Sequence : Nsp1

Total row(s): 14
Select item(s)
Key Findings
Original Article
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Phylogenetic analysis of Israeli and Non-Israeli SARS-CoV-2 sequences revealed that the Israeli SARS-CoV-2 Strain containing P681H mutation originated from the B.1.1.50 Pangolin lineage. Pre-print (medRXiv)
Date of Publishing 2021 Mar 25
Title A unique SARS-CoV-2 spike protein P681H strain detected in Israel
Author(s) nameNeta S. Zuckerman, Shay Fleishon et al.
Date of Entry 2021 Jun 14
The study reports a newly identified SARS-CoV-2 Strain from Israel. The strain included a non-synonymous mutation in the S protein: P681H (C23604A) and additional four synonymous mutations, Nsp3:C7765T, Nsp12b: C13821T, Nsp16:T21111C, and C29545A. Pre-print (medRXiv)
Date of Publishing -
Title A unique SARS-CoV-2 spike protein P681H strain detected in Israel
Author(s) name -
Date of Entry 2021 Jun 14
Indian metadata was analyzed to associate the frequent mutations and co-mutation patterns with COVID-19 patient status (deceased, symptomatic, mild, and asymptomatic groups). Pre-print (bioRXiv)
Date of Publishing 2021 Mar 25
Title Genomic surveillance and phylodynamic analyses reveal emergence of novel mutation and co-mutation patterns within SARS-CoV2 variants prevalent in India
Author(s) nameNupur Biswas, Priyanka Mallick et al.
Date of Entry 2021 Jun 14
Mutation analysis of 2213 complete genomes from six geographical regions worldwide revealed 3178 polymorphic sites. Of these polymorphic sites, 58.5% (1861 sites) were non-synonymous, compared with the reference genome, Wuhan-Hu-1. Seven frequent non-synonymous mutations were observed in the global population of SARS-CoV-2. 33572190
(Pathogens)
PMID
33572190
Date of Publishing: 2021 Feb 9
Title Molecular Epidemiology Surveillance of SARS-CoV-2: Mutations and Genetic Diversity One Year after Emerging
Author(s) nameFlores-Alanis A, Cruz-Rangel A et al.
Journal Pathogens
Impact factor
3.31
Citation count: 1
62 mutations identified, including 30 mis-sense mutations, in 22 Moroccan patient isolates showed that Spike_D614G and NSP12_P323L mutations were present in all the analyzed sequences, whereas N_G204R and N_R203K were present in 9 sequences. 33558859
(Biosaf Health)
PMID
33558859
Date of Publishing: 2021 Feb 3
Title Genetic diversity and genomic epidemiology of SARS-CoV-2 in Morocco
Author(s) nameBadaoui B, Sadki K et al.
Journal Biosaf Health
Impact factor
Cant find
Citation count: 1
Most frequent and prevalent mutation reported, with reference to Wuhan sequence (hCoV-19/Wuhan/WIV04/2019), was P323L in the non-structural protein 12 (94.7%) whereas the second frequent mutation was D614G in the Spike glycoprotein region (92.6%), followed by G71S in the non-structural protein 5 (70%). 33359061
(Int J Infect Dis)
PMID
33359061
Date of Publishing: 2020 Dec 21
Title Molecular epidemiology of COVID-19 in Oman: A molecular andsurveillance study for the early transmission of COVID-19 in thecountry
Author(s) nameAl-Mahruqi S, Al-Wahaibi A et al.
Journal Int J Infect Dis
Impact factor
3.42
Citation count: 1
Compared to the SARS-CoV-2 reference genome (GenBank accession number: MN996528.1), the SARS-CoV-2 genome of Bangladesh, BCSIR-NILMRC-006, (accession number: MT539159) had eight mutations. A unique mutation was observed in the non-structural protein NSP2 of the ORF1ab gene. 32972934
(Microbiol Resour Announc)
PMID
32972934
Date of Publishing: 2020 Sep 24
Title Coding-Complete Genome Sequences of Three SARS-CoV-2 Strains from Bangladesh
Author(s) nameAkter S, Banu TA et al.
Journal Microbiol Resour Announc
Impact factor
0.88
Citation count: 1
Compared to the SARS-CoV-2 reference genome (GenBank accession number: MN996528.1), the SARS-CoV-2 genome of Bangladesh, BCSIR-NILMRC-007, (accession number: MT539158) had six mutations. 32972934
(Microbiol Resour Announc)
PMID
32972934
Date of Publishing: 2020 Sep 24
Title Coding-Complete Genome Sequences of Three SARS-CoV-2 Strains from Bangladesh
Author(s) nameAkter S, Banu TA et al.
Journal Microbiol Resour Announc
Impact factor
0.88
Citation count: 1
Compared to the SARS-CoV-2 reference genome (GenBank accession number: MN996528.1), the SARS-CoV-2 genome of Bangladesh, BCSIR-NILMRC-008, (accession number: MT539160) had six mutations. 32972934
(Microbiol Resour Announc)
PMID
32972934
Date of Publishing: 2020 Sep 24
Title Coding-Complete Genome Sequences of Three SARS-CoV-2 Strains from Bangladesh
Author(s) nameAkter S, Banu TA et al.
Journal Microbiol Resour Announc
Impact factor
0.88
Citation count: 1
Mutation analysis of 2492 SARS-CoV-2 genomes (belonging to 58 different countries representing six continents and five different climatic zones) revealed 1516 nucleotide variations, 744 amino acid substitutions, and 12 deletion sites. The pattern of mutations was different among the six different continents (Europe, Asia, North America, South America, Africa, and Australia) and five different climatic zones (temperate, tropical, diverse, dry, and continental). 32814791
(Sci Rep)
PMID
32814791
Date of Publishing: 2020 Aug 19
Title Genome-wide analysis of SARS-CoV-2 virus strains circulating worldwide implicates heterogeneity
Author(s) nameIslam MR, Hoque MN et al.
Journal Sci Rep
Impact factor
4.12
Citation count: 17
Compared to the SARS-CoV-2 reference genome (MN908947.3), the SARS-CoV-2 isolate, CHRF_nCoV19_0001/Bangladesh (accession number: MT476385), was observed to have nine mutations. 32527780
(Microbiol Resour Announc)
PMID
32527780
Date of Publishing: 2020 Jun 11
Title Complete Genome Sequence of a Novel Coronavirus (SARS-CoV-2) Isolate from Bangladesh
Author(s) nameSaha S, Malaker R et al.
Journal Microbiol Resour Announc
Impact factor
0.88
Citation count: 4
Primer pairs for a real-time RT-PCR test specific for the nsp1 gene of SARS-CoV-2. 32501535
(J Med Virol)
PMID
32501535
Date of Publishing: 2020 Nov
Title Identification of nsp1 gene as the target of SARS-CoV-2 real time RT-PCR using nanopore whole genome sequencing
Author(s) nameChan WM, Ip JD et al.
Journal J Med Virol
Impact factor
2.07
Citation count: 5
Probe for a real-time RT-PCR test specific for the nsp1 gene of SARS-CoV-2. 32501535
(J Med Virol)
PMID
32501535
Date of Publishing: 2020 Nov
Title Identification of nsp1 gene as the target of SARS-CoV-2 real time RT-PCR using nanopore whole genome sequencing
Author(s) nameChan WM, Ip JD et al.
Journal J Med Virol
Impact factor
2.07
Citation count: 5
Sequence alignment of SARSCoV2 Nsp15 coronaviral homologs with SARSCoV2, SARSCoV, MERSCoV, HCoV229E, MHV 32304108
(Protein Sci)
PMID
32304108
Date of Publishing: 2020 Jul
Title Crystal structure of Nsp15 endoribonuclease NendoU from SARSCoV2
Author(s) nameKim Y, Jedrzejczak R et al.
Journal Protein Sci
Impact factor
2.4
Citation count: 58

Structure : Nsp1

Total row(s): 19
Select item(s)
Key Findings
Original Article
(hover to see details)
The pseudoknot at the entry to the mRNA channel is a key structural characteristic for translation of the SARS-CoV-2 RNA genome. It specifically interacts with ribosomal proteins (Rabbit 80S ribosome) and 18S rRNA and causes ribosomal pausing prior to -1 frameshifting and the translating ribosome structure. Here, rabbit 80S ribosome colliding in another ribosome stalled by the SARS-CoV-2 pseudoknot is structurally characterized. 34029205
(Science)
PMID
34029205
Date of Publishing: 2021 Jun 18
Title Structural basis of ribosomal frameshifting during translation of the SARS-CoV-2 RNA genome
Author(s) nameBhatt PR, Scaiola A et al.
Journal Science
Impact factor
20.57
Citation count: 2
Date of Entry 2021 Aug 11
The pseudoknot at the entry to the mRNA channel is a key structural characteristic for translation of the SARS-CoV-2 RNA genome. It specifically interacts with ribosomal proteins (Rabbit 80S ribosome) and 18S rRNA and causes ribosomal pausing prior to -1 frameshifting and the translating ribosome structure. By cryo-electron microscopy the structure of rabbit 80S ribosome in complex with eRF1 and ABCE1, stalled at the STOP codon in the mutated SARS-CoV-2 slippery site is studied. 34029205
(Science)
PMID
34029205
Date of Publishing: 2021 Jun 18
Title Structural basis of ribosomal frameshifting during translation of the SARS-CoV-2 RNA genome
Author(s) nameBhatt PR, Scaiola A et al.
Journal Science
Impact factor
20.57
Citation count: 2
Date of Entry 2021 Aug 11
The pseudoknot at the entry to the mRNA channel is a key structural characteristic for translation of the SARS-CoV-2 RNA genome. It specifically interacts with ribosomal proteins (Rabbit 80S ribosome) and 18S rRNA and causes ribosomal pausing prior to -1 frameshifting and the translating ribosome structure was studied by cryo-electron microscopy. The rabbit 80S ribosome is stalled close to the mutated SARS-CoV-2 slippery site by a pseudoknot. 34029205
(Science)
PMID
34029205
Date of Publishing: 2021 Jun 18
Title Structural basis of ribosomal frameshifting during translation of the SARS-CoV-2 RNA genome
Author(s) nameBhatt PR, Scaiola A et al.
Journal Science
Impact factor
20.57
Citation count: 2
Date of Entry 2021 Aug 11
The pseudoknot at the entry to the mRNA channel is a key structural characteristic for translation of the SARS-CoV-2 RNA genome. It specifically interacts with ribosomal proteins (Rabbit 80S ribosome) and 18S rRNA and causes ribosomal pausing prior to -1 frameshifting and the translating ribosome structure was studied by cryo-electron microscopy to a high resolution. 34029205
(Science)
PMID
34029205
Date of Publishing: 2021 Jun 18
Title Structural basis of ribosomal frameshifting during translation of the SARS-CoV-2 RNA genome
Author(s) nameBhatt PR, Scaiola A et al.
Journal Science
Impact factor
20.57
Citation count: 2
Date of Entry 2021 Aug 11
Structure of SARS-CoV-2 Nsp15 endoribonuclease with Uridine-2',3'-Vanadate (UV, a transition state analog), results in the formation of 2′,3′-cyclic phosphodiester. This is critical for further RNA maturations and functions. 33564093
(Commun Biol)
PMID
33564093
Date of Publishing: 2021 Feb 9
Title Tipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU from SARS-CoV-2
Author(s) nameKim Y, Wower J et al.
Journal Commun Biol
Impact factor
~
Citation count: 2
Date of Entry 2021 Aug 2
The structure of Tipiracil (a uracil derivative ) and SARS-CoV-2 Nsp15 endoribonuclease shows Tipiracil competitively inhibits the enzyme action by binding to its active site. 33564093
(Commun Biol)
PMID
33564093
Date of Publishing: 2021 Feb 9
Title Tipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU from SARS-CoV-2
Author(s) nameKim Y, Wower J et al.
Journal Commun Biol
Impact factor
~
Citation count: 2
Date of Entry 2021 Aug 2
SARS-CoV-2 Nsp15 is inhibited by interactions with the uridine binding pocket in the enzyme's active site. Structure of SARS CoV-2 Nsp15 endoribonuclease in complex with Uridine-5'-Monophosphate shows Nsp15 discriminates between the uracil and purine bases by forming van der Waals contacts with Tyr343 and hydrogen bonds Ser294 (an active site residue ). 33564093
(Commun Biol)
PMID
33564093
Date of Publishing: 2021 Feb 9
Title Tipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU from SARS-CoV-2
Author(s) nameKim Y, Wower J et al.
Journal Commun Biol
Impact factor
~
Citation count: 2
Date of Entry 2021 Aug 2
Structure of SARS-CoV-2 Nsp15 endoribonuclease in complex with 3'-uridine monophosphate shows uracil demonstrates higher affinity for Trp333 site than in uracil-recognition site created by His235, His250, and Thr341. 33564093
(Commun Biol)
PMID
33564093
Date of Publishing: 2021 Feb 9
Title Tipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU from SARS-CoV-2
Author(s) nameKim Y, Wower J et al.
Journal Commun Biol
Impact factor
~
Citation count: 2
Date of Entry 2021 Aug 2
Structure of SARS-CoV-2 Nsp15 endoribonuclease in complex with dinucleoside monophosphate (GpU), which binds to the active site of the enzyme with uracil interacting with Tyr343 and Ser294. This results in the SARS-CoV-2 Nsp15 is inhibition. 33564093
(Commun Biol)
PMID
33564093
Date of Publishing: 2021 Feb 9
Title Tipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU from SARS-CoV-2
Author(s) nameKim Y, Wower J et al.
Journal Commun Biol
Impact factor
~
Citation count: 2
Date of Entry 2021 Aug 2
Structural characterisation of SARS-CoV-2 mini replication and transcription complex 33208736
(Nat Commun)
PMID
33208736
Date of Publishing: 2020 Nov 18
Title Architecture of a SARS-CoV-2 mini replication and transcription complex
Author(s) nameYan L, Zhang Y et al.
Journal Nat Commun
Impact factor
11.8
Citation count: 4
Structural characterisation of SARS-CoV-2 mini replication and transcription complex 33208736
(Nat Commun)
PMID
33208736
Date of Publishing: 2020 Nov 18
Title Architecture of a SARS-CoV-2 mini replication and transcription complex
Author(s) nameYan L, Zhang Y et al.
Journal Nat Commun
Impact factor
11.8
Citation count: 4
 Structural characterization of SARS-CoV-2 nsp10 in its unbound form and its behavior in a liquid. 33036230
(Int J Mol Sci)
PMID
33036230
Date of Publishing: 2020 Oct 6
Title Crystal Structure of Non-Structural Protein 10 from Severe Acute Respiratory Syndrome Coronavirus-2
Author(s) nameRogstam A, Nyblom M et al.
Journal Int J Mol Sci
Impact factor
4.21
Citation count: 1
The structure of the SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) complex in its active form comprises the non-structural protein 12 (nsp12), nsp8, and nsp7, and more than two turns of RNA template-product duplex. The active-site cleft of nsp12 binds to the first turn of RNA. Two copies of nsp8 bind to opposite sides of the cleft and position the second turn of RNA. Long helical extensions in nsp8 protrude along exiting RNA, forming positively charged 'sliding poles'. These sliding poles help in the processivity of RdRp, required for replicating the long genome of coronaviruses. 32438371
(Nature)
PMID
32438371
Date of Publishing: 2020 Aug
Title Structure of replicating SARS-CoV-2 polymerase
Author(s) nameHillen HS, Kokic G et al.
Journal Nature
Impact factor
24.36
Citation count: 74
Structural characteirzation of the nsp12-nsp7-nsp8 complex bound to the template-primer RNA and triphosphate form of Remdesivir(RTP) 32358203
(Science)
PMID
32358203
Date of Publishing: 2020 Jun 26
Title Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir
Author(s) nameYin W, Mao C et al.
Journal Science
Impact factor
20.57
Citation count: 156
Structural characterization of cryo-EM structure of the apo nsp12-nsp7-nsp8 complex 32358203
(Science)
PMID
32358203
Date of Publishing: 2020 Jun 26
Title Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir
Author(s) nameYin W, Mao C et al.
Journal Science
Impact factor
20.57
Citation count: 156
Structural characterization of NSP15 Endoribonuclease from SARS CoV-2 in the complex with a citrate 32304108
(Protein Sci)
PMID
32304108
Date of Publishing: 2020 Jul
Title Crystal structure of Nsp15 endoribonuclease NendoU from SARSCoV2
Author(s) nameKim Y, Jedrzejczak R et al.
Journal Protein Sci
Impact factor
2.4
Citation count: 58
Structural characterization of NSP15 Endoribonuclease from SARS CoV-2 32304108
(Protein Sci)
PMID
32304108
Date of Publishing: 2020 Jul
Title Crystal structure of Nsp15 endoribonuclease NendoU from SARSCoV2
Author(s) nameKim Y, Jedrzejczak R et al.
Journal Protein Sci
Impact factor
2.4
Citation count: 58
Structure of SARS-CoV-2 RNA-dependent RNA polymerase nsp12 in complex with cofactors nsp7 and nsp8 under reducing condition, forms a β hairpin domain (residues N215 to N218) at its N-terminus. This structure aids in antiviral viral study of remdesivir and other antiviral drugs. 32277040
(Science)
PMID
32277040
Date of Publishing: 2020 May 15
Title Structure of the RNA-dependent RNA polymerase from COVID-19 virus
Author(s) nameGao Y, Yan L et al.
Journal Science
Impact factor
20.57
Citation count: 198
Date of Entry 2021 Jul 28
Structure of SARS-Cov-2 RNA-dependent RNA polymerase nsp12, in complex with nsp7 and nsp8 reports a conserved polymerase core and a β hairpin domain (residues N215 to N218) at its N-terminus. This structure aids in the study of remdesivir and other drug candidates' antiviral activity. 32277040
(Science)
PMID
32277040
Date of Publishing: 2020 May 15
Title Structure of the RNA-dependent RNA polymerase from COVID-19 virus
Author(s) nameGao Y, Yan L et al.
Journal Science
Impact factor
20.57
Citation count: 198
Date of Entry 2021 Jul 28

Drugs : Nsp1

Total row(s): 9
Select item(s)
Key Findings
Original Article
(hover to see details)
11,000 compounds out of this library was chosen for target-specific virtual screening based on Lipinskis rule of 5. The natural screening suggested two efficient compounds (PubChem ID: 95372568 and 1776037) with dihydroxyphenyl region of the compound, found to be important in the interaction with the viral protein showing promising activity which may act as a potent lead inhibitory molecule against the virus. In combina tion with virtual screening, modelling, drug like liness, molecular docking, and 500 ns cumulative molecular dynamics simulations (100 ns for each complex) along with the decomposition analysis to calculate and confirm the stability and fold, we propose 95372568 and 1776037 as novel compo unds of natural origin capable of getting develop ed into potent lead molecules against SARS-CoV- 2 target protein NSP15. 33963942
(J Mol Model)
PMID
33963942
Date of Publishing: 2021 May 8
Title Analysis of natural compounds against the activity of SARS-CoV-2 NSP15 protein towards an effective treatment against COVID-19: a theoretical and computational biology approach
Author(s) name Motwalli O, Alazmi M.
Journal J Mol Model
Citation count 1
Date of Entry 2021 Sep 5
Different potential repurposed drugs, including, chloroquine , hydroxychloroquine, ivermectin, remdesivir, and favipiravir, were screened in the present study. Molecular docking of these drugs with different SARS-CoV-2 target proteins, including spike and membrane proteins, RdRp, nucleoproteins, viral proteases, and nsp14, was performed. Molecular dynamics simulation and MM-PBSA calculation were also conducted. Ivermectin and remdesivir were found to be the most promising drugs. 33746908
()
PMID
33746908
Title Molecular Docking Reveals Ivermectin and Remdesivir as Potential Repurposed Drugs Against SARS-CoV-2
Date of Entry 2021 Sep 5
Virulence protein factor Nsp1 was targeted by in silico virtual screening of ligand libraries. Molecular docking simulations of the top6 screened ligands with Nsp1 were used and the ligand-Nsp1 complexes were subjected to molecular dynamics simulations to analyze the behaviours of the ligands in a virtual cell 33612076
(J Biomol Struct Dyn)
PMID
33612076
Date of Publishing: 2021 Feb 22
Title Identification of the binding interactions of some novel antiviral compounds against Nsp1 protein from SARS-CoV-2 (COVID-19) through high throughput screening.
Author(s) name Chowdhury N, Bagchi A.
Journal J Biomol Struct Dyn
Impact factor
3.22
Citation count: 1
Date of Entry 2021 Sep 5
Virtual screening of 970 000 chemical compounds against the ATP-binding site to identify potential inhibitors indicates two of the top drug hits (Cepharanthine,Lumacaftor) have significant activity in inhibiting purified recombinant SARS-CoV-2 helicase. 33052685
(J Phys Chem Lett)
PMID
33052685
Date of Publishing: 2020 Nov 5
Title Discovery of COVID-19 Inhibitors Targeting the SARS-CoV-2 Nsp13 Helicase
Author(s) name White MA, Lin W, Cheng X.
Journal J Phys Chem Lett
Impact factor
7.33
Citation count: 2
Date of Entry 2021 Sep 5
The study showed that SARS-CoV-2 NSP14-a bifunctional enzyme ,could be a potential drug target for intervention and four drugs-Saquinavir, Hypericin, Baicalein and Bromocriptine were seen to be able to bind to the N-terminal and C-terminal domains of SARS-CoV-2 NSP 14 were seen as potential drug targets for intervention. 32923004
(J Pharm Anal)
PMID
32923004
Date of Publishing: 2020 Sep 7
Title Potential Treatment of Chinese and Western Medicine Targeting Nsp14 of SARS-CoV-2
Author(s) nameLiu C, Zhu X et al.
Journal J Pharm Anal
Impact factor
4.84
Citation count: 3
Date of Entry 2021 Sep 5
In-silico models of Nsp13 helicase and nsp14 were generated using comparative homology modelling. The structures were validated and then used for virtual screening of pre-existing, FDA approved antiviral drugs.This was done to verify that these drugs could be repurposed to be used against SARS-CoV-2 infection. 32875166
(Gene Rep)
PMID
32875166
Date of Publishing: 2020 Dec
Title In silico structure modelling of SARS-CoV-2 Nsp13 helicase and Nsp14 and repurposing of FDA approved antiviral drugs as dual inhibitors
Author(s) name Gurung AB.
Journal Gene Rep
Impact factor
0.61
Citation count: 5
Date of Entry 2021 Sep 5
In the present study, the in silico models of SARS-CoV-2 nsp13 helicase and nsp14 protein were elucidated using a comparative homology modelling approach. Simeprevir (SMV), Paritaprevir (PTV) and Grazoprevir (GZR) were the common leads identified which show higher binding affinity to both nsp13 helicase and nsp14 as compared to the control inhibitors and therefore, they might be potential dual-target inhibitors. 32875166
(Gene Rep)
PMID
32875166
Date of Publishing: 2020 Dec
Title In silico structure modelling of SARS-CoV-2 Nsp13 helicase and Nsp14 and repurposing of FDA approved antiviral drugs as dual inhibitors
Author(s) name Gurung AB.
Journal Gene Rep
Impact factor
0.61
Citation count: 5
Date of Entry 2021 Sep 5
The in silico models were further used for virtual screening of the Food and Drug Administration (FDA) approved antiviral drugs. Simeprevir (SMV), Paritaprevir (PTV) and Grazoprevir (GZR) were the common leads identified which show higher binding affinity to both nsp13 helicase and nsp14 as compared to the control inhibitors and therefore, they might be potential dual-target inhibitors. 32875166
(Gene Rep)
PMID
32875166
Date of Publishing: 2020 Dec
Title In silico structure modelling of SARS-CoV-2 Nsp13 helicase and Nsp14 and repurposing of FDA approved antiviral drugs as dual inhibitors
Author(s) name Gurung AB.
Journal Gene Rep
Impact factor
0.61
Citation count: 5
Date of Entry 2021 Sep 5
Identification of a potent inhibitor of Methyltransferase, Endoribonuclease, Phosphatase and Main Protease enzymes of SARS CoV-2 by coumarin derivatives using insilico approach. The in silico studies were performed on maestro 12.0 software (Schrodinger LLC 2019, USA). Two thousand seven hundred fifty-five biologically active coumarin derivative was docked with above receptor proteins of SARS CoV-2. 32835632
(J Biomol Struct Dyn)
PMID
32835632
Date of Publishing: 2020 Aug 24
Title In silico validation of coumarin derivatives as potential inhibitors against Main Protease, NSP10/NSP16-Methyltransferase, Phosphatase and Endoribonuclease of SARS CoV-2
Author(s) name Maurya AK, Mishra N.
Journal J Biomol Struct Dyn
Impact factor
3.22
Citation count: 2
Date of Entry 2021 Sep 5

Diagnostics : Nsp1

Total row(s): 1
Select item(s)
Key Findings
Original Article
(hover to see details)
Reporting a novel nsp1 real-time RT-PCR assay for the detection of SARS-CoV-2, based on nanopore sequencing. 32501535
(J Med Virol)
PMID
32501535
Date of Publishing: 2020 Nov
Title Identification of nsp1 gene as the target of SARS-CoV-2 real time RT-PCR using nanopore whole genome sequencing
Author(s) nameChan WM, Ip JD et al.
Journal J Med Virol
Impact factor
2.07
Citation count: 5

Molecular_interactions : Nsp1

Total row(s): 3
Select item(s)
Key Findings
Original Article
(hover to see details)
Nsp13-1 stabilizes SARS-CoV-2 replication and transcription (RTC) complex by contacting with nsp13-2, which anchors the 5'-extension of RNA template, and interacting with nsp7-nsp8-nsp12-RNA. Different orientations of nsp13-1 results in different interactions with the two forms of mini RTC. 33208736
(Nat Commun)
PMID
33208736
Date of Publishing: 2020 Nov 18
Title Architecture of a SARS-CoV-2 mini replication and transcription complex
Author(s) nameYan L, Zhang Y et al.
Journal Nat Commun
Impact factor
11.8
Citation count: 4
Cryo-electron microscopy structure of the SARS-CoV-2 RdRp with non-structural protein 12 (nsp12), nsp8 and nsp7, and more than two turns of RNA template-product duplex, shows active-site cleft of nsp12 binds to the first turn of RNA and mediates RdRp activity and two copies of nsp8 bind to opposite sides of the cleft and position the second turn of RNA. Nsp8 along the exiting RNA, forms positively charged 'sliding poles' which affect the processivity of RdRp. 32438371
(Nature)
PMID
32438371
Date of Publishing: 2020 Aug
Title Structure of replicating SARS-CoV-2 polymerase
Author(s) nameHillen HS, Kokic G et al.
Journal Nature
Impact factor
24.36
Citation count: 74
The complex cryo-electron microscopy structure of SARS-CoV-2 RdRp with a 50-base template-primer RNA and remdesivir, shows the partial double-stranded RNA template is present in the central channel of RdRp where remdesivir is covalently attached as the first replicated base pair and results in the termination of chain elongation. 32358203
(Science)
PMID
32358203
Date of Publishing: 2020 Jun 26
Title Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir
Author(s) nameYin W, Mao C et al.
Journal Science
Impact factor
20.57
Citation count: 156