F John Gennari, MD Associate Chair for Academic Affairs, Robert F and Genevieve B Patrick Professor, Department of Medicine, University of Vermont College of Medicine
F John Gennari, MD is a member of the following medical societies: Alpha Omega Alpha , American College of Physicians-American Society of Internal Medicine , American Federation for Medical Research , American Heart Association , American Physiological Society , American Society for Clinical Investigation , American Society of Nephrology , International Society of Nephrology
Disclosure: Nothing to disclose.
Protein Modification Description Cross-linking is a method of covalently joining two proteins.
Cross-linkers contain reactive ends to specific functional groups (primary amines, sulfhydryls, etc.) on proteins or Cross-linking other molecules. Several chemical groups may be targets for reactions in proteins and peptides. For example, Ethylene glycol bis[succinimidylsuccinate, Bis[2-(succinimidooxycarbonyloxy)ethyl]sulfone, and Bis[sulfosuccinimidyl] suberate link amines to amines.
For example, cyclization of amino acids to create optimized Cyclization delivery forms that are resistant to, ., aminopeptidases (., formation of pyroglutamate, a cyclized form of glutamic acid).
Disulfide bonds in proteins are formed by thiol-disulfide Disulfide bond formation exchange reactions, particularly between cysteine residues (., formation of cystine).
Demethylation See, ., . 4,250,088 (Process for demethylating lignin).
The addition of a formyl group to, ., the N-terminus of a Formylation protein. See, ., . Patent Nos. 4,059,589, 4,801,742, and 6,350,902.
Glycylation The covalent linkage of one to more than 40 glycine residues to the tubulin C-terminal tail.
Glycosylation may be used to add saccharides (or polysaccharides) to the hydroxy oxygen atoms of serine and threonine side chains (which is also known as 0-linked Glycosylation Glycosylation). Glycosylation may also be used to add saccharides (or polysaccharides) to the amide nitrogen of asparagine side chains (which is also known as N-linked Glycosylation), ., via oligosaccharyl transferase.
The addition of glycosylphosphatidylinositol to the C-terminus of a protein. GPI anchor formation involves the addition of a hydrophobic phosphatidylinositol group -GPI anchor formation linked through a carbohydrate containing linker (., glucosamine and mannose linked to phosphoryl ethanolamine residue) - to the C-terminal amino acid of a protein.