They turned the vamp around so I could see his face.

She could have been a real vamp, this dead girl.

If he could tell for dead certain they were vamps.

"You really think the vamp will come back to the house?"

He was one of the few vamps I'd known before and after death.

"I am not the one living in a church with a vamp!"

The only other vamp I'd ever met with a last name had been dead less than a month.

She was the most powerful vamp in his group right now.

Maybe it was her power that had made them so much more than most vamps.

That was the great thing about vamps, at least from my point of view: They were dead.

"Unless one vamp was strong enough to have mind control over Robert."

But the more vamps you get in an area, the higher your crime rate.

If the vamp had meant to take out more people, it could have.

Three male vamps moved a little distance from the man.

We matched up every vamp with at least one girl.

On the other hand, great, because the list of vamps that could do this was pretty small.

Most of the female Vamps were at least a hundred years old.

There was even a movement to give the vamps the vote.

Once upon a time I'd avoided looking any vamp in the eyes.

Plan was to put the vamps in the bags and take them back up.

Maybe a vamp will talk to me with you around."

There was no such thing as a life sentence for a vamp.

She'd been drained to death by a group of vamps.

Some of the vamps jumped at the small sound it made.

She was like most of the old vamps, a survivor at heart.

I have a man for you needs to be vamped on.

She was going to try to vamp Sam into telling her where he'd been last night.

At the same time he wondered why she was making this effort to vamp him.

It had been weeks since she vamped out on me, and never without warning.

So why, after seven years of vamping, is all this suddenly happening?

"But it seems like trying to vamp a holy man."

She was a tiny little thing, always trying to prove something by vamping him.

By now, she was either vamping like crazy or remembering someone else.

Terry had told him to vamp around, make up his own lyrics if he wanted.

"Is it just vamps or can he take over humans, too?"

Her outrageous outfits and vamping always bring down the house.

They look as if they're having fun, flirting and vamping.

For about half an hour after they began to bring us the proceedings, the networks vamped.

I saw no reason to vamp on the subject.

If only it weren't Justin she was trying to vamp!

His mother opened the door as he vamped away.

"Well, that should have told you something," Bill said, vamping like crazy.

And while she clearly enjoys vamping for photos, she's very serious about the music.

"I can vamp for time, but we need Peter's report now!

"Straight is trying to vamp you with his daughter."

In others he vamps it up with wigs and makeup.

Now, if she had been beautiful, they might have thought she could vamp him into telling.

They both whistled at Cynthia and she vamped it up for them.

He vamps and snaps at her, but remains tied to the chair.

When the man goes to the men's room, I want you to follow him in and start to vamp on him.

Complexin binds to the groove between the synaptobrevin and syntaxin helices.

Proteins such as synaptotagmin and synaptobrevin interact to fuse the vesicle into the membrane.

Complexin promotes interaction of the transmembrane regions of syntaxin and synaptobrevin.

The Tetanus toxin follows a similar pathway, but instead attacks the protein synaptobrevin on the synaptic vesicle.

Synaptobrevin is degraded by tetanospasmin, a protein derived from the bacterium Clostridium tetani, which causes tetanus.

A related bacterium, Clostridium botulinum, produces botulinum toxin that also hydrolyzes synaptobrevin.

EGR-1 has also been found to regulate the expression of synaptobrevin II (a protein important for synaptic exocytosis).

Vesicle-associated membrane protein 5 also known as VAMP5 is a human gene which encodes a member of the synaptobrevin protein family.

One particular R-SNARE is synaptobrevin, which is located in the synaptic vesicles.

Tetanospasmin appears to prevent the release of neurotransmitters by selectively cleaving a component of synaptic vesicles called synaptobrevin II.

Synaphin promotes neuronal exocytosis by promoting interaction between the complementary syntaxin and synaptobrevin transmembrane regions that reside in opposing membranes prior to fusion.

Synaptobrevin and syntaxin contribute one -helix each, while SNAP-25 participates with two -helices (abbreviated as Sn1 and Sn2).

By exploiting the rapid change in pH upon synaptic vesicle fusion, pHluorins tagged to synaptobrevin have been used to visualize synaptic activity in neurons.

Synaptobrevin is one of the SNARE proteins involved in formation of the SNARE complexes.

The action of the A-chain stops the affected neurons from releasing the inhibitory neurotransmitters GABA (gamma-aminobutyric acid) and glycine by degrading the protein synaptobrevin.

The toxin appears to act by selective cleavage of a protein component of synaptic vesicles, synaptobrevin II, and this prevents the release of neurotransmitters by the cells.

The VAMP5 gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family and the SNARE superfamily.

SNAP-25 is a Q-SNARE protein contributing two α-helices in the formation of the exocytotic fusion complex in neurons where it assembles with syntaxin-1 and synaptobrevin.

The SNARE (H3) domain binds to both synaptobrevin and SNAP-25 forming the core SNARE complex.

Südhof was also responsible for elucidating the action of tetanus and botulinum toxins, which selectively cleave synaptobrevin and SNAP-25, respectively, inhibiting vesicle fusion with the presynaptic membrane.

Out of four α-helices of the core SNARE complex one is contributed by synaptobrevin, one by syntaxin, and two by SNAP-25 (in neurons).

In neuronal exocytosis, syntaxin and synaptobrevin are anchored in respective membranes by their C-terminal domains, whereas SNAP-25 is tethered to the plasma membrane via several cysteine-linked palmitoyl chains.

The exact function of the protein is unknown: it interacts with the essential synaptic vesicle protein synaptobrevin, but when the synaptophysin gene is experimentally inactivated in animals, they still develop and function normally.

This light chain is an enzyme (a protease) that attacks one of the fusion proteins (SNAP-25, syntaxin or synaptobrevin) at a neuromuscular junction, preventing vesicles from anchoring to the membrane to release acetylcholine.

Formation of the "trans"-SNARE complex proceeds through an intermediate complex composed of SNAP-25 and syntaxin-1, which later accommodates synaptobrevin-2 (the quoted syntaxin and synaptobrevin isotypes participate in neuronal neuromediator release).