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1 he removal of different chain terminators by HIV-1 reverse transcriptase.
2 e (NgoM IV) cleavage site at its 3'-end, and HIV-1 reverse transcriptase.
3 AZT P3Ms exhibited very potent inhibition of HIV-1 reverse transcriptase.
4 ch was previously reported in a complex with HIV-1 reverse transcriptase.
5  domain of human tRNA(Lys,3), the primer for HIV-1 reverse transcriptase.
6 f AZTMP from the end of the primer strand by HIV-1 reverse transcriptase.
7 n compared with the complex of nevirapine in HIV-1 reverse transcriptase.
8 osophila pol gamma complex resemble those of HIV-1 reverse transcriptase.
9 in CEM-SS cell culture and for inhibition of HIV-1 reverse transcriptase.
10  accessory subunit and the RNase H domain of HIV-1 reverse transcriptase.
11 e observed for other polymerases such as the HIV-1 reverse transcriptase.
12 f DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase.
13  was found to target the RNase H activity of HIV-1 reverse transcriptase.
14 etroviral reverse transcription catalyzed by HIV-1 reverse transcriptase.
15 sphates into a primer-template complex using HIV-1 reverse transcriptase.
16 eries of 12 TIBO nonnucleoside inhibitors of HIV-1 reverse transcriptase.
17 ich line the nonnucleoside binding pocket of HIV-1 reverse transcriptase.
18  for two complexes of catechol diethers with HIV-1 reverse transcriptase.
19 erleukin 8, and the ribonuclease H domain of HIV-1 reverse transcriptase.
20 nal changes are critical for the function of HIV-1 reverse transcriptase.
21 tors of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase.
22 itor of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase.
23 tion of HIV-1 induced syncytia formation and HIV-1 reverse transcriptase activity.
24  transcriptase variants for their effects on HIV-1 reverse transcriptase activity.
25 ed the effects of RNA secondary structure on HIV-1 reverse transcriptase activity.
26 F61A in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase affect strand displacement
27 ld-type human immunodeficiency virus type 1 (HIV-1) reverse transcriptase, an exonuclease-deficient T
28 ymidine 5'-triphosphate (AZTTP) by wild-type HIV-1 reverse transcriptase and a clinically important A
29 e of these hybrids was examined with p66/p51 HIV-1 reverse transcriptase and a mutant carrying an alt
30 Human tRNA(Lys,3) is the specific primer for HIV-1 reverse transcriptase and also requires nucleoside
31 d 20th nucleotides from the recessed end for HIV-1 reverse transcriptase and between the 17th and 20t
32                     Phylogenetic analyses of HIV-1 reverse transcriptase and env DNA sequences isolat
33 tRNA(Lys,3), is the specific tRNA primer for HIV-1 reverse transcriptase and has a similar modificati
34                                              HIV-1 reverse transcriptase and protease gene sequences,
35  inhibited CDK2-dependent phosphorylation of HIV-1 reverse transcriptase and significantly reduced th
36 in more insight into the interaction between HIV-1 reverse transcriptase and the alkenyldiarylmethane
37 /2 = 61 h) along with the ability to inhibit HIV-1 reverse transcriptase and the cytopathic effect of
38 ns between the human immunodeficiency virus (HIV-1) reverse transcriptase and substrate DNA were prob
39 hing by human immunodeficiency virus type 1 (HIV-1) reverse transcriptase and the role of template di
40 e context of our results, related studies on HIV-1 reverse transcriptase, and previous structural stu
41 teraction between the p66 thumb subdomain of HIV-1 reverse transcriptase, and the DNA template in the
42      Specific applications for inhibition of HIV-1 reverse transcriptase are reported.
43 s) and evaluated their inhibitory effects on HIV-1 reverse transcriptase as well as their stability i
44 he dynamic behavior of the RNase H domain of HIV-1 reverse transcriptase at a more physiological pH (
45 on studies of the isolated RNase H domain of HIV-1 reverse transcriptase at low pH have revealed that
46 tent inhibitory activity against recombinant HIV-1 reverse transcriptase at submicromolar concentrati
47 V structure superimposed upon a structure of HIV-1 reverse transcriptase bound to an RNA/DNA hybrid s
48 t function in template and primer binding in HIV-1 reverse transcriptase, but the integrity of the re
49 ic basis for understanding the inhibition of HIV-1 reverse transcriptase by 3TC.
50 r machinery, and identify the suppression of HIV-1 reverse transcriptase by a directly interacting ho
51                                              HIV-1 reverse transcriptase can remove chain terminators
52 Our results show that actinomycin D inhibits HIV-1 reverse transcriptase catalyzed DNA strand transfe
53 ycin D was found to be a potent inhibitor of HIV-1 reverse transcriptase catalyzed DNA strand transfe
54 level, we investigated the inhibition of the HIV-1 reverse transcriptase-catalyzed viral DNA synthesi
55 main of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase cleaves the tRNA 1 nucleoti
56 ucleoside inhibitor and was absent in mutant HIV-1 reverse transcriptase deficient in polymerase acti
57                                              HIV-1 reverse transcriptase discriminates poorly between
58 everse transcription products indicated that HIV-1 reverse transcriptase efficiently used the HIV-2 P
59         All four ADAMs were found to inhibit HIV-1 reverse transcriptase enzyme activity, to inhibit
60  antiviral efficacy and activity against the HIV-1 reverse transcriptase enzyme.
61                                    Moreover, HIV-1 reverse transcriptase extends this binary complex
62 s bacteriophage DNA polymerase T7- (T7-) and HIV-1 reverse transcriptase for comparison with previous
63 nst the ribonuclease H (RNase H) activity of HIV-1 reverse transcriptase has been developed.
64 he RNA dependent DNA replication fidelity of HIV-1 reverse transcriptase has been investigated using
65 pre-steady-state kinetic investigations with HIV-1 reverse transcriptase (HIV-1 RT) have reported sub
66                                              HIV-1 reverse transcriptase (HIV-1 RT) is a multifunctio
67                           The active site of HIV-1 reverse transcriptase (HIV-1 RT) was investigated
68 otide (FANA) aptamer (referred to as FA1) to HIV-1 reverse transcriptase (HIV-1 RT) was selected.
69 has been identified as a potent inhibitor of HIV-1 reverse transcriptase (HIV-1 RT).
70                       The mechanism by which HIV-1 reverse transcriptase (HIV-RT) discriminates betwe
71 n be understood in light of the structure of HIV-1 reverse transcriptase in a complex with an RNA/DNA
72 hlorines in the aromatic rings might bind to HIV-1 reverse transcriptase in a slightly different mode
73  the 3.0 A resolution structure of wild-type HIV-1 reverse transcriptase in complex with an RNA:DNA o
74 effective as ddATP in reactions catalyzed by HIV-1 reverse transcriptase in that both analogs have si
75                                       Mutant HIV-1 reverse transcriptase in the viral isolates from t
76  was well tolerated in the catalytic site of HIV-1 reverse transcriptase in the wild-type virus.
77 nhibits human immunodeficiency virus type 1 (HIV-1) reverse transcriptase in a cell-free system.
78 ture of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase in a complex with an RNA-DN
79 ing by human immunodeficiency virus, type 1 (HIV-1) reverse transcriptase in front of the primer term
80 utations in the connection subdomain (cn) of HIV-1 reverse transcriptase increase AZT resistance by a
81        Here we analyzed whether abacavir, an HIV-1 reverse transcriptase inhibitor often inducing sev
82 rmittently dosed vaginal gels containing the HIV-1 reverse transcriptase inhibitor tenofovir protecte
83 ring containing dapivirine, a non-nucleoside HIV-1 reverse-transcriptase inhibitor, involving women b
84 trate these new features with a simple case (HIV-1 reverse transcriptase/inhibitor interaction) and w
85                                         When HIV-1 reverse transcriptase inhibitors, protease inhibit
86 significant increase in activity against the HIV-1 reverse transcriptase/integrase and P2/nucleocapsi
87 at the structural basis of AZT resistance in HIV-1 reverse transcriptase involves the conformation of
88  accuracy of plus-strand primer selection by HIV-1 reverse transcriptase is not immediately clear.
89 DNA by human immunodeficiency virus, type 1 (HIV-1) reverse transcriptase is accompanied by RNase H d
90 itor of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase, is a promising addition to
91 e applied the assay to phi29 DNA polymerase, HIV-1 reverse transcriptase, lambda exonuclease and Esch
92  by CPHM was found to be highly specific for HIV-1 reverse transcriptase; little or no inhibition of
93 uggests that large A3G oligomers could block HIV-1 reverse transcriptase-mediated DNA synthesis, ther
94 such as human immunodeficiency virus type 1 (HIV-1) reverse transcriptase monomers and homodimers.
95 -1 replication and can select for a specific HIV-1 reverse transcriptase mutation (V75I) with concomi
96                 Non-nucleoside inhibitors of HIV-1 reverse transcriptase (NNRTIs) are part of the com
97 or more than 200 nonnucleoside inhibitors of HIV-1 reverse transcriptase (NNRTIs) representing eight
98 e highly potent non-nucleoside inhibitors of HIV-1 reverse transcriptase (NNRTIs).
99 nhibitors of human immunodeficiency virus-1 (HIV-1) reverse transcriptase (NNRTIs).
100 ocused on three widely studied drug targets, HIV-1 reverse transcriptase, p38 MAP kinase, and cyclin-
101 al entry and did not affect formation of the HIV-1 reverse transcriptase products R/U5 and long termi
102 mpounds showed detectable activities against HIV-1 reverse transcriptase, protease, virus attachment,
103  create 63-mers that served as templates for HIV-1 reverse transcriptase replication.
104                  V75I and other mutations in HIV-1 reverse transcriptase reported from in vitro acycl
105 ochemical, and crystallographic studies with HIV-1 reverse transcriptase revealed that alpha-CNPs mim
106                                          For HIV-1 reverse transcriptase, reverse transcription (RNA-
107 tion by human immunodeficiency virus type 1 (HIV-1) reverse transcriptase RNase H is critical for gen
108 d precise cleavage at the PPT/U3 junction by HIV-1 reverse transcriptase/RNase H.
109 ar carbocyclic deoxyribose ring that acts on HIV-1 reverse transcriptase (RT(WT)) as a molecular targ
110 ques infected with an SIV variant containing HIV-1 reverse transcriptase (RT) (RT-simian-human immuno
111  for inhibitory properties against wild-type HIV-1 reverse transcriptase (RT) and an RT carrying the
112 tase inhibitors (NNRTIs) specifically target HIV-1 reverse transcriptase (RT) and do not effectively
113                                Inhibition of HIV-1 reverse transcriptase (RT) and HIV protease are ef
114  for viral replication: HIV-1 protease (PR), HIV-1 reverse transcriptase (RT) and HIV-1 integrase (IN
115 wealth of structural and biochemical data on HIV-1 reverse transcriptase (RT) and mutants.
116 thione), is an extremely potent inhibitor of HIV-1 reverse transcriptase (RT) and of HIV-1 infection
117 entary dNTP by the binary complex containing HIV-1 reverse transcriptase (RT) and primer-template ind
118                          The contribution of HIV-1 reverse transcriptase (RT) and protease (PR) allel
119 e of all four nucleotides revealed that both HIV-1 reverse transcriptase (RT) and T7 DNA polymerase s
120 triphosphate form of ETV with wild type (WT) HIV-1 reverse transcriptase (RT) and the nucleoside reve
121                   Drug-resistant variants of HIV-1 reverse transcriptase (RT) are also known to be re
122                     Nucleic acid aptamers to HIV-1 reverse transcriptase (RT) are potent inhibitors o
123 flipping at the single molecule level, using HIV-1 reverse transcriptase (RT) as a model system.
124 o facilitate HDX analysis of multimers using HIV-1 reverse transcriptase (RT) as a model.
125 rts 13-15 in HIV-1 infected cells and in the HIV-1 reverse transcriptase (RT) assays is here describe
126 n of amino acids in the fingers subdomain of HIV-1 reverse transcriptase (RT) at positions 69 and 70.
127  of 99 available X-ray crystal structures of HIV-1 reverse transcriptase (RT) at the flexible non-nuc
128                       Crystal structures for HIV-1 reverse transcriptase (RT) bound to double-strande
129 oxy-3'-thiacytidine (3TC), and AZT-resistant HIV-1 reverse transcriptase (RT) can increase the virus
130                                              HIV-1 reverse transcriptase (RT) catalyzes the conversio
131            While many point mutations in the HIV-1 reverse transcriptase (RT) confer resistance to an
132 348I mutation at the connection subdomain of HIV-1 reverse transcriptase (RT) confers clinically sign
133  protein footprinting methodology to dissect HIV-1 reverse transcriptase (RT) contacts to the viral R
134                                              HIV-1 reverse transcriptase (RT) contains a C-terminal r
135                                              HIV-1 reverse transcriptase (RT) contributes to the deve
136                                              HIV-1 reverse transcriptase (RT) degrades the plus stran
137  solution structure of the RNase H domain of HIV-1 reverse transcriptase (RT) determined by NMR metho
138                                     Although HIV-1 reverse transcriptase (RT) DNA polymerase and ribo
139                                      Because HIV-1 reverse transcriptase (RT) does not possess 3'- to
140 ling of T7 DNA polymerase exo(-) (T7(-)) and HIV-1 reverse transcriptase (RT) during replication of p
141     Biochemical simulations demonstrate that HIV-1 reverse transcriptase (RT) efficiently incorporate
142   During reverse transcription of viral RNA, HIV-1 reverse transcriptase (RT) encounters RNA stem-loo
143 ion from methionine-184 to valine (M184V) of HIV-1 reverse transcriptase (RT) evokes the 1000-fold 3T
144                                              HIV-1 reverse transcriptase (RT) frequently incorporates
145 he cleavage and functional expression of the HIV-1 reverse transcriptase (RT) from the modified RV ge
146 sizing a double-stranded DNA from viral RNA, HIV-1 reverse transcriptase (RT) generates an RNA/DNA in
147  Mutations at either Tyr181 or Tyr188 within HIV-1 reverse transcriptase (RT) give high level resista
148                                 Mutations in HIV-1 reverse transcriptase (RT) give rise to 3'-azido-3
149 e 1 (HIV-1) can induce the development of an HIV-1 reverse transcriptase (RT) harboring a dipeptide i
150 dideoxy-3'-thiacytidine drug-resistant M184I HIV-1 reverse transcriptase (RT) has been shown to synth
151 orophenyl)benzimidazole analogues (BPBIs) to HIV-1 reverse transcriptase (RT) have been determined us
152 nd 20 nevirapine nonnucleoside inhibitors of HIV-1 reverse transcriptase (RT) have been explored in a
153 ole of patient-derived C-terminal domains of HIV-1 reverse transcriptase (RT) in NRTI resistance.
154                       RNA aptamers that bind HIV-1 reverse transcriptase (RT) inhibit HIV-1 replicati
155 ile groups at the wings of the nonnucleoside HIV-1 reverse transcriptase (RT) inhibitor TMC278 are bo
156 rt to develop novel and potent nonnucleoside HIV-1 reverse transcriptase (RT) inhibitors that are eff
157                               In a search of HIV-1 reverse transcriptase (RT) inhibitors, a new chemo
158                                              HIV-1 reverse transcriptase (RT) is a heterodimeric enzy
159                                              HIV-1 reverse transcriptase (RT) is a highly error prone
160                                              HIV-1 reverse transcriptase (RT) is a major target of an
161                                              HIV-1 reverse transcriptase (RT) is a primary target for
162 ry and characterization of new inhibitors of HIV-1 reverse transcriptase (RT) is an important step to
163                                              HIV-1 reverse transcriptase (RT) is an important target
164 teraction of the NNRTI nevirapine (NVP) with HIV-1 reverse transcriptase (RT) is characterized by a p
165                   The polymerase activity of HIV-1 reverse transcriptase (RT) is entirely dependent o
166              The biologically active form of HIV-1 reverse transcriptase (RT) is the p66/p51 heterodi
167 al and biochemical analysis of 3TC-resistant HIV-1 reverse transcriptase (RT) led to a model in which
168                               We employed an HIV-1 reverse transcriptase (RT) mutant (Q151N), which i
169 ndings show that AZT resistance mutations in HIV-1 reverse transcriptase (RT) not only reduce suscept
170  These silent K65K and K66K mutations in the HIV-1 reverse transcriptase (RT) occur in over 35% of dr
171          The effect of the K103N mutation of HIV-1 reverse transcriptase (RT) on the activity of efav
172                      Formation of the mature HIV-1 reverse transcriptase (RT) p66/p51 heterodimer req
173 ts, we suggest that the polymerase domain of HIV-1 reverse transcriptase (RT) plays a critical role i
174                   We have discovered that an HIV-1 reverse transcriptase (RT) polymorphism (RT(172K))
175                                              HIV-1 reverse transcriptase (RT) possesses both DNA poly
176 le, Val106Ala and Val108Ile are mutations in HIV-1 reverse transcriptase (RT) that are observed in th
177 tors (NNRTIs) that are capable of inhibiting HIV-1 reverse transcriptase (RT) through an allosteric m
178                                      We used HIV-1 reverse transcriptase (RT) to monitor the annealin
179                                              HIV-1 reverse transcriptase (RT) undergoes a series of c
180 e reverse transcriptase inhibitor (NNRTI) of HIV-1 reverse transcriptase (RT) used for the treatment
181    However, clinical data suggest that while HIV-1 reverse transcriptase (RT) usually uses an ATP-dep
182                             We characterized HIV-1 reverse transcriptase (RT) variants either with or
183                                              HIV-1 reverse transcriptase (RT) was found to bind with
184 nection subdomain (CN) and RNase H domain of HIV-1 reverse transcriptase (RT) were observed to exhibi
185 have identified fragment-sized inhibitors of HIV-1 reverse transcriptase (RT) with distinct chemical
186 ed clinically as anti-HIV drugs which target HIV-1 reverse transcriptase (RT), (-)-2', 3'-dideoxy-3'-
187                                              HIV-1 reverse transcriptase (RT), a critical enzyme of t
188 y host DNA-dependent RNA polymerase II or by HIV-1 reverse transcriptase (RT), but the relative contr
189 dynamics simulations of a ternary complex of HIV-1 reverse transcriptase (RT), double-stranded DNA, a
190 wo nucleoside analog resistance mutations in HIV-1 reverse transcriptase (RT), E89G and M184V, were p
191 luding non-nucleoside inhibitors (NNRTIs) of HIV-1 reverse transcriptase (RT), has been limited by th
192         tRNA(Lys)(3) interacts directly with HIV-1 reverse transcriptase (RT), is packaged into viral
193 lides are nonnucleoside inhibitors (NNIs) of HIV-1 reverse transcriptase (RT), of potential clinical
194 6A, 181C, 188C, and 190A), with mutations in HIV-1 reverse transcriptase (RT), singly and in combinat
195 id substitutions within the coding region of HIV-1 reverse transcriptase (RT), such as the 3'-azido-3
196 3) in the fingers and palm subdomains of the HIV-1 reverse transcriptase (RT), the enzyme that replic
197 on in the ribonuclease H (RNase H) domain of HIV-1 reverse transcriptase (RT), which increases resist
198 ine undergoes conformational changes to bind HIV-1 reverse transcriptase (RT), which is an essential
199  the decreased binding affinity to wild-type HIV-1 reverse transcriptase (RT), which may be one of th
200 ions have been biochemically shown to impact HIV-1 reverse transcriptase (RT)-mediated strand transfe
201 s on dimerization of p66 and p51 subunits of HIV-1 reverse transcriptase (RT).
202 d using T7 DNA polymerase exo(-) (T7(-)) and HIV-1 reverse transcriptase (RT).
203 se targeting the essential viral polymerase, HIV-1 reverse transcriptase (RT).
204 ve excellent antiretroviral activity against HIV-1 reverse transcriptase (RT).
205 icient mouse cells are higher than the KM of HIV-1 reverse transcriptase (RT).
206  forms and assessed their ability to inhibit HIV-1 reverse transcriptase (RT).
207 ity, as well as the viral target protein, WT HIV-1 reverse transcriptase (RT).
208 e sites of wild-type (WT) and drug-resistant HIV-1 reverse transcriptase (RT).
209 riphosphates (dNTP) for incorporation by the HIV-1 reverse transcriptase (RT).
210 simian immunodeficiency virus containing the HIV-1 reverse transcriptase (RT).
211 ranscriptase inhibitors (NNRTI) 3 and 4 with HIV-1 reverse transcriptase (RT).
212 rm a group of related sequences that inhibit HIV-1 reverse transcriptase (RT).
213 genic simian immunodeficiency virus encoding HIV-1 reverse transcriptase (RT-SHIV) to examine the imp
214 simian immunodeficiency virus (SIV) carrying HIV-1 reverse transcriptase (RT-SHIV), compared to uninf
215 ions of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) (T69S mutations follow
216 tors of human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) active against the dru
217 itor of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) activity and of HIV-1
218 lity of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) and protease sequencin
219 ld-type human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) and two RT mutants, Y1
220 gion of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) are associated with re
221 /A/K in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) are rilpivirine resist
222 loop to human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) between residues 230 a
223 fic for human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) bind at the template-p
224 ture of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) bound to an RNA/DNA hy
225 tion in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) causes resistance to l
226 ity of human immunodeficiency virus, type 1 (HIV-1) reverse transcriptase (RT) cleaves the viral geno
227 AMs) at human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) codons 41, 67, 70, 210
228 ture of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) complexed with a 19-me
229 ations in the human immunodeficiency type 1 (HIV-1) reverse transcriptase (RT) connection domain sign
230 grip of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) contacts the DNA prime
231         Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) contains four structur
232         Human immunodeficiency virus-type 1 (HIV-1) reverse transcriptase (RT) coordinates DNA polyme
233 A synthesis, human immunodeficiency virus 1 (HIV-1) reverse transcriptase (RT) degrades the RNA genom
234         Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) displays a characteris
235     The human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) functions as a heterod
236 idue of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) greatly enhance RT fid
237 lthough human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) has been extensively s
238  of the human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) have yet to be develop
239  of the human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) heterodimer.
240 ains of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) increase 3'-azido-3'-d
241         Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) initiates DNA synthesi
242 vity of human immunodeficiency virus type I (HIV-1) reverse transcriptase (RT) is a critical componen
243         Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) is a dimeric enzyme co
244     The human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) is a heterodimer compr
245         Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) is a major target of a
246         Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) is a putative source o
247  of the human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) is comprised of a clus
248 tion in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) is selected in vitro b
249 ve (ts) human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) mutant was generated b
250 ge library of immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) mutants with amino aci
251 y using human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) mutants with unique cy
252 ed with human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) mutants with unique cy
253 ntified human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) mutants, Q151N and V14
254     The human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) resistance mutation K6
255 ting by human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) result from template s
256 ants of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) that displayed higher
257 ants of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) that influence its tem
258 ance of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) to nucleoside analogs:
259         Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) variants with the K65R
260 n catalyzed by human immunodeficiency virus (HIV-1) reverse transcriptase (RT) was studied using a sy
261 tion in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT), a variety of non-natu
262 itor of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT), acting through the PP
263 tion in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT), I132M, which confers
264         Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT), like all retroviral R
265         Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT), nucleocapsid protein
266 nhibitors of human immunodeficiency virus-1 (HIV-1) reverse transcriptase (RT)-associated RNase H act
267 are allosteric inhibitors of the HIV type 1 (HIV-1) reverse transcriptase (RT).
268 ld-type human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT).
269 tion in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT).
270 ively effective inhibitors of drug-resistant HIV-1 reverse transcriptases (RTs) that are excision pro
271 d therefore effective against drug-resistant HIV-1 reverse transcriptases (RTs) that are proficient a
272 LV) and human immunodeficiency virus type 1 (HIV-1) reverse transcriptases (RTs) during RNA-dependent
273       We reviewed all GenBank submissions of HIV-1 reverse transcriptase sequences with or without pr
274                                              HIV-1 reverse transcriptase shares the key features of h
275 l structure of the complex of 3v (739W94) in HIV-1 reverse transcriptase showed an overlap in the bin
276 al structure of the active sites of MuLV and HIV-1 reverse transcriptases shows the presence of a lys
277 emplate/primers were not altered if bound to HIV-1 reverse transcriptase, signifying that the deposit
278 oth for the isolated domain and for the full HIV-1 reverse transcriptase structure, suggests that the
279 ption with a slightly higher efficiency than HIV-1 reverse transcriptase, suggesting that the activit
280 a nucleotide-dependent reaction catalyzed by HIV-1 reverse transcriptase that can efficiently remove
281       Like other nonnucleoside inhibitors of HIV-1 reverse transcriptase, the dipyridodiazepinone nev
282 to bind human immunodeficiency virus type 1 (HIV-1) reverse transcriptase tightly, are potent inhibit
283 ecifically, we evaluated the contribution of HIV-1 reverse transcriptase to proviral DNA uracilation
284 urified human immunodeficiency virus type 1 (HIV-1) reverse transcriptase to convert single-stranded
285                                              HIV-1 reverse transcriptase uses human tRNA(Lys,3) as a
286 C on RNA 5'-end-directed RNase H cleavage by HIV-1 reverse transcriptase, using an RNA.DNA hybrid in
287                                              HIV-1 reverse transcriptase utilizes a metamorphic polym
288 ants of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (V106A, V179D, and Y181C),
289 ectiveness of the compounds as inhibitors of HIV-1 reverse transcriptase was determined using a fluor
290 he initiation of (-) strand DNA synthesis by HIV-1 reverse transcriptase was examined using a transie
291                                Sequencing of HIV-1 reverse transcriptase was simultaneously performed
292 er complexes, in the absence and presence of HIV-1 reverse transcriptase, were irradiated with high-e
293                      The F61W mutant form of HIV-1 reverse transcriptase, which is partially impaired
294                            ADAM 28 inhibited HIV-1 reverse transcriptase with an IC(50) of 0.3 microM
295                            ADAM II inhibited HIV-1 reverse transcriptase with an IC50 of 0.3 microM b
296 res were determined with wild-type and K103N HIV-1 reverse transcriptase with etravirine (TMC125) and
297  a potent competitive inhibitor of wild-type HIV-1 reverse transcriptase with K(i) close to ddATP.
298 n the two previously published structures of HIV-1 reverse transcriptase with mutations at 181 or 188
299  and two strong noncompetitive inhibitors of HIV-1 reverse transcriptase with one series of inhibitor
300 plex of human immunodeficiency virus-type 1 (HIV-1) reverse transcriptase with a DNA template:primer

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