ライフサイエンスコーパス: HCoV-NL63

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1 virus (SARS-CoV) and human coronavirus NL63 (HCoV-NL63).

2 ike virus, an ancestor of the human pathogen HCoV-NL63.

3 molecules serve as attachment receptors for HCoV-NL63.

4 ction (PCR) with primers that also amplified HCoV-NL63.

5 A total of 8 illnesses were associated with HCoV-NL63, 1 with HCoV-HKU1.

6 Human coronavirus NL63 (HCoV-NL63), a common human respiratory pathogen, is asso

7 ACE2 protein was proposed as a receptor for HCoV-NL63 already in 2005, but an in-depth analysis of e

8 e HCoVs corresponded to the newly recognized HCoV-NL63 and HCoV-HKU1 viruses, and >20 different serot

9 ossibly facilitating the interaction between HCoV-NL63 and its receptor.

10 nts directed against human pathogens such as HCoV-NL63 and SARS-CoV.

11 Previous studies showed that HCoV-NL63 and the genetically distant severe acute respi

12 Patients infected by HCoV-NL63 are typically young children with upper and lo

13 er ACE2 interactions are sufficient to allow HCoV-NL63 binding to cells.

14 matched control subjects tested positive for HCoV-NL63 by reverse transcription-polymerase chain reac

15 not universal for all group 1 CoVs, because HCoV-NL63 did not cross-react with SARS-CoV.

16 d nsp4) and detected replicase proteins from HCoV-NL63-infected LLC-MK2 cells by immunofluorescence,

17 results show that the initial events during HCoV-NL63 infection are more complex than anticipated an

18 ly no effective antiviral therapy to contain HCoV-NL63 infection.

19 Human coronavirus NL63 (HCoV-NL63) is an alphacoronavirus that was first identif

20 Here we present the crystal structure of HCoV-NL63 M(pro) in complex with a Michael acceptor inhi

21 heir related zoonotic CoVs, our structure of HCoV-NL63 M(pro) provides critical insight into rational

22 nts with acute KD was positive by RT-PCR for HCoV-NL63/NH in a nasopharyngeal swab.

23 S-CoV spike (S) protein but not infection by HCoV-NL63 or a retrovirus pseudotyped with the HCoV-NL63

24 D, the PL(pro)s from SARS-CoV, MERS-CoV, and HCoV-NL63 physically interact with and stabilize RCHY1,

25 e replicase products and characterization of HCoV-NL63 PLP DUB activity will facilitate comparative s

26 acute respiratory syndrome (SARS) CoV PLpro, HCoV-NL63 PLP2 has DUB activity.

27 me 2 (ACE2) on cells previously resistant to HCoV-NL63 renders them susceptible, showing that ACE2 pr

28 s representing the amino-terminal end of the HCoV-NL63 replicase gene and established protease cis-cl

29 Here, we identify HCoV-NL63 replicase gene products and characterize two v

30 We found that HCoV-NL63 replicase products can be detected at 24 h pos

31 arly human strains replicated inefficiently, HCoV-NL63 replicated for multiple passages in the immort

32 and by filovirus GP proteins but not by the HCoV-NL63 S protein or the vesicular stomatitis virus G

33 lly less effect on infection mediated by the HCoV-NL63 S protein than on that mediated by the SARS-Co

34 oV-NL63 or a retrovirus pseudotyped with the HCoV-NL63 S protein.

35 ins unchanged across 30 clinical isolates of HCoV-NL63 strains.

36 In contrast, binding of HCoV-NL63 to heparan sulfates was required for viral att

37 Here we show that SARS-CoV, but not HCoV-NL63, utilizes the enzymatic activity of the cystei

38 These data suggest that, although HCoV-NL63 was circulating in children in our community d

39 the study, the prevalence of infection with HCoV-NL63 was not greater in patients with KS than in co

40 Netherlands in 2004, human coronavirus NL63 (HCoV-NL63) was found to cause worldwide infections.

41 One-way cross-reactivity of HCoV-NL63 with group 1 CoVs was localized to aa 1 to 39

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