User:Mausfield

W:Wikipedian for 7 years, 7 months and 15 days

Please read Randy in space and WP:CHEESE to understand the nightmare that is having expertise in a topic on Wikipedia.

My created userboxes

This user loves sugars
and glycobiology.

This user (like you)
has a busted
CMAH enzyme.

Hello!

I am an evolutionary biologist interested in human origins, and in particular our unusual glycobiology and how it shapes our unique immune systems and life history. On Wikipedia my main project is improving articles related to those topics. For example, there are thousands of Wiki articles on glycoconjugate biomolecules and currently only 193 pages categorized as such!

What is glycobiology? What the heck is a glycoconjugate? Glad you asked ....

HALT, KNAVE!

To pass you must FIRST endure (aka "click on") the
~ SYMBOL NOMENCLATURE FOR GLYCANS ~

LYCOBIOLOGY is the study of the billions (yes, billions) of different combinatorial outcomes that occur when sugars (also called saccharides) are added to biomolecules in a process called glycosylation. The enzymes that do this work are glycosyltransferases (the adders) and glycosidases (the removers). For example: proteins, lipids, and amino groups can be glycosylated to yield glycoproteins, glycolipids, and glycosylamines, respectively.   The same type of protein may often have different layouts of sugars (or "glycans", once they're involved in this situation) which are called glycoforms, similar to protein isoforms. In mammals, the two major domains of protein-modifying glycans are N-glycans which attach to asparagine residues (in biology a "residue" is just an individual molecule when many of that molecule are involved in something) and O-glycans which attach to serine or threonine residues. N-glycans are a kind of family tree, in that they share a common starting point called the pentasaccharide core, seen below as the bottom two blue blocks (a sugar called N-acetylglucosamine or GlcNAc, pronounced "glook-nack", the funnest word in biology), the first mannose above them, and the two mannose residues above that.

O-glycans have several more starting core structures (and certainly more we have not found yet), and like N-glycans they do all kinds of amazing work in our biology, such as attracting a ton of water to form the mucous in our mucous membranes, providing the starting point for our bones, helping hundreds of our intracellular proteins fold in the right ways, and much more. Wikipedia is an incredible resource for biology around the world, and glyobiology has historically been under-appricated despite its intimate involvement in nearly every biological outcome. My main project on Wikipedia is increasing the recording of established understanding in glycobiology.

Now go join WikiProject: Molecular Biology and help CATEGORIZE!

Even a single sugar can have a huge effect on our biology, such as defining our ABO blood group (see right). If you have a regular galactose on your h-antigen precursor added by your trusty galactosyl transferase, you're in group B. If that galactose has an N-acetyl group on it because you have a fancy N-acetylgalactosaminyl transferase, you're in group A. If you have any of the various mutations that result in neither, you are stuck with the h-antigen precursor are in group O (go donate blood please). About 2–3 million years ago, someone in our lineage experienced a mutation that made them unable to produce a very common vertebrate sugar, a sialic acid called 5-glycolylneuraminic acid or Neu5Gc from its closely related starting material, Neu5Ac. This appears to have had widespread effects on our biology, at the very least making us molecularly invisible to the many pathogens which use Neu5Gc as their hook to get into target cells. Fun fact! The "H" in influenza strains (you've probably heard of H1N1) stands for a sugar-binding protein (also known as a lectin) called hemagglutinin. The "N" stands for neuraminidase (which is reall a sialidase), and lets influenza virus particles release themselves from the sugar-coated surfaces of our red blood cells by chopping off those same sugars they grabbed to get inside. Variations in these two proteins define the influenza (and many other pathogen) clades we care about in medicine, and have wide-ranging effects on how well a given flu spreads or affects someone who gets it.