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1 virus (SARS-CoV) and human coronavirus NL63 (HCoV-NL63).
2 A59 (MHV) and human coronavirus strain NL63 (HCoV-NL63).
3  molecules serve as attachment receptors for HCoV-NL63.
4 ction (PCR) with primers that also amplified HCoV-NL63.
5 gest a potential therapeutic target site for HCoV-NL63.
6 uman coronavirus (HCoV)-229E, HCoV-OC43, and HCoV-NL63.
7 s correlates with stronger immune evasion of HCoV-NL63.
8 s of the Coronaviridae family SARS-CoV-1 and HCoV-NL63.
9 ike virus, an ancestor of the human pathogen HCoV-NL63.
10  A total of 8 illnesses were associated with HCoV-NL63, 1 with HCoV-HKU1.
11                      Human coronavirus NL63 (HCoV-NL63), a common human respiratory pathogen, is asso
12  ACE2 protein was proposed as a receptor for HCoV-NL63 already in 2005, but an in-depth analysis of e
13 led that replication of both seasonal HCoVs (HCoV-NL63 and -229E) is significantly attenuated at 37 d
14                           We then focused on HCoV-NL63 and detected broad T cell responses to the spi
15 atory syndrome-CoV (MERS-CoV)] and seasonal (HCoV-NL63 and HCoV-229E) HCoVs.
16 -CoV) and seasonal human coronavirus (HCoV) (HCoV-NL63 and HCoV-229E) replication.
17 e HCoVs corresponded to the newly recognized HCoV-NL63 and HCoV-HKU1 viruses, and >20 different serot
18 ossibly facilitating the interaction between HCoV-NL63 and its receptor.
19                          Human coronaviruses HCoV-NL63 and SARS-CoV-2 enter host cells via ACE2 and u
20 nts directed against human pathogens such as HCoV-NL63 and SARS-CoV.
21                 Previous studies showed that HCoV-NL63 and the genetically distant severe acute respi
22 ars for HCoV-OC43, 31 months to 12 years for HCoV-NL63, and 16 months to 12 years for HCoV-229E).
23 piratory Syndrome (MERS)-CoV, and hCoV-OC43, hCoV-NL63, and hCoV-229E spike proteins.
24 oV, MERS-CoV, human coronavirus (HCoV)-HKU1, HCoV-NL63, and HCoV-229E with micromolar half maximal in
25 and three seasonal coronaviruses (HCoV-OC43, HCoV-NL63, and HCoV-229E).
26 ralizing activity against genuine hCoV-OC43, hCoV-NL63, and hCoV-229E.
27 es human coronavirus (HCoV)-OC43, HCoV-229E, HCoV-NL63, and HCoV-HKU1.
28 n of 3 common cold coronaviruses (HCoV-229E, HCoV-NL63, and HCoV-OC43) and SARS-CoV-2 in 21 healthy d
29 tides from SARS-CoV-2 and 3 CCCs (HCoV-229E, HCoV-NL63, and HCoV-OC43) before and after study partici
30 viruses (human coronavirus 229E [HCoV-229E], HCoV-NL63, and HCoV-OC43), allowing us to probe this int
31                                   HCoV-229E, HCoV-NL63, and human rhinovirus-16 are common cold-assoc
32                         Patients infected by HCoV-NL63 are typically young children with upper and lo
33 er ACE2 interactions are sufficient to allow HCoV-NL63 binding to cells.
34 pro)s of SARS-CoV-2, SARS-CoV, MERS-CoV, and HCoV-NL63 bound to the inhibitor PF-07304814 revealed a
35 matched control subjects tested positive for HCoV-NL63 by reverse transcription-polymerase chain reac
36 onaviruses human coronavirus (HCoV)-OC43 and HCoV-NL63 by the intranasal route, and viral shedding an
37  not universal for all group 1 CoVs, because HCoV-NL63 did not cross-react with SARS-CoV.
38 for inactivated coronaviruses SARS-CoV-2 and HCoV-NL63 extracted from filters was between 10 to 100 c
39  SARS-CoV from the betacoronavirus genus and HCoV-NL63 from the alphacoronavirus genus, were determin
40 g T cells specific for the spike proteins of HCoV-NL63, HCoV-229E, and HCoV-OC43.
41 c human coronaviruses (HCoV-229E, HcoV-HKU1, HcoV-NL63, HcoV-OC43) infections, and community and hous
42  moderate respiratory infections (HCoV-229E, HCoV-NL63, HCoV-OC43, HCoV-HKU1) as well as severe illne
43 cytial virus, human coronavirus (HCoV)-229E, HCoV-NL63, HCoV-OC43, Middle East respiratory syndrome-r
44 d nsp4) and detected replicase proteins from HCoV-NL63-infected LLC-MK2 cells by immunofluorescence,
45  results show that the initial events during HCoV-NL63 infection are more complex than anticipated an
46 ly no effective antiviral therapy to contain HCoV-NL63 infection.
47 y of camostat mesylate, a known inhibitor of HCoV-NL63 infection.
48                      Human coronavirus NL63 (HCoV-NL63) is an alphacoronavirus that was first identif
49 as ACE2, the receptor used by SARS-CoV-2 and HCoV-NL63, is down-regulated.
50     Here we present the crystal structure of HCoV-NL63 M(pro) in complex with a Michael acceptor inhi
51 heir related zoonotic CoVs, our structure of HCoV-NL63 M(pro) provides critical insight into rational
52 nts with acute KD was positive by RT-PCR for HCoV-NL63/NH in a nasopharyngeal swab.
53 S-CoV spike (S) protein but not infection by HCoV-NL63 or a retrovirus pseudotyped with the HCoV-NL63
54 D, the PL(pro)s from SARS-CoV, MERS-CoV, and HCoV-NL63 physically interact with and stabilize RCHY1,
55 e replicase products and characterization of HCoV-NL63 PLP DUB activity will facilitate comparative s
56 acute respiratory syndrome (SARS) CoV PLpro, HCoV-NL63 PLP2 has DUB activity.
57 SARS-CoV-2 antigen results for HCoV 229E and HCoV NL63 positive samples.
58 plication but reduces that of SARS-CoV-2 and HCoV-NL63, reflecting the impact of IL-13 on HCoV recept
59 me 2 (ACE2) on cells previously resistant to HCoV-NL63 renders them susceptible, showing that ACE2 pr
60 s representing the amino-terminal end of the HCoV-NL63 replicase gene and established protease cis-cl
61                            Here, we identify HCoV-NL63 replicase gene products and characterize two v
62                                We found that HCoV-NL63 replicase products can be detected at 24 h pos
63 arly human strains replicated inefficiently, HCoV-NL63 replicated for multiple passages in the immort
64  and by filovirus GP proteins but not by the HCoV-NL63 S protein or the vesicular stomatitis virus G
65 lly less effect on infection mediated by the HCoV-NL63 S protein than on that mediated by the SARS-Co
66 oV-NL63 or a retrovirus pseudotyped with the HCoV-NL63 S protein.
67 dly potent in vitro against alphacoronavirus HCoV-NL63, SARS-CoV, SARS-CoV-related bat-CoV RsSHC014,
68 old increase in the CD4+ T cell responses to HCoV-NL63 spike peptides after vaccination.
69 dies suggested that T cells specific for the HCoV-NL63 spike protein in this individual could also re
70     The higher oligomannose glycan shield on HCoV-NL63 spikes than on SARS-CoV-2 spikes correlates wi
71 ins unchanged across 30 clinical isolates of HCoV-NL63 strains.
72 uctures of the main protease of SARS-CoV and HCoV-NL63 that bound to shikonin.
73                      In contrast, binding of HCoV-NL63 to heparan sulfates was required for viral att
74  the coronaviruses SARS-CoV, SARS-CoV-2, and HCoV-NL63 utilize human ACE2 as the receptor to enter ce
75  The coronaviruses SARS-CoV, SARS-CoV-2, and HCoV-NL63 utilize the angiotensin-converting enzyme 2 (A
76          Here we show that SARS-CoV, but not HCoV-NL63, utilizes the enzymatic activity of the cystei
77 mations on vitrified human coronavirus NL63 (HCoV-NL63) virions without chemical fixation by cryogeni
78            These data suggest that, although HCoV-NL63 was circulating in children in our community d
79                            Neutralization of hCoV-NL63 was more variable and all sera showed only mod
80  the study, the prevalence of infection with HCoV-NL63 was not greater in patients with KS than in co
81 Netherlands in 2004, human coronavirus NL63 (HCoV-NL63) was found to cause worldwide infections.
82                  One-way cross-reactivity of HCoV-NL63 with group 1 CoVs was localized to aa 1 to 39