme-catalysed reaction, whereas glycation (also 'non-enzymatic glycation' and 'non-enzymatic glycosylation') may refer to a non-enzymatic reaction.

Glycosylation is a form of co-translational and post-translational modification. Glycans serve a variety of structural and functional roles in membrane and secreted proteins. The majority of proteins synthesized in the rough endoplasmic reticulum undergo glycosylation. Glycosylation is also present in the cytoplasm and nucleus as the O-GlcNAc modification. Aglycosylation is a feature of engineered antibodies to bypass glycosylation. Five classes of glycans are produced:

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Glycan in the context of Oligosaccharide

An oligosaccharide (/ˌɒlɪɡˈsækəˌrd/; from Ancient Greek ὀλίγος (olígos) 'few' and σάκχαρ (sákkhar) 'sugar') is a saccharide polymer containing a small number (typically three to ten) of monosaccharides (simple sugars). Oligosaccharides can have many functions including cell recognition and cell adhesion.

They are normally present as glycans: oligosaccharide chains are linked to lipids or to compatible amino acid side chains in proteins, by N- or O-glycosidic bonds. N-Linked oligosaccharides are always pentasaccharides attached to asparagine via a beta linkage to the amine nitrogen of the side chain. Alternately, O-linked oligosaccharides are generally attached to threonine or serine on the alcohol group of the side chain. Not all natural oligosaccharides occur as components of glycoproteins or glycolipids. Some, such as the raffinose series, occur as storage or transport carbohydrates in plants. Others, such as maltodextrins or cellodextrins, result from the microbial breakdown of larger polysaccharides such as starch or cellulose.

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