Before and after

37C incubator
Before:


After:



Aliens came down and abducted our sterile pipette tips, eppendorf tubes and conical flasks, not to forget our half-dried Nature/Science/Cell-publication quality western blots and plaque assay wells! ARGH! Lazy aliens, who don't even try to pack, seal, autoclave, dry and store thier own lab consumables.

GASP!
panic!

NaAaH....

Got them transfered to the next door lab:



See how neat they all are now? (ahemm, ahemm... who did it?)



Done under directive of the great Half-day.
And where did all the stuff in the shelves got displaced to?


Reminds me of Jengga.

fun with co2

forgot to add this pic of me playing with the dry ice:

new paper

link --> here

J Biol Chem. 2005 Nov 7; [Epub ahead of print]

Quantifying the specific binding between west nile virus envelope domain III protein and the cellular receptor alpha Vbeta 3 integrin.
Lee JW, Chu JJ, Ng ML.

Previous study has illustrated that the aVss3 integrin served as the functional receptor for West Nile virus (WNV) entry into cells. Domain III (DIII) of WNV envelope protein (E) was postulated to mediate virus binding to the cellular receptor. In this study, the specificity and affinity binding of WNV E DIII protein to aVss3 integrin was confirmed with co-immunoprecipitation and receptor competition assay. Binding of WNV E DIII protein to aVss3 integrin induced the phosphorylation of focal adhesion kinase that is required to mediate ligand-receptor internalization into cells. A novel platform was then developed using the atomic force microscopy (AFM) to measure this specific binding force between WNV E DIII protein and the cellular receptor, aVss3 integrin. The single protein pair interacting force measured was in the range of 45+/-5 picoNewton (pN). This interacting force was highly specific as minimal force was measured in the WNV E DIII protein interaction with aVss5 integrin molecules and heparan sulphate. These experiments provided an insight to quantitate virus-receptor interaction. Force measurement using AFM can serve to quantitatively analyze the effect of candidate drugs that modulate virus-host receptor affinity.

box

Two totally unrelated pictures.
A box of infectious stuff. Euuuu...
Don't ask me what's inside, all i know is that I have dry ice to play with later :)

And secondly, Christmas deco are appearing all over town! Yay!

Inverted ice-cream cones good for the hot weather here.

More Bacon, Please

Now I really know why I am thin.
hahha

As any chef at a greasy spoon can attest, humans have a taste for fatty foods. Now, scientists may know why. Researchers have found a new receptor on mice and rat tongues that detects fat and helps prepare the body to digest it. The results may help explain why some people crave fat more than others and could help researchers uncover new ways to fight obesity.
It's long been clear that humans and rodents taste sweet, sour, bitter, salty, and protein-rich foods, but researchers thought we sensed the fat in food by its smell and creamy texture. Over the past decade or so, however, results have dribbled in suggesting we--or at least mice and rats--taste fats. In one study, applying a chemical to the tongue that blocks a fat-digesting enzyme prevented rats and mice from tasting fats and fatty acids, a breakdown product of fats.Intrigued, physiologist Philippe Besnard of the University of Bourgogne in Dijon, France, and colleagues focused on a fatty-acid receptor called CD36 that's found in fat and other tissues. After chemically linking a red fluorescent dye to antibodies that bound CD36, the researchers showed that taste buds glowed red, indicating that CD36 was in the right place to do the job.
To see if animals use CD36 to taste fats, the team bred a line of mice that lacked the receptor. When given a choice between their standard fare and fat-enriched treats, normal mice consumed 3 times as much of the junk food, but mutant mice showed no preference, presumably because they couldn't taste the difference.
The taste bud receptors send a signal when they sense fat. The researchers learned this by applying fatty acids to the tongues of mice that had their digestive tracts tied off to prevent ingestion. Normal mice--but not those lacking the CD36 receptors-- immediately cranked up their production of bile, which breaks down fats, the researchers report in the November issue of the Journal of Clinical Investigation. The results indicate that CD36 helps relay a signal to the digestive system, telling it to get ready to digest fats; receptors that taste sweetness relay similar signals.
Because genetic variants of CD36 exist in humans, studies of the receptor in humans could help explain why some people crave fat more than others do. Scientists could potentially uncover compounds that block CD36, which could cut fat cravings and combat obesity, says biochemist Nada Abumrad at Washington University School of Medicine in St. Louis, Missouri. That's still in the future, but the research is a good start, she says. "The work was very well done."
--DAN FERBER
ScienceNow 2nd November 2005
Copyright © 2005 by the American Association for the Advancement of Science