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1 ific RNA-induced stabilisation of a trimeric capsomere.
2 id protein, each of which forms an arch-like capsomere.
3 ting the cytoplasmic assembly of papovavirus capsomeres.
4 l hollow spikes that clustered into distinct capsomeres.
5 an interconnected network within and across capsomeres.
6 tiple domains capable of interacting with L1 capsomeres.
7 s, respectively, which compose the hexameric capsomeres.
8 tained one monomer from each of two adjacent capsomeres.
9 g the local symmetry axes of the surrounding capsomeres.
10 molecules of both pentavalent and hexavalent capsomeres.
11 es for the 5B6 epitope in the 12 pentavalent capsomeres.
12 igenic domains are contained entirely within capsomeres.
13 americ capsomeres and capsids composed of 72 capsomeres.
14 apsomeres and flexible links that form among capsomeres.
15 he corresponding N termini of the pentameric capsomere A subunits were not visible at all in electron
16 omogeneity as pentamers (equivalent to viral capsomeres), after thrombin cleavage from the GST moiety
20 n the cytoplasm, L1 and VP1 pentamerize into capsomeres and are then imported into the nucleus using
22 equence of stable contacts that occur within capsomeres and flexible links that form among capsomeres
23 The absence of mAb 5B6 from the pentavalent capsomeres and its inability to prevent viral binding to
24 nsition could occur by shedding of hexameric capsomeres and restructuring of remaining pentamers acco
26 and partially degraded capsids with missing capsomeres; and 5) the DNA extruded from damaged virions
28 ly and bivalently to the sides of hexavalent capsomeres approximately two-thirds of the way down from
29 avirus family) are composed of 72 pentameric capsomeres arranged on a skewed icosahedral lattice (tri
31 found that recombinant MCPyV VP1 pentameric capsomeres both hemagglutinated sheep red blood cells an
33 and human papillomavirus type 11 (HPV11) L1 capsomeres bound the karyopherin heterodimer alpha2beta1
34 helix (helix 2(58-72)) is likely involved in capsomere-capsomere interactions during shell accretion.
35 along with fragments of the membrane; 3) the capsomeres composing the capsid and their surface arrang
36 sts that the cross-linked species is a cross-capsomere contact between a pentamer and hexamer at the
37 er at the quasi-threefold axis or is a cross-capsomere contact between hexamers at the threefold axis
39 y of purified HPV-11 L1 VLPs to the level of capsomeres, demonstrating that disulfide bonds alone are
40 ical arrangements of the VP5 subunits in the capsomeres exposes different residues, resulting in the
41 he B and C subunits comprising the hexameric capsomeres formed an annulus about the interior of the c
44 The particles are composed of pentameric capsomeres from the wild-type virions which have reorien
45 /or neutralizing monoclonal antibodies, both capsomeres generated by disulfide reduction of purified
46 highly immunoreactive with trypsin-generated capsomeres in an enzyme-linked immunosorbent assay (ELIS
47 JAM-A), which binds to the outer face of the capsomere, inducing a conformational change in the capsi
49 he region of maximum contact, papillomavirus capsomeres interact in a manner similar to that found in
51 1 fusion protein formed pentamers, but these capsomere-like structures did not assemble into VLPs.
53 pproximately 60 versus approximately 50 nm), capsomere morphology (11 to 12 nm star-shaped versus 8 n
55 rus (papovavirus) capsids are composed of 72 capsomeres of their major capsid proteins, VP1 and L1, r
56 of the particles, exhibited arrangements of capsomeres on their surfaces which were consistent with
57 actions (slightly different contacts between capsomeres), papovavirus capsids have a conserved, 72-pe
60 In contrast, 5B6 binds only to hexavalent capsomeres, reflecting the significant structural or env
61 intact L1 protein, likely still arranged as capsomeres, remains associated with the incoming viral g
62 ired to form both pentavalent and hexavalent capsomeres result in structures that exhibit very differ
63 onent of the triplexes that connect adjacent capsomeres), results in the formation of spherical parti
64 pose that the L1 protein, likely arranged as capsomeres, stabilizes the viral genome within the subvi
65 t-subunit interactions within and across the capsomeres that are required to stabilize the virus.
66 n can be trypsinized to generate recombinant capsomeres that retain HPV genotype-restricted capsid an
67 ized HeLa cells were incubated with HPV16 L1 capsomeres, the L1 protein was imported into the nucleus
69 plays a distinctive skewing of the hexameric capsomeres, to the mature virion, which is larger and mo
70 rified VLPs and reassembled VLPs formed from capsomeres upon removal of reducing agents exhibited epi
72 to these epitopes and requires assembly into capsomeres, we propose that L1 protein is present in the
73 was resolved to a resolution of 6.1 nm, and capsomeres were observed to be arranged on the virus sur
75 e 3-fold axis at the center of the hexameric capsomere, where there is a pore of about 6 A diameter.
76 hat mAb #9 binds monovalently to the tips of capsomeres whereas 5B6 binds both monovalently and bival
77 ull-length L1 protein appeared as pentameric capsomeres which self-assembled into capsid-like particl
78 r particle at the center of the 20 hexameric capsomeres, which are a direct result of the K42R mutati
79 an assembly of loosely associated hexameric capsomeres, which may be the basis for the swelling and
80 formed an annulus about the interior of the capsomere, while the corresponding N termini of the pent
81 f 195 A, is made from distinctive pentameric capsomeres with large holes along the 3-fold axis, while
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