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Document Page 463 change of the hemagglutinin necessary for fusion. Drug-resistant mutants arise where the hemagglutinin trimers are thought to be less stable than the wild type [14]. At low concentrations (
Document Page 464 could not again be agglutinated by either the eluted virus or fresh virus preparations. This activity is now attributed to neuraminidase, which is one of the two integral membrane glycoproteins of influenza virus (for reviews see References 24 and 25). A. Function Neuraminidase is an exoglycosidase that destroys the hemagglutinin receptor by cleaving the αketosidic linkage of terminal sialic acid [(N-actylneuraminic acid (Neu5Ac))] to an adjacent sugar [26,27]. Viral hemagglutinin binds specifically to Neu5Ac-containing receptors on the surface of susceptible cells [28]. Neuraminidase, which also removes terminal sialic acid from a range of glycoconjugates, plays an important, but not completely understood, role in the viral replication cycle. Without neuraminidase activity viruses [29] were thought to be immobilized by mucosal secretions in the upper respiratory tract. By removing terminal sialic acid from the sialic-acid-rich mucous layer [27,30] protecting target cells, neuraminidase could facilitate penetration of the virus to the cell surface. It has been shown that neuraminidase-deficient virus [31] can still replicate in vivo, albiet at a much reduced rate [32]. This shows that neuraminidase does not play an essential role in viral entry, replication, assembly or budding in mice, but has an important role in the spread of the infection by preventing aggregation at the cell surface and possible immobilization in the mucin by hemagglutinin. Once replication is initiated in the infected cell, the freshly synthesised viral glycoproteins have to be desialylated to prevent self-aggregation at the infected host cell surface by hemagglutinin binding to terminal sialic acid on these glycoproteins. Finally on elution of progeny virions from infected cells, neuraminidase activity is required to facilitate viral escape from the cell surface. Inactivation or inhibition of neuraminidase during budding has been observed to result in aggregation of virions on the cell surface [33–35]. Inhibition of this glycohydrolase could provide a means of controlling this disease by slowing the rate of viral attachment and subsequent release of progeny virions allowing the host immune system to eliminate the virus while the number of infected cells is low. B. Morphology There are between 50 to 100 neuraminidase spikes per virion [36] which is approximately 10% of the visible spikes projecting out of the surface of the virion [37]. These spikes can be removed from the virus by treatment with detergent [38]. Electron microscopic images of the neuraminidase spikes [39] reveal a mushroom-shaped molecule made up of a boxlike head of about 80 × http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_464.html [4/9/2004 12:13:17 AM]
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Structure-based Drug Design 14 Stru
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Document 74. Reddy RM, Varney MD, K
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Document 2 Structural Studies of HI
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Document dine (3TC), and 2',3'-dide
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Document Analysis of various HIV-1
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Document Page 54 Table 2) [12,54].
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Document Page 56 It is also attract
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Document Table 3 HIV-1 RT Amino Aci
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Document ever, once an NNRTI is bou
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Document Page 61 now clear that the
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Document Page 67 Biochemical data s
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Document Page 69 determining the me
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Document Chris Tantillo. The work i
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Document Page 72 16. Goldman ME, Nu
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Document 30. Coffin JM. HIV populat
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Document 45. Majumadar C, Abbotts J
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Document reverse transcriptase inhi
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Document 106. Cirino NM, Cameron CE
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Document 122. Marshall WS, Beaton G
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Document dine) and didanosine (dide
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Document 163. Lacey SF, Larder BA.
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Document Page 96 region in the HIV-
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Document -62° for HIV-1 integrase,
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Document Page 106 on the same ring
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Document Page 108 mulate during tre
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Document when metals are bound. Fin
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Document cubation of phosphotyrosin
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Document 4 Bradykinin Receptor Anta
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Document Page 121 Nearly all cells
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Document Page 123 were poorly satis
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Document Page 125 binding site on t
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Document receptor, it has not yet b
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Document Figure 6 Rat and human B2
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Document Page 141 receptor with int
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Document Figure 9 Composition of te
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Document We determined the structur
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Document Figure 3 Previously known
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Document Page 166 As predicated, th
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Document 17. Ealick SE, Rule SA, Ca
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Document 6 Structural Implications
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Document Page 176 0.43 Å) as the c
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Document IX. S2' Interactions Page
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Document 7 Structure—Function Rel
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Document Important for the validity
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Document Figure 4 Amino acids impor
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Document III. Results and Discussio
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Document Page 202 269, and valine-2
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Document Figure 6 Structure of α h
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Document Page 205 enzyme and of phe
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Page 541 and 542: Document 17 Structure and Functiona
Page 543 and 544: Document Table 1 Approval Indicatio
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Page 547 and 548: Document II. Type IFNs A great deal
Page 549 and 550: Document Page 441 sequence of the m
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Page 553 and 554: Document Figure 4 Stereo view of IF
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Page 557 and 558: Document Figure 6 Proposed receptor
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Page 567 and 568: Document 47. Igarashi K, Garotta G,
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Page 579 and 580: Document B. Protein Structure Page
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Page 583 and 584: Document Page 471 molecules in the
Page 585 and 586: Document hydroxy, and 6 Neu5Ac2en -
Page 587 and 588: Document Figure 8 Stereo image of t
Page 589 and 590: Document Page 476 nM, respectively.
Page 591 and 592: Document Page 478 lished—was asso
Page 593 and 594: Document VI. Conclusion Page 480 It
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Page 611 and 612: Document A. The Canyon Page 491 The
Page 613 and 614: Document Subsequent studies have sh
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Page 617 and 618: Document Figure 4 A ribbon diagram
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Document Acknowledgments Page 620 I
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Document Cyclotheonamide A (CtA), 2
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Document D ddI, 152 tumour necrosis
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Document antistasin peptides, 281 c
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Document fragment-based programs, 5
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Document [Human immunodeficiency vi
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Document Phosphoglycerate kinase (P
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Document [Protease targets] serinyl
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