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Search results 101 to 200 out of 414 for Sars

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Type Details Score
Allele  
Name: host response to SARS QTL 8, log titer; WSB/EiJ
Allele Type: QTL
Allele  
Name: host response to SARS QTL 8, log titer; NOD/ShiLtJ
Allele Type: QTL
Allele  
Name: host response to SARS QTL 4, vascular cuffing; CAST/EiJ
Allele Type: QTL
Publication
First Author: Law PY
Year: 2006
Journal: FEBS Lett
Title: Expression and functional characterization of the putative protein 8b of the severe acute respiratory syndrome-associated coronavirus.
Volume: 580
Issue: 15
Pages: 3643-8
Publication
First Author: Keng CT
Year: 2006
Journal: Virology
Title: The human severe acute respiratory syndrome coronavirus (SARS-CoV) 8b protein is distinct from its counterpart in animal SARS-CoV and down-regulates the expression of the envelope protein in infected cells.
Volume: 354
Issue: 1
Pages: 132-42
Publication  
First Author: Pereira F
Year: 2020
Journal: Infect Genet Evol
Title: Evolutionary dynamics of the SARS-CoV-2 ORF8 accessory gene.
Volume: 85
Pages: 104525
Publication  
First Author: Mohammad S
Year: 2020
Journal: Pathogens
Title: SARS-CoV-2 ORF8 and SARS-CoV ORF8ab: Genomic Divergence and Functional Convergence.
Volume: 9
Issue: 9
Publication
First Author: Chan JF
Year: 2020
Journal: Lancet
Title: A familial cluster of pneumonia associated with the 2019 novel coronavirus indicating person-to-person transmission: a study of a family cluster.
Volume: 395
Issue: 10223
Pages: 514-523
Publication  
First Author: Zhang Y
Year: 2021
Journal: Proc Natl Acad Sci U S A
Title: The ORF8 protein of SARS-CoV-2 mediates immune evasion through down-regulating MHC-Ι.
Volume: 118
Issue: 23
Publication  
First Author: Geng H
Year: 2021
Journal: Front Immunol
Title: SARS-CoV-2 ORF8 Forms Intracellular Aggregates and Inhibits IFNγ-Induced Antiviral Gene Expression in Human Lung Epithelial Cells.
Volume: 12
Pages: 679482
Publication
First Author: Qiu M
Year: 2005
Journal: Microbes Infect
Title: Antibody responses to individual proteins of SARS coronavirus and their neutralization activities.
Volume: 7
Issue: 5-6
Pages: 882-9
Publication
First Author: Moshynskyy I
Year: 2007
Journal: Virus Res
Title: Intracellular localization of the SARS coronavirus protein 9b: evidence of active export from the nucleus.
Volume: 127
Issue: 1
Pages: 116-21
Publication
First Author: von Grotthuss M
Year: 2003
Journal: Cell
Title: mRNA cap-1 methyltransferase in the SARS genome.
Volume: 113
Issue: 6
Pages: 701-2
Publication
First Author: Meier C
Year: 2006
Journal: Structure
Title: The crystal structure of ORF-9b, a lipid binding protein from the SARS coronavirus.
Volume: 14
Issue: 7
Pages: 1157-65
Publication
First Author: Gralinski LE
Year: 2015
Journal: PLoS Genet
Title: Genome Wide Identification of SARS-CoV Susceptibility Loci Using the Collaborative Cross.
Volume: 11
Issue: 10
Pages: e1005504
Publication
First Author: Liu SJ
Year: 2006
Journal: Vaccine
Title: Immunological characterizations of the nucleocapsid protein based SARS vaccine candidates.
Volume: 24
Issue: 16
Pages: 3100-8
Publication
First Author: Wu F
Year: 2020
Journal: Nature
Title: A new coronavirus associated with human respiratory disease in China.
Volume: 579
Issue: 7798
Pages: 265-269
Protein
Organism: Mus musculus/domesticus
Length: 512  
Fragment?: false
Publication
First Author: Tan J
Year: 2009
Journal: PLoS Pathog
Title: The SARS-unique domain (SUD) of SARS coronavirus contains two macrodomains that bind G-quadruplexes.
Volume: 5
Issue: 5
Pages: e1000428
Publication    
First Author: Orduz D
Year: 2015
Journal: Elife
Title: Interneurons and oligodendrocyte progenitors form a structured synaptic network in the developing neocortex.
Volume: 4
Publication
First Author: Imbert I
Year: 2006
Journal: EMBO J
Title: A second, non-canonical RNA-dependent RNA polymerase in SARS coronavirus.
Volume: 25
Issue: 20
Pages: 4933-42
Publication
First Author: Luo H
Year: 2005
Journal: Biochemistry
Title: SR-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization.
Volume: 44
Issue: 46
Pages: 15351-8
Publication
First Author: Johnson MA
Year: 2010
Journal: J Mol Biol
Title: SARS coronavirus unique domain: three-domain molecular architecture in solution and RNA binding.
Volume: 400
Issue: 4
Pages: 724-42
Publication
First Author: Lin X
Year: 2021
Journal: iScience
Title: ORF8 contributes to cytokine storm during SARS-CoV-2 infection by activating IL-17 pathway.
Volume: 24
Issue: 4
Pages: 102293
Publication
First Author: Li W
Year: 2003
Journal: Nature
Title: Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus.
Volume: 426
Issue: 6965
Pages: 450-4
Publication
First Author: Wong SK
Year: 2004
Journal: J Biol Chem
Title: A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2.
Volume: 279
Issue: 5
Pages: 3197-201
Publication
First Author: Belouzard S
Year: 2009
Journal: Proc Natl Acad Sci U S A
Title: Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites.
Volume: 106
Issue: 14
Pages: 5871-6
Publication
First Author: Teoh KT
Year: 2010
Journal: Mol Biol Cell
Title: The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis.
Volume: 21
Issue: 22
Pages: 3838-52
Publication
First Author: Surya W
Year: 2018
Journal: Biochim Biophys Acta Biomembr
Title: Structural model of the SARS coronavirus E channel in LMPG micelles.
Volume: 1860
Issue: 6
Pages: 1309-1317
Publication
First Author: Ma Y
Year: 2015
Journal: Proc Natl Acad Sci U S A
Title: Structural basis and functional analysis of the SARS coronavirus nsp14-nsp10 complex.
Volume: 112
Issue: 30
Pages: 9436-41
Publication
First Author: Kamitani W
Year: 2009
Journal: Nat Struct Mol Biol
Title: A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein.
Volume: 16
Issue: 11
Pages: 1134-40
Publication  
First Author: Sakai Y
Year: 2017
Journal: Virology
Title: Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication.
Volume: 510
Pages: 165-174
Publication
First Author: Guarino LA
Year: 2005
Journal: J Mol Biol
Title: Mutational analysis of the SARS virus Nsp15 endoribonuclease: identification of residues affecting hexamer formation.
Volume: 353
Issue: 5
Pages: 1106-17
Publication
First Author: Song W
Year: 2018
Journal: PLoS Pathog
Title: Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2.
Volume: 14
Issue: 8
Pages: e1007236
Publication  
First Author: Graham RL
Year: 2006
Journal: Adv Exp Med Biol
Title: The nsp2 proteins of mouse hepatitis virus and SARS coronavirus are dispensable for viral replication.
Volume: 581
Pages: 67-72
Allele
Name: angiotensin converting enzyme 2; endonuclease-mediated mutation 1, Maria Cecilia C Canesso
Allele Type: Endonuclease-mediated
Attribute String: Humanized sequence
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Publication
First Author: Akerström S
Year: 2007
Journal: Antiviral Res
Title: Inhibition of SARS-CoV replication cycle by small interference RNAs silencing specific SARS proteins, 7a/7b, 3a/3b and S.
Volume: 73
Issue: 3
Pages: 219-27
Publication
First Author: Huang C
Year: 2011
Journal: PLoS Pathog
Title: SARS coronavirus nsp1 protein induces template-dependent endonucleolytic cleavage of mRNAs: viral mRNAs are resistant to nsp1-induced RNA cleavage.
Volume: 7
Issue: 12
Pages: e1002433
Publication
First Author: Minakshi R
Year: 2009
Journal: PLoS One
Title: The SARS Coronavirus 3a protein causes endoplasmic reticulum stress and induces ligand-independent downregulation of the type 1 interferon receptor.
Volume: 4
Issue: 12
Pages: e8342
Publication
First Author: Gralinski LE
Year: 2017
Journal: G3 (Bethesda)
Title: Allelic Variation in the Toll-Like Receptor Adaptor Protein Ticam2 Contributes to SARS-Coronavirus Pathogenesis in Mice.
Volume: 7
Issue: 6
Pages: 1653-1663
Publication
First Author: Marra MA
Year: 2003
Journal: Science
Title: The Genome sequence of the SARS-associated coronavirus.
Volume: 300
Issue: 5624
Pages: 1399-404
Protein Domain
Type: Family
Description: This is a family of unknown function found in SARS and SARS-like coronaviruses. It includes uncharacterised protein 14 from SARS coronavirus 2 (SARS-CoV-2), Human SARS coronavirus (SARS-CoV) and Bat coronavirus Rp3/2004 (SARS-like coronavirus Rp3) []. In SARS-CoV, Orf14 is completely contained within the ORF encoding the nucleocapsid protein (N) []. In SARS-CoV-2 uncharacterised protein 14 is predicted to contain one transmembrane helix.
Publication
First Author: Hänel K
Year: 2006
Journal: J Biomed Sci
Title: Solution structure of the X4 protein coded by the SARS related coronavirus reveals an immunoglobulin like fold and suggests a binding activity to integrin I domains.
Volume: 13
Issue: 3
Pages: 281-93
Allele
Name: transgene insertion AC70, Chien-Te K Tseng
Allele Type: Transgenic
Attribute String: Humanized sequence, Inserted expressed sequence
Allele
Name: signal transducer and activator of transcription 1; targeted mutation 1, Robert D Schreiber
Allele Type: Targeted
Attribute String: Null/knockout
Gene
Type: gene
Organism: human
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Transgene
Type: transgene
Organism: mouse, laboratory
Allele
Name: transgene insertion 2, Stanley Perlman
Allele Type: Transgenic
Attribute String: Humanized sequence, Inserted expressed sequence
Transgene
Type: transgene
Organism: mouse, laboratory
Allele
Name: transgene insertion 1, Ralph Baric
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
Allele
Name: transgene insertion 1, Chuan Qin
Allele Type: Transgenic
Attribute String: Humanized sequence, Inserted expressed sequence
Transgene
Type: transgene
Organism: mouse, laboratory
Genotype
Symbol: Stat1/Stat1
Background: 129S6/SvEv-Stat1/Tac
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Tg(CAG-ACE2)AC70Ctkt/?
Background: either: (involves: BALB/c * C3H/HeJ * C57BL/6J) or (involves: C3H/HeJ * C57BL/6 * C57BL/6J)
Zygosity: ot
Has Mutant Allele: true
Genotype
Symbol: Tg(Ace2-ACE2)1Cqin/?
Background: involves: ICR
Zygosity: ot
Has Mutant Allele: true
Genotype
Symbol: Tg(K18-ACE2)2Prlmn/?
Background: involves: C57BL/6J * SJL/J
Zygosity: ot
Has Mutant Allele: true
Genotype  
Background: CC053/Unc
Zygosity: ot
Has Mutant Allele: false
Publication
First Author: Xu K
Year: 2009
Journal: Virology
Title: Severe acute respiratory syndrome coronavirus accessory protein 9b is a virion-associated protein.
Volume: 388
Issue: 2
Pages: 279-85
Publication
First Author: Sharma K
Year: 2011
Journal: PLoS One
Title: SARS-CoV 9b protein diffuses into nucleus, undergoes active Crm1 mediated nucleocytoplasmic export and triggers apoptosis when retained in the nucleus.
Volume: 6
Issue: 5
Pages: e19436
Protein Domain
Type: Family
Description: This is a family of proteins found in SARS and SARS-like coronaviruses. It includes Protein 9b from SARS coronavirus 2 (SARS-CoV-2), Human SARS coronavirus (SARS-CoV) and Bat coronaviruses.Protein 9b is one of 8 accessory proteins in SARS-CoV []. The gene (ORF 9b, also known as ORF13) that encodes this protein is included within the nucleocapsid (N) gene (alternative ORF) []. Data suggest that protein 9b is a structural component of SARS-CoV virions and functions as an unusual lipid binding protein [, ].SARS-CoV ORF-9b has been shown to localise to the outer mitochondrial membrane and to target mitochondrial antiviral signalling proteins (MAVS), suppressing innate immunity [, , ]. Antibodies against SARS-CoV ORF-9b have been found in patients, demonstrating that it is produced during infection [, ].Protein 9b from SARS CoV comprises 98 amino acids. Its structure has a novel fold which forms a dimeric tent-like beta structure with an amphipathic surface, and a central hydrophobic cavity that binds lipidmolecules []. This cavity is likely to be involved in membrane attachment [].Protein 9b is a group-specific protein of SARS coronavirus (CoV). The sequence of ORF-9b is well conserved in different SARS isolates, however, there is little homology between Protein 9b from SARS-CoV and the I protein (Protein 9b homologue) present in other coronaviruses [, , ].
Publication
First Author: Hammond RG
Year: 2017
Journal: Protein Sci
Title: SARS-unique fold in the Rousettus bat coronavirus HKU9.
Volume: 26
Issue: 9
Pages: 1726-1737
Protein Domain
Type: Domain
Description: This entry represents the SUD-C domain of Rousettus bat coronavirus (CoV) HKU9 non-structural protein 3 (NSP3) and other NSP3s from betacoronaviruses in the nobecovirus subgenera (D lineage).NSP3 of SARS coronavirus includes a SARS-unique domain (SUD) consisting of three globular domains separated by short linker peptide segments: SUD-N, SUD-M, and SUD-C. SUD-N and SUD-M are macro domains which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides) []. SUD is not as specific to SARS CoV as originally thought and is also found in Rousettus bat CoV HKU9 and related bat CoVs []. Similar to SARS SUD-C, Rousettus bat CoV HKU9 SUD-C (HKU9 C), also adopts a frataxin-like fold that has structural similarity to DNA-binding domains of DNA-modifying enzymes. However, there is little sequence similarity between the two domains. SARS SUD-C has been shown to bind to single-stranded RNA and recognize purine bases more strongly than pyrimidine bases; it also regulates the RNA binding behavior of the SARS SUD-M macrodomain. It is not known whether HKU9 C functions in the same way [].
Protein Domain
Type: Domain
Description: This entry represents the SUD-C of Middle East respiratory syndrome-related (MERS) coronavirus (CoV) NSP3 and other NSP3s from betacoronaviruses in the merbecovirus subgenera (C lineage), including several bat-CoVs such as Tylonycteris bat CoV HKU4, Pipistrellus bat CoV HKU5, and Hypsugo bat CoV HKU25.NSP3 of SARS coronavirus includes a SARS-unique domain (SUD) consisting of three globular domains separated by short linker peptide segments: SUD-N, SUD-M, and SUD-C. SUD-N and SUD-M are macro domains which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides) []. SUD is not as specific to SARS CoV as originally thought and is also found in MERS and related bat coronaviruses. Similar to SARS SUD-C, Tylonycteris bat-CoV HKU4 SUD-C (HKU4 C), a member of the MERS SUD-C group, also adopts a frataxin-like fold that has structural similarity to DNA-binding domains of DNA-modifying enzymes. However, there is little sequence similarity between the two domains. SARS SUD-C has been shown to bind to single-stranded RNA and recognise purine bases more strongly than pyrimidine bases; it also regulates the RNA binding behaviour of the SARS SUD-M macrodomain. It is not known whether MERS SUD-C or HKU4 C functions in the same way [, ].
Transgene
Type: transgene
Organism: mouse, laboratory
Genotype
Symbol: Tg(FOXJ1-ACE2)1Rba/?
Background: involves: C3H * C57BL/6
Zygosity: ot
Has Mutant Allele: true
Publication  
First Author: Deng L
Year: 2018
Journal: Viruses
Title: Suppression of NF-κB Activity: A Viral Immune Evasion Mechanism.
Volume: 10
Issue: 8
Publication
First Author: Zhang L
Year: 2018
Journal: Autophagy
Title: Viral strategies for triggering and manipulating mitophagy.
Volume: 14
Issue: 10
Pages: 1665-1673
Publication
First Author: Shi CS
Year: 2014
Journal: J Immunol
Title: SARS-coronavirus open reading frame-9b suppresses innate immunity by targeting mitochondria and the MAVS/TRAF3/TRAF6 signalosome.
Volume: 193
Issue: 6
Pages: 3080-9
Gene
Type: gene
Organism: human
Protein Domain
Type: Homologous_superfamily
Description: This superfamily represents a domain found in SARS and bat coronaviruses, which is about 70 amino acids in length. PL2pro is a domain of the non-structural protein NSP3, found associated with various other coronavirus proteins due to the polyprotein nature of most viral translation. The domain performs three of the cleavages required to separate the translated polyprotein into its distinct proteins []. Structurally, this domain consists of two α-helices and seven β-strands arranged into an antiparallel β-sheet.
Publication
First Author: Chen Y
Year: 2015
Journal: J Biol Chem
Title: X-ray Structural and Functional Studies of the Three Tandemly Linked Domains of Non-structural Protein 3 (nsp3) from Murine Hepatitis Virus Reveal Conserved Functions.
Volume: 290
Issue: 42
Pages: 25293-306
Protein Domain
Type: Domain
Description: MHV NSP3 contains a DPUP that is located N-terminal to the ubiquitin-like domain 2 (Ubl2) and papain-like protease 2 (PLP2) catalytic domain. It is structurally similar to the Severe Acute Respiratory Syndrome (SARS) CoV unique domain C (SUD-C), adopting a frataxin-like fold that has structural similarity to DNA-binding domains of DNA-modifying enzymes. SUD-C is also located N-terminal to Ubl2 and PLP2 in SARS NSP3, similar to the DPUP of MHV NSP3; however, unlike DPUP, it is preceded by SUD-N and SUD-M macrodomains that are absent in MHV NSP3. Though structurally similar, there is little sequence similarity between DPUP and SUD-C. SARS SUD-C has been shown to bind to single-stranded RNA and recognize purine bases more strongly than pyrimidine bases; it also regulates the RNA binding behavior of the SARS SUD-M macrodomain. It is not known whether DPUP functions in the same way [].This entry represents the DPUP (domain preceding Ubl2 and PLP2) of murine hepatitis virus (MHV) non-structural protein 3 (NSP3) and other NSP3s from betacoronaviruses in the embecovirus subgenera (A lineage), including human CoV OC43, rabbit CoV HKU14 and porcine hemagglutinating encephalomyelitis virus (HEV), among others.
Publication
First Author: Neuman BW
Year: 2008
Journal: J Virol
Title: Proteomics analysis unravels the functional repertoire of coronavirus nonstructural protein 3.
Volume: 82
Issue: 11
Pages: 5279-94
Publication      
First Author: Mann BJ
Year: 2022
Journal: bioRxiv
Title: Adenosine A2A receptor (A2AR) agonists improve survival in K28-hACE2 mice following SARS-CoV-2 infection.
Publication
First Author: Roberts A
Year: 2005
Journal: J Virol
Title: Aged BALB/c mice as a model for increased severity of severe acute respiratory syndrome in elderly humans.
Volume: 79
Issue: 9
Pages: 5833-8
Publication
First Author: Hogan RJ
Year: 2004
Journal: J Virol
Title: Resolution of primary severe acute respiratory syndrome-associated coronavirus infection requires Stat1.
Volume: 78
Issue: 20
Pages: 11416-21
Protein Domain
Type: Family
Description: This entry includes the ORF8 gene products (also known as NS8, accessory protein 8) from human SARS coronavirus (SARS-CoV), SARS-CoV-2, Bat coronavirus HKU3 and pangolin coronaviruses [].ORF8 is an accessory protein that is not shared by all members of subgenus sarbecovirus. The presence and location of ORF8 in the SARS-CoV-2 genome has led its classification with SARS-CoV [, ]. ORF8 is a potential pathogenicity factor which evolves rapidly to counter the immune response and facilitate the transmission between hosts []. ORF8 has been suggested to be one of the relevant genes in the study of human adaptation of the virus [, ].The ORF8 protein is a fast-evolving protein in SARS-related CoVs, with a tendency to recombine and undergo deletions. During the early phases of the SARS (SARS-CoV) epidemic in 2002, human isolates were found to possess a unique continuous ORF8 with 366 nucleotides and a predicted protein with 122 amino acids. During the middle and late phases of the SARS epidemic, two functional ORFs (ORF8a and ORF8b) were emerged; they are predicted to encode two small proteins, 8a with 39 amino acids and 8b with 84 amino acids. Interestingly, SARS-CoV-2 ORF8 has not undergone any significantly measurable deletion events, so its function as a full-length protein might be more important to its pathogenicity []. ORF8 plays a role in modulating host immune response []which may act by down-regulating major histocompatibility complex class I (MHC-I) []. It may inhibit expression of some members of the IFN-stimulated gene (ISG) family including hosts IGF2BP1/ZBP1, MX1 and MX2, and DHX58 []. ORF8 also binds to IL17RA receptor, leading to IL17 pathway activation and an increased secretion of pro-inflammatory factors, contributing to cytokine storm during COVID-19 infection [].
Protein Domain
Type: Family
Description: This subfamily includes the ORF8 immunoglobulin (Ig) domain proteins of bat coronavirus Rf1 (Bat SARS CoV Rf1) and Bat CoV 273/2005, which have been classified previously as type II ORF8 proteins.ORF8 is an accessory protein that is not shared by all members of subgenus sarbecovirus. The presence and location of ORF8 in the SARS-CoV-2 genome has led its classification with SARS-CoV [, ]. ORF8 is a potential pathogenicity factor which evolves rapidly to counter the immune response and facilitate the transmission between hosts []. ORF8 has been suggested to be one of the relevant genes in the study of human adaptation of the virus [, ].The ORF8 protein is a fast-evolving protein in SARS-related CoVs, with a tendency to recombine and undergo deletions. During the early phases of the SARS (SARS-CoV) epidemic in 2002, human isolates were found to possess a unique continuous ORF8 with 366 nucleotides and a predicted protein with 122 amino acids. During the middle and late phases of the SARS epidemic, two functional ORFs (ORF8a and ORF8b) were emerged; they are predicted to encode two small proteins, 8a with 39 amino acids and 8b with 84 amino acids. Interestingly, SARS-CoV-2 ORF8 has not undergone any significantly measurable deletion events, so its function as a full-length protein might be more important to its pathogenicity []. ORF8 plays a role in modulating host immune response []which may act by down-regulating major histocompatibility complex class I (MHC-I) []. It may inhibit expression of some members of the IFN-stimulated gene (ISG) family including hosts IGF2BP1/ZBP1, MX1 and MX2, and DHX58 []. ORF8 also binds to IL17RA receptor, leading to IL17 pathway activation and an increased secretion of pro-inflammatory factors, contributing to cytokine storm during COVID-19 infection [].
Publication  
First Author: Nakandakari-Higa S
Year: 2022
Journal: Front Immunol
Title: A minimally-edited mouse model for infection with multiple SARS-CoV-2 strains.
Volume: 13
Pages: 1007080
Publication
First Author: Imai Y
Year: 2008
Journal: Cell
Title: Identification of oxidative stress and Toll-like receptor 4 signaling as a key pathway of acute lung injury.
Volume: 133
Issue: 2
Pages: 235-49
Publication
First Author: Zumla A
Year: 2016
Journal: Nat Rev Drug Discov
Title: Coronaviruses - drug discovery and therapeutic options.
Volume: 15
Issue: 5
Pages: 327-47
Publication
First Author: Netland J
Year: 2010
Journal: Virology
Title: Immunization with an attenuated severe acute respiratory syndrome coronavirus deleted in E protein protects against lethal respiratory disease.
Volume: 399
Issue: 1
Pages: 120-128
Publication
First Author: Menachery VD
Year: 2016
Journal: Proc Natl Acad Sci U S A
Title: SARS-like WIV1-CoV poised for human emergence.
Volume: 113
Issue: 11
Pages: 3048-53
Publication  
First Author: Morales-Nebreda L
Year: 2021
Journal: JCI Insight
Title: Aging imparts cell-autonomous dysfunction to regulatory T cells during recovery from influenza pneumonia.
Volume: 6
Issue: 6
Publication
First Author: Channappanavar R
Year: 2016
Journal: Cell Host Microbe
Title: Dysregulated Type I Interferon and Inflammatory Monocyte-Macrophage Responses Cause Lethal Pneumonia in SARS-CoV-Infected Mice.
Volume: 19
Issue: 2
Pages: 181-93
Publication    
First Author: Klemm T
Year: 2020
Journal: EMBO J
Title: Mechanism and inhibition of the papain-like protease, PLpro, of SARS-CoV-2.
Pages: e106275
Publication
First Author: Subbarao K
Year: 2004
Journal: J Virol
Title: Prior infection and passive transfer of neutralizing antibody prevent replication of severe acute respiratory syndrome coronavirus in the respiratory tract of mice.
Volume: 78
Issue: 7
Pages: 3572-7
Publication
First Author: Subbarao K
Year: 2006
Journal: Trends Microbiol
Title: Is there an ideal animal model for SARS?
Volume: 14
Issue: 7
Pages: 299-303
Publication
First Author: Day CW
Year: 2009
Journal: Virology
Title: A new mouse-adapted strain of SARS-CoV as a lethal model for evaluating antiviral agents in vitro and in vivo.
Volume: 395
Issue: 2
Pages: 210-22
Publication
First Author: Hou YJ
Year: 2020
Journal: Cell
Title: SARS-CoV-2 Reverse Genetics Reveals a Variable Infection Gradient in the Respiratory Tract.
Volume: 182
Issue: 2
Pages: 429-446.e14
Publication    
First Author: Kumar S
Year: 2020
Journal: Virusdisease
Title: Selection of animal models for COVID-19 research.
Pages: 1-6
Protein Domain
Type: Homologous_superfamily
Description: This superfamily represents the N-terminal region of the SUD domain (SUD-N or Mac2) found in non-structural protein NSP3, the product of ORF1a in group 2 (beta) coronaviruses. It is found in human SARS-CoV and SARS-CoV-2 polyprotein 1a and 1ab, and in related coronavirus polyproteins [].Non-structural protein Nsp3 contains at least seven different functional modules within its 1922-amino-acid polypeptide chain. One of these is the so-called SARS (severe acute respiratory syndrome)-unique domain (SUD), a stretch of about 338 residues that is completely absent from any other coronavirus. The SUD domain may be responsible for the high pathogenicity of the SARS coronavirus, compared to other viruses of this family [, ]. Later, the NSP3 of MHV was shown by X-ray crystallography to contain a SUD-C-like fold, so it is no longer appropriate to call this domain "SARS-unique". This region has been renamed into "Domain Preceding Ubl2 and PL2pro"(DPUP) []. NSP3 has been shown to bind to viral RNA, nucleocapsid protein, as well as other viral proteins, and participates in polyprotein processing. It is a multifunctional protein comprising up to 16 different domains and regions []. SUD(core) exhibits a two-domain architecture. The N-terminal subdomain (SUD-N) and the C-terminal subdomain of SUDcore, also named middle SUD subdomain, or SUD-M [, ]. SUD-N has been shown to be dispensable for the SARS-CoV replication/transcription complex within the context of a SARS-CoV replicon []. SUD consists of three globular domains separated by short linker peptide segments: SUD-N, SUD-M, and SUD-C []. Among these, SUD-N and SUD-M are macrodomains. The SUD-N domain is a related macrodomain which also binds G-quadruplexes []. While SUD-N is specific to the NSP3 of SARS and betacoronaviruses of the sarbecovirus subgenera (B lineage), SUD-M is present in most NSP3 proteins except the NSP3 from betacoronaviruses of the embecovirus subgenera (A lineage). SUD-M, despite its name, is not specific to SARS. SUD-C adopts a frataxin-like fold, has structural similarity to DNA-binding domains of DNA-modifying enzymes, binds single-stranded RNA, and regulates the RNA binding behavior of the SUD-M macrodomain. SARS-CoV Nsp3 contains a third macrodomain (the X-domain). The X-domain may function as a module binding poly(ADP-ribose); however, SUD-N and SUD-M do not bind ADP-ribose, as the triple glycine sequence involved in its binding is not conserved in these [].
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory