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For controllers that do support scatter-gather, because the hardware imposes the structure of the descriptor, it is dif cult to include any additional descriptor information required by the framework alone. Therefore, the framework associates a separate descriptor header with each descriptor. This is the SDmaDesHdr structure. The descriptor header is generic and the PIL manipulates descriptors via their associated header. The framework still creates associated descriptor headers even when pseudo descriptors are used. Each time a driver opens a channel, it has to supply information on the number of descriptors that the framework should reserve for it. This depends on the buffering scheme being used and the maximum number of DMA requests that are likely to be outstanding at any time. The class DDmaRequest encapsulates a DMA request over a channel. This is the second main element of the DMA device driver API. The main public parts of this class and data members are as follows:

350 300 Alive Particles 250 200 150 100 50 0 0 2 4 6 8 10 12 14 16 18 20 22 24 26 28 30 32 Distance from Sink (section)

In Vitro Antiviral Activity of Early and Late Inhibitors of Arenaviruses Viruses JUNV, TCRV LCMV, LASV JUNV JUNV, TCRV, PICV JUNV JUNV, TCRV JUNV, TCRV JUNV, TCRV JUNV, TCRV, PICV JUNV, TCRV, PICV JUNV, TCRV JUNV JUNV, TCRV, PICV Target Early Early Early Early/late Early Early/late Late Late Late/virion Late Late Late Late References 67,83 77 85 95 96 99,100 112 113 134,138,139 142 144 145 146

Figure 15.21. Alive particles (hA ) for VTRPp at different time instances (n = 5000).

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class DDmaRequest : public DBase { public: // Signature of completion/failure callback function typedef void (*TCallback)(TResult, TAny*); public: DDmaRequest(TDmaChannel& aChannel, TCallback aCb=NULL, TAny* aCbArg=NULL, TInt aMaxTransferSize=0); DDmaRequest(); TInt Fragment(TUint32 aSrc, TUint32 aDest, TInt aCount, TUint aFlags, TUint32 aPslInfo); void Queue(); public: TDmaChannel& iChannel; TCallback iCb; TAny* iCbArg; TInt iDesCount; SDmaDesHdr* iFirstHdr; SDmaDesHdr* iLastHdr; };

Polysulfates Soluble a-dystroglycan Procaine, chlorpheniramine, ammonium chloride Tri uoperazine, chlorpromazine Caffeine Meliacine Myristic acid analogues Lauric acid Aromatic disul des, dithianes, azodicarboamide Brassinosteroids Macrocyclic trichothecenes Thiosemicarbazone derivatives Cecropin A

particle to S increases (see Figure 15.14), the strategy of making small steps becomes inef cient. The series of small increments in the transmission range and failed searches waste the power sources of the particles and eventually cause the death of the particle before the information reaches the sink.

//Channel this request is bound to //Called on completion/failure //Callback argument //Number of fragments in list //The first fragment in the list. //The last fragment in the list.

350 300 Alive Particles 250 200 150 100 50 0 0 2 4 6 8 10 12 14 16 18 20 22 24 26 28 30 32 Distance from Sink (section)

different classes of polysulfates, including sulfated polysaccharides (dextran sulfate, heparin, pentosan polysulfate), polyacetal polysulfate, and polyvinylalcohol sulfate and its copolymer with acrylic acid, were found to be highly selective inhibitors of JUNV and TCRV replication (Table 5.2).67,83 For other enveloped viruses, including HIV, herpesviruses, and papillomaviruses, the antiviral activity of these negatively charged molecules has been attributed to an interference with virus adsorption by blockade of the interaction between the cellular receptor and the virion external glycoprotein.83 However, potential clinical application of these kinds of agents against viral hemorrhagic fevers has not been investigated. Entry After binding to the cell receptor, arenaviruses enter into the host cell through an endocytic pathway. The complete process includes virion uptake into vesicles followed by a low pH-dependent fusion of viral envelope and endosome membranes, and nally the nucleocapsid is released into the cytoplasm. The mode of entry of arenaviruses by endocytosis relied on results provided by different experimental approaches. The sensitivity of early events in the arenavirus replicative cycle to lysosomotropic compounds was the rst evidence of an endosomal route of entry. Weak bases, such as ammonium chloride and chloroquine, as well as carboxylic ionophores, such as nigericin and monensin, were effective inhibitors of the internalization of several arenaviruses, including LASV, MOPV, PICV, JUNV, and LCMV.84 86 Both classes of compounds raise the endosomal pH either by protonization of the base in the acidic vesicle or by exchange of H for Na /K , respectively, and under these conditions arenavirus

Typically a driver will allocate itself one or more request objects for each channel that it has open. The constructor for the DDmaRequest class is

Figure 15.22. Alive particles (hA ) for VTRPr at different time instances (n = 5000).

internalization is inhibited Accordingly, the blockade in JUNV infection induced by weak bases could be overcome by buffering the extracellular medium at a pH below 60, a treatment that allowed direct fusion of virus envelope with the cell membrane85 Lysosomotropic compounds have side effects on other cellular functions, which can affect virus multiplication; but the mechanism of entry of arenaviruses was con rmed using agents targeted speci cally to the components of the endocytic pathway The macrolide antibiotics ba lomycin A1 and concanamycin A, which are speci c inhibitors of the vacuolar proton ATPase, the enzyme responsible for maintaining the low pH of endosomes, inhibited simultaneously JUNV penetration and vesicle acidication87 Furthermore, the presence of LCMV particles inside vesicles during virus entry into the cell was visualized by immunoelectronmicroscopy.

as follows:

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