Operator's manual : testing kit, impregnite-in-clothing, ABC-M2, NSN 6630-00-783-8192 and impregnating set, clothing, field, M3, NSN 4230-00-368-6145.

"May 1986."

Organizational, direct support, general support and depot maintenance manual including repair parts and special tools list : machine gun, caliber .50, Browning, M2, heavy barrel, flexible, W/E (1005-322-9715), mount, tripod, machine gun, M3, W/E (1005-322-9716), mount, machine gun, antiaircraft, M63 ... commander's cupola (1005-013-6944).

"July 1968."

Operator's manual : machine gun, caliber .50, Browning, M2, heavy barrel, flexible, W/E (1005-322-9715), mount, tripod, machine gun, caliber .50, M3, W/E (1005-322-9716), mount, machine gun, antiaircraft, M63 ....

"14 June 1985"--Change 6.

Operator's manual : fighting vehicle, infantry, M2 (2350-01-048-5920) and fighting vehicle, cavalry, M3 (2350-01-049-2659) hull.

Includes index.

Direct support and general support maintenance : fighting vehicle, infantry, M2 (2350-01-048-5920) and fighting vehicle, cavalry, M3 (2350-01-049-2695), hull.

Includes index.

Technical manual, operator's manual : fighting vehicle, infantry, M2 (2350-01-048-5920) and fighting vehicle, cavalry, M3 (2350-01-049-2695), turret.

At head of title: Advance copy.

Technical manual organizational maintenance : fighting vehicle, infantry, M2 (2350-01-048-5920) and fighting vehicle, cavalry, M3 (2350-01-049-2695) turret.

Includes indexes.

Hand receipt covering content of Components of End Item (COEI), Basic Issue Items (BII), and Additional Authorization List (AAL) for fighting vehicle, infantry, M2, (2350-01-048-5920) and fighting vehicle, cavalry, M3, (2350-01-049-2695).

"August 1984."

Direct support and general support maintenance : fighting vehicle, Infantry, M2 (2350-01-048-5920) and fighting vehicle, Cavalry, M3 (2350-01-049-2695) turret.

Includes index.

Unit support, intermediate direct support, and intermediate general support maintenance repair parts and special tools list (including depot maintenance repair parts and special tools) for fighting vehicle, infantry, M2, (2350-01-048-5920), fighting vehicle, infantry, M2A1, (2350-01-179-1027), fighting vehicle, cavalry, M3, (2350-01-049-2695) ....

"9 February 1987."

Unit maintenance : fighting vehicle, infantry, M2, (2350-01-048-5920), M2A1 (2350-01-179-1027), and fighting vehicle, cavalry, M3 (2350-01-049-2695), M3A1 (2350-01-179-1028), turret.

"December 1986"--Vol. 3.

Unit maintenance : fighting vehicle, infantry, M2, (2350-01-048-5920), M2A1 (2350-01-179-1027), and fighting vehicle, cavalry, M3 (2350-01-049-2695), M3A1 (2350-01-179-1028), turret.

"December 1986"--Vol. 3.

On strongly regular graphs with m2 = qm3 and m3 = qm2

2010 Mathematics Subject Classification: 05C50.

Paired activation of two components within muscarinic M3 receptor dimers is required for recruitment of beta-arrestin-1 to the plasma membrane.

beta-Arrestins regulate the functioning of G protein-coupled receptors in a variety of cellular processes including receptor-mediated endocytosis and activation of signaling molecules such as ERK. A key event in these processes is the G protein-coupled receptor-mediated recruitment of beta-arrestins to the plasma membrane. However, despite extensive knowledge in this field, it is still disputable whether activation of signaling pathways via beta-arrestin recruitment entails paired activation of receptor dimers. To address this question, we investigated the ability of different muscarinic receptor dimers to recruit beta-arrestin-1 using both co-immunoprecipitation and fluorescence microscopy in COS-7 cells. Experimentally, we first made use of a mutated muscarinic M(3) receptor, which is deleted in most of the third intracellular loop (M(3)-short). Although still capable of activating phospholipase C, this receptor loses almost completely the ability to recruit beta-arrestin-1 following carbachol stimulation in COS-7 cells. Subsequently, M(3)-short was co-expressed with the M(3) receptor. Under these conditions, the M(3)/M(3)-short heterodimer could not recruit beta-arrestin-1 to the plasma membrane, even though the control M(3)/M(3) homodimer could. We next tested the ability of chimeric adrenergic muscarinic alpha(2)/M(3) and M(3)/alpha(2) heterodimeric receptors to co-immunoprecipitate with beta-arrestin-1 following stimulation with adrenergic and muscarinic agonists. beta-Arrestin-1 co-immunoprecipitation could be induced only when carbachol or clonidine were given together and not when the two agonists were supplied separately. Finally, we tested the reciprocal influence that each receptor may exert on the M(2)/M(3) heterodimer to recruit beta-arrestin-1. Remarkably, we observed that M(2)/M(3) heterodimers recruit significantly greater amounts of beta-arrestin-1 than their respective M(3)/M(3) or M(2)/M(2) homodimers. Altogether, these findings provide strong evidence in favor of the view that binding of beta-arrestin-1 to muscarinic M(3) receptors requires paired stimulation of two receptor components within the same receptor dimer.

A conserved basic loop in hepatitis C virus p7 protein is required for amantadine-sensitive ion channel activity in mammalian cells but is dispensable for localization to mitochondria

We previously identified the function of the hepatitis C virus (HCV) p7 protein as an ion channel in artificial lipid bilayers and demonstrated that this in vitro activity is inhibited by amantadine. Here we show that the ion channel activity of HCV p7 expressed in mammalian cells can substitute for that of influenza virus M2 in a cell-based assay. This was also the case for the p7 from the related virus, bovine viral diarrhoea virus (BVDV). Moreover, amantadine was shown to abrogate HCV p7 function in this assay at a concentration that specifically inhibits M2. Mutation of a conserved basic loop located between the two predicted trans-membrane alpha helices rendered HCV p7 non-functional as an ion channel. The intracellular localization of p7 was unaffected by this mutation and was found to overlap significantly with membranes associated with mitochondria. Demonstration of p7 ion channel activity in cellular membranes and its inhibition by amantadine affirm the protein as a target for future anti-viral chemotherapy.