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1 S1977P only impaired replication as a NS3-5B polyprotein.
2 aged into the virion as a part of the GagPol polyprotein.
3 rus type 1 (HIV-1) Gag precursor (Pr55(Gag)) polyprotein.
4 and human hepatoma cells that express a HCV polyprotein.
5 roteolytic processing of the viral replicase polyprotein.
6 e expression of NS5A within the context of a polyprotein.
7 y sensitive to a reduction in levels of this polyprotein.
8 for its release from the nascent structural polyprotein.
9 ing translation of the alphavirus structural polyprotein.
10 sframe peptide and p6* domain of the Gag-Pol polyprotein.
11 yl-tRNA synthetase (LysRS) and the HIV-1 Gag polyprotein.
12 not interfere with normal processing of the polyprotein.
13 red membrane protein, and processing the HCV polyprotein.
14 the correct proteolytic cleavage of the Gag polyprotein.
15 en Env and the matrix (MA) domain of the Gag polyprotein.
16 the PPR as in the rest of the nonstructural polyprotein.
17 tural proteins (nsP1-4) produced as a single polyprotein.
18 nships among many sites along the entire HCV polyprotein.
19 ural proteins that are translated as the gag polyprotein.
20 of the MA domain within the full-length Gag polyprotein.
21 the integration of the target protein into a polyprotein.
22 nced by cotranslation of viral proteins as a polyprotein.
23 teins in the same reading frame as the viral polyprotein.
24 RNA and trans-acting elements within the Gag polyprotein.
25 onded variant of the I91 human cardiac titin polyprotein.
26 ta, defined as the complete unfolding of the polyprotein.
27 tural proteins via the cleavage of the viral polyprotein.
28 ose requiring expression of a minimum NS3-5B polyprotein.
29 virus type 1 (HIV-1) are governed by the Gag polyprotein.
30 s, may only be a minor contributor to GagPol polyprotein.
31 sidue of nsP2 protease) in the nonstructural polyprotein.
32 o putative recombination hotspots within the polyprotein.
33 c RNA genome and a small number of viral Gag polyproteins.
34 proteolytic cleavage of the PRRSV replicase polyproteins.
35 ration by processing the gag and gag-pro-pol polyproteins.
36 dae, possess macro domains embedded in their polyproteins.
37 s, releasing inhibitory domains and cleaving polyproteins.
38 hemorrhagic fever virus (SHFV) nonstructural polyprotein 1a is predicted to encode three papain-like
39 te an antibody response to the nonstructural polyprotein 3ABC but generated a neutralizing antibody r
42 ition sites into the primary sequence of the polyprotein allows for the selective cleavage of MBP3 in
44 inase (L(pro)) cleaves itself from the viral polyprotein and cleaves the translation initiation facto
45 broad epistatic connectivity across the HCV polyprotein and essentially shape intrahost HCV evolutio
46 fied the IFN antagonists within the HEV ORF1 polyprotein and expanded our understanding of the functi
47 age of membrane-anchored portions of the HCV polyprotein and for cleavage of MAVS for control of RIG-
50 iated that the matrix (MA) domain of the Gag polyprotein and the cytoplasmic tail of Env are central
51 en previously reported to bind the HIV-1 Gag polyprotein and to make a positive contribution to the e
52 rame (ORF) of 3,494 codons translatable as a polyprotein and two embedded shorter ORFs in the -1 fram
53 y cleaving a site within the viral replicase polyproteins and also removes ubiquitin from cellular pr
54 ns of a small number of assembling viral Gag polyproteins and RNA elements within the 5'-untranslated
55 eases, 2A(pro) and 3C(pro), to process their polyproteins and shut off host cell activities detriment
56 d from the proteolytic processing of a large polyprotein, and an additional P3N-PIPO product, with th
57 red NS5A to be expressed as part of a larger polyprotein, and this correlated with detection of NS5A
58 -like protease (PLpro) domain in coronavirus polyproteins, and it may play a critical role in proteas
60 uring the late phase of HIV-1 infection, Gag polyproteins are transported to the plasma membrane (PM)
61 1 gp140 protein or a Gag(ZM96)-Pol-Nef(CN54) polyprotein as Gag-derived virus-like particles (termed
62 eric cell-released protein and a Gag-Pol-Nef polyprotein as Gag-induced virus-like particles (VLPs) (
66 of human immunodeficiency virus (HIV)-1 Gag polyprotein at distinct membrane components to enable th
67 t that is responsible for cleaving the viral polyprotein at junctions 3-4A, 4A4B, 4B5A, and 5A5B and
68 ted cell, the viral protease cleaves the Gag polyprotein at specific sites, triggering maturation.
69 e (PL(pro)) that cleaves the viral replicase polyproteins at three sites releasing non-structural pro
70 ndidates were investigated, and concatenated polyproteins based on recombinantly expressed maltodextr
71 Gaussia luciferase (GLuc) inserted into the polyprotein between P1 and P2 (N(2)H-P1-GLuc-P2-P3-COOH)
72 the covalent tethering of protein L and I27 polyproteins between an atomic force microscopy (AFM) ca
74 NA oligonucleotide that binds tightly to the polyprotein but is too short to promote Gag dimerization
75 -2 RNA stability or translation of the viral polyprotein, but is required for viral RNA synthesis.
76 Cleavage of the group-specific antigen (Gag) polyprotein by HIV-1 protease represents the critical fi
78 -1 maturation involves dissection of the Gag polyprotein by the viral protease and assembly of a coni
79 al replication, involves cleavage of the Gag polyprotein by the viral protease into its matrix (MA),
81 ncy virus type 1 (HIV-1) Gag and Gag-Pro-Pol polyproteins by the HIV-1 protease (PR) is essential for
82 g the proteolysis of the Gag and Gag-Pro-Pol polyproteins by the HIV-1 protease (PR) remain obscure.
83 nger RNA for the overlapping Gag and Gag-Pol polyproteins, by using a programmed -1 ribosomal framesh
84 -terminal domain of an HIV-1 capsid assembly polyprotein (C-CA) showed enhancement in binding, cell p
85 mechanical detection of binding to unfolded polyprotein can serve, to our knowledge, as a novel labe
87 one another, the mechanical hierarchy in the polyprotein chain, and the functional form of the probab
89 aturation requires multiple cleavage of long polyprotein chains into functional proteins that include
90 in particle morphology, fusion activity, and polyprotein cleavage between Sindbis and Ross River viru
91 ally, we demonstrate that replacement of MNV polyprotein cleavage sites with the GI or GII equivalent
92 tion kinetics, confirming that PLP2-mediated polyprotein cleavage was intact, but the loss of DUB act
93 y disrupt Ub binding without affecting viral polyprotein cleavage, as determined using an in trans ns
95 es rise to viable rhinovirus chimeras in the polyprotein coding region and that recombination hotspot
96 is-acting replication element (CRE) from the polyprotein coding region to the 3' non-coding region we
100 x assembly, as it enables improved composite polyprotein complex formation compared to traditional tr
101 is 1 of 2 genes encoding for ubiquitin as a polyprotein consisting of multiple copies of ubiquitin m
109 th HCV, expressing the core protein alone or polyprotein displayed an increased level of glucose-6-ph
110 s (VSV) expressing the entire CHIKV envelope polyprotein (E3-E2-6K-E1) in place of the VSV glycoprote
113 pathogenesis that may be applicable to other polyprotein-encoding viruses such as HIV, hepatitis C vi
114 ith concurrent HAX-1 suppression in core- or polyprotein-expressing cells compared to control HepG2 c
115 hich allow to investigate the effects of HCV polyprotein expression independent from viral RNA replic
116 yprotein or individual viral proteins, viral polyprotein expression resulted in enhanced cytoplasmic
117 olymorphisms in the clade B1 enterovirus D68 polyprotein, five were present in neuropathogenic poliov
118 picornavirus and encodes a 2,469-amino-acid polyprotein flanked by 5' and 3' untranslated regions.
119 an 18-kDa protein, L*, out of frame with the polyprotein from an initiation codon 13 nucleotides down
121 s essential in the production of the Gag-Pol polyprotein from the overlapping gag and pol coding sequ
123 is initiated by the trafficking of viral Gag polyproteins from the cytoplasm to the plasma membrane,
125 quire the proteolytic cleavage of structural polyprotein Gag and the clustering of envelope glycoprot
129 ain motifs in the viral structural precursor polyprotein Gag, which serve as links to the ESCRT (endo
131 h as mRNA for the synthesis of the key viral polyproteins Gag and Gag-Pol and as genomic RNA for enca
132 ns inhibited proteolytic processing of HIV-1 polyproteins Gag and Gag-Pol, resulting in immature viri
133 PTAP motif in the viral structural precursor polyprotein, Gag, allows the recruitment of Tsg101 and o
135 d by oligomerization of the major structural polyprotein, Gag, into a hexameric protein lattice at th
137 ferase (RLuc) fused to the N terminus of the polyprotein H(2)N-RLuc-P1-P2-P3-COOH (P1, structural dom
139 e (PLP), which processes the viral replicase polyprotein, has deubiquitinating (DUB) activity, and an
140 intraspecies recombination sites within the polyprotein highlighted recombinant hotspots in nonstruc
141 e importance of flanking residues within the polyprotein in defining the cleavage specificity of the
143 baculovirus-based system to express the IBDV polyprotein in insect cells and found inefficient format
147 ticles requires proper cleavage of the viral polyprotein, including processing of 8 of the 13 substra
148 ion involves sequential cleavages of the Gag polyprotein, initially arrayed in a spherical shell, lea
150 ion of the FMDV 3C protease to cleave the P1 polyprotein into mature capsid proteins, but the FMDV 3C
152 equence for translocation of the E3-E2-6K-E1 polyprotein into the endoplasmic reticulum (ER), and cle
153 studies of HIV-1 Gag, the primary structural polyprotein involved in retroviral assembly, have been c
155 Proteolytic processing of the flavivirus polyprotein is an essential step in the replication cycl
156 fference between the PPR and the rest of the polyprotein is due to the higher tolerance of the PPR fo
157 During HIV-1 assembly and release, the Gag polyprotein is organized into a signature hexagonal latt
161 nce: Mounting evidence suggests that the Gag polyprotein is responsible for annealing primer tRNAs to
162 he major RNA binding region of the HIV-1 Gag polyprotein is the nucleocapsid (NC) domain, which is re
163 t with that of the rest of the nonstructural polyprotein, is molded by pressures that lead toward inc
165 ion of HIV-1 requires disassembly of the Gag polyprotein lattice, which lines the viral membrane in t
166 s sequential proteolytic cleavage of the Gag polyprotein leading to the formation of a conical capsid
168 mount the noisy proximal region, a homomeric polyprotein marker, a carrier to mechanically protect th
170 and recall antigens using a Leishmania major polyprotein (MML) vaccine given with poly-ICLC adjuvant.
175 ecules could be expressed from the replicase polyprotein of murine hepatitis virus as fusions with no
176 d from native locations within the replicase polyprotein of murine hepatitis virus as fusions with no
178 served region near the junction of the viral polyprotein (open reading frame 1 [ORF1]) and capsid (OR
179 o effect on its ability to process the viral polyprotein or act as an interferon antagonist, which in
180 l lines with inducible expression of the HCV polyprotein or individual viral proteins, viral polyprot
181 nd p6 domains, the multifunctional HIV-1 Gag polyprotein orchestrates the highly coordinated process
185 ced by the partially processed nonstructural polyprotein P123 and nsP4, but synthesis of dsRNA is an
186 The MA (matrix) domain of the retroviral Gag polyprotein plays several critical roles during virus as
187 pproximately 20:1 mixture of Gag and Gag-Pol polyproteins plus a single genomic RNA (gRNA) dimer.
189 tranded RNA viruses) express their replicase polyproteins pp1a and pp1ab from two long ORFs (1a and 1
191 es of the HIV-1 replication cycle, the viral polyprotein Pr55(Gag) is recruited to the plasma membran
193 The Env glycoproteins are synthesized as a polyprotein precursor (gp160) that is cleaved by cellula
195 sly expressing both a mutated and functional polyprotein precursor needed for RNA genome replication
197 For HIV-1, the Gag protein has the role of a polyprotein precursor that contains all of the structura
198 a trans-complementation assay, an HCV NS3-5A polyprotein precursor was required to facilitate efficie
199 uent proteins, GFP and RFP (mCherry), from a polyprotein precursor, in bacterial, mammalian, and plan
200 se domain within the nonstructural replicase polyprotein precursor, is responsible for the self-cleav
203 ntation systems to examine the role that HCV polyprotein precursors play in RNA replication and virio
204 Western blot analysis showed expression of polyprotein prM/E in different forms as monomers (~65 kD
205 t, we report expression of dengue-3 serotype polyprotein (prM/E) consisting of part of capsid, comple
206 like compound, GW5074, interfered with viral polyprotein processing affecting both 3C- and 2A-depende
209 lles, where cholesterol then regulates viral polyprotein processing and facilitates genome synthesis.
210 additional insight into understanding viral polyprotein processing and has important implications fo
211 roteases (2A(pro)) that contribute essential polyprotein processing and host cell shutoff functions d
213 ired for viral replication and nsp5-mediated polyprotein processing at the nonpermissive temperature.
215 he protease active site blocks NS3-dependent polyprotein processing but might impact other steps of t
218 hat BeAn virus RNA replication, translation, polyprotein processing into final protein products, and
221 B activity of PL(pro) from its role in viral polyprotein processing now provides an approach to furth
222 Previously, we demonstrated that the NoV polyprotein processing order is directly correlated with
224 oundary, and their effect on replication and polyprotein processing was examined in the context of a
225 errogate the precise mechanisms employed for polyprotein processing, a critical step that can ultimat
226 viral infection, such as aphid transmission, polyprotein processing, and suppression of host antivira
227 ized the role of cdE2 residues in structural polyprotein processing, glycoprotein transport, and caps
228 and analyzed the effects of these changes on polyprotein processing, replication, and infectious viru
229 f the third IN substitution (V165I) restored polyprotein processing, virus particle maturation, and s
230 hibit YFV replication had minimal effects on polyprotein processing, while overexpressed wild-type DN
234 sults reveal an unanticipated role of IN for polyprotein proteolytic processing during virion morphog
238 ed in this study that exchanges of the P1-2A polyprotein region between members of the same rhinoviru
240 ucts and other methods, we have assessed the polyprotein requirements for rescue of different lethal
244 81 (WSMV-S81) and Type (WSMV-T) share 98.7% polyprotein sequence identity but differentially infect
246 if containing families; seven endogenous Gag polyproteins sharing the same binding sequence; and seve
248 n [Ser(139)-->Asn(139) (S139N)] in the viral polyprotein substantially increased ZIKV infectivity in
249 l the exposure of reactive sites in a single polyprotein substrate composed of repeated domains.
250 4 hours after addition of an NS5A inhibitor, polyprotein synthesis was reduced <50%, even at micromol
251 NA synthesis and steady-state RNA abundance, polyprotein synthesis, virion assembly, and infectious v
254 tively, our results demonstrate the DI-based polyprotein technology as a highly valuable addition to
255 ly 5,600 nucleotides in length and encodes a polyprotein that also contains a region homologous to th
257 he host cell, viral RNA is translated into a polyprotein that is cleaved by host and viral proteinase
258 V-1 proteins are initially made as part of a polyprotein that is cleaved by the viral protease into t
259 rticularly if the viral chimeras contain the polyprotein that provides all of the proteins necessary
262 ession of the polymerase in the context of a polyprotein that undergoes proteolytic processing for NS
263 ssemble as immature particles containing Gag polyproteins that are processed by the viral protease in
264 strand RNA virus genomes are translated into polyproteins that are processed by viral proteases to yi
265 ral decades, extensive research into the Gag polyprotein, the main structural protein of HIV-1 and al
266 inging these ORFs in frame with the upstream polyprotein, thus leading to P1N-PISPO and P3N-PIPO prod
267 us (HCV) requires proteins from the NS3-NS5B polyprotein to create a replicase unit for replication o
268 ta and repeatedly probed the same individual polyprotein to deduce its dynamic force spectrum in just
269 ) that have the ability to process the viral polyprotein to facilitate RNA replication and antagonize
271 Although best known for targeting the Gag polyprotein to the inner leaflet of the plasma membrane
276 egy, a mutant was created in which replicase polyprotein translation initiated with nsp3, thereby est
277 e host's plasma membrane, the retroviral Gag polyprotein triggers formation of the viral protein/memb
278 confirmed by the observation of full length polyprotein unfolding, combined with high detachment for
279 ll molecule binding to mechanically unfolded polyprotein using sodium dodecyl sulfate (SDS) as an exa
280 llowing challenge by infected sand fly bite, polyprotein-vaccinated animals had comparable parasite l
284 y, the release of p48 from the ORF B-encoded polyprotein was not prevented by mutation of the p48 cat
285 WNV NS2B/3 cleavage of the DENV structural polyprotein was possible when a threonine (Thr101 in str
286 both FRET-based peptides and full-length NoV polyprotein, we have successfully demonstrated that the
287 e domains in the open reading frame 1 (ORF1) polyprotein, we identified two IFN antagonists and perfo
288 leavage sites within the Gag and Gag-Pro-Pol polyproteins were placed at the MA/CA site, the rates of
289 N inhibiting replication as a minimum NS3-5A polyprotein whereas V1665G and S1977P only impaired repl
290 pen reading frame 1 (ORF1) encodes a 200-kDa polyprotein which is cleaved by the viral 20-kDa 3C-like
292 reticulum (ER) membranes to produce a single polyprotein, which is cleaved by host and viral protease
293 A/DNA binding protein encoded within the Gag polyprotein, which is critical for the selection and cha
294 NV protease recognizes multiple sites in the polyprotein with differential affinities during virus re
296 (ORF1) protein of HEV encodes nonstructural polyprotein with putative domains for methyltransferase,
298 mitations by merging two developments: (i) a polyprotein with versatile, genetically encoded short pe
299 al interactions of all 18 HIV-1 proteins and polyproteins with host proteins in two different human c
300 ulated ~0-fold compared to the larger 2BC3AB polyprotein, with most of this stimulation occurring upo
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