|
|
| Zeile 2: |
Zeile 2: |
| | {{up|PHA antivirals by mechanism}} | | {{up|PHA antivirals by mechanism}} |
| | {{up|PHA pharmacophore by screened target}} | | {{up|PHA pharmacophore by screened target}} |
| − | {{qt|RSP - On RAS drugs}}
| + | |
| | | | |
| | {{ttp|p=32449939|t=2020. SARS-CoV-2 spike glycoprotein-binding proteins expressed by upper respiratory tract bacteria may prevent severe viral infection.|pdf=|usr=007}} | | {{ttp|p=32449939|t=2020. SARS-CoV-2 spike glycoprotein-binding proteins expressed by upper respiratory tract bacteria may prevent severe viral infection.|pdf=|usr=007}} |
| | | | |
| | | | |
| − | {{qt|PHA ACE2 regulation of ACE2}} | + | {{qt|PHA ACE2 Structure spike-ace2}} |
| − | {{tp|p=32291076|t=ä. EZH2-mediated H3K27me3 inhibits ACE2 expression |pdf=|usr=}}
| + | |
| − | {{tp|p=32133153|t=2020. Comparative genetic analysis of the novel coronavirus (2019-nCoV/SARS-CoV-2) receptor ACE2 in different populations |pdf=|usr=}}
| + | |
| − | {{tp|p=32372801|t=2020. (ACE2) Does a cell protein explain covid-19 severity?|pdf=|usr=}}
| + | |
| − | {{tp|p=32302706|t=2020. Physiological and pathological regulation of ACE2, the SARS-CoV-2 receptor |pdf=|usr=}}
| + | |
| − | {{ttp|p=32333398|t=2020. A hypothesis for pathobiology and treatment of COVID-19: The centrality of ACE1/ACE2 imbalance |pdf=|usr=}}
| + | |
| − | {{tp|p=32442315|t=2020. Alternative splicing of ACE2 possibly generates variants that may limit the entry of SARS-CoV-2: a potential therapeutic approach using SSOs.|pdf=|usr=007}}
| + | |
| − | | + | |
| − | {{qt|PHA ACE2 ace2 species specificity clade specificity}}
| + | |
| − | {{tp|p=32092392|t=2020. Analysis of angiotensin-converting enzyme 2 (ACE2) from different species sheds some light on cross-species receptor usage of a novel coronavirus 2019-nCoV |pdf=|usr=}}
| + | |
| − | {{tp|p=32199943|t=ä. Predicting the angiotensin converting enzyme 2 (ACE2) utilizing capability as the receptor of SARS-CoV-2 |pdf=|usr=}}
| + | |
| − | {{tp|p=32100877|t=ä. Composition and divergence of coronavirus spike proteins and host ACE2 receptors predict potential intermediate hosts of SARS?CoV?2 |pdf=|usr=}}
| + | |
| − | {{tp|p=32249956|t=ä. Structural variations in human ACE2 may influence its binding with SARS?CoV?2 spike protein |pdf=|usr=}}
| + | |
| − | {{tp|p=32374452|t=2020. SARS-CoV-2: Structural diversity, phylogeny, and potential animal host identification of spike glycoprotein |pdf=|usr=}}
| + | |
| − | {{tp|p=32239522|t=ä. SARS?CoV?2 spike protein favors ACE2 from Bovidae and Cricetidae |pdf=|usr=}}
| + | |
| − | {{tp|p=32520981|t=2020. ACE2 diversity in placental mammals reveals the evolutionary strategy of SARS-CoV-2.|pdf=|usr=008}}
| + | |
| − | | + | |
| − | | + | |
| | {{qt|PHA ACE2 in target tissues}} | | {{qt|PHA ACE2 in target tissues}} |
| − | {{tp|p=32199615|t=ä. Single cell RNA sequencing of 13 human tissues identify cell types and receptors of human coronaviruses |pdf=|usr=}}
| |
| − | {{tp|p=32430651|t=2020. The SARS-CoV-2 receptor, ACE-2, is expressed on many different cell types: implications for ACE-inhibitor- and angiotensin II receptor blocker-based cardiovascular therapies.|pdf=|usr=008}}
| |
| − | {{tp|p=32490715|t=2020. In vitro analysis of the renin-angiotensin system and inflammatory gene transcripts in human bronchial epithelial cells after infection with severe acute respiratory syndrome coronavirus.|pdf=|usr=007}}
| |
| − | {{tp|p=32279908|t=ä. Is the ACE2 Overexpression a Risk Factor for COVID-19 Infection?|pdf=|usr=}}
| |
| − | {{tp|p=32251718|t=2020. ACE2 at the centre of COVID-19 from paucisymptomatic infections to severe pneumonia |pdf=|usr=}}
| |
| − | {{tp|p=32227090|t=ä. The ACE2 expression in human heart indicates new potential mechanism of heart injury among patients infected with SARS-CoV-2 |pdf=|usr=}}
| |
| − | {{tp|p=32364961|t=2020. Severe respiratory SARS-CoV2 infection: Does ACE2 receptor matter?|pdf=|usr=}}
| |
| − | {{tp|p=32448590|t=ä. Marked Up-Regulation of ACE2 in Hearts of Patients With Obstructive Hypertrophic Cardiomyopathy: Implications for SARS-CoV-2 Mediated COVID-19 |pdf=|usr=}}
| |
| − | {{tp|p=32422146|t=2020. Type 2 inflammation modulates ACE2 and TMPRSS2 in airway epithelial cells.|pdf=|usr=008}}
| |
| − | {{tp|p=32531372|t=2020. Expression of SARS-CoV-2 Receptor ACE2 and Coincident Host Response Signature Varies by Asthma Inflammatory Phenotype.|pdf=|usr=008}}
| |
| − | {{tp|p=32366279|t=2020. Genetic alteration, RNA expression, and DNA methylation profiling of coronavirus disease 2019 (COVID-19) receptor ACE2 in malignancies: a pan-cancer analysis.|pdf=|usr=008}}
| |
| − | {{tp|p=32442454|t=2020. Which cancer type has the highest risk of COVID-19 infection?|pdf=|usr=008}}
| |
| − | {{tp|p=32454066|t=2020. High expression of ACE2 on the keratinocytes reveals skin as a potential target for SARS-CoV-2.|pdf=|usr=008}}
| |
| − | {{tp|p=32413354|t=2020. Age, inflammation and disease location are critical determinants of intestinal expression of SARS-CoV-2 receptor ACE2 and TMPRSS2 in inflammatory bowel disease.|pdf=|usr=008}}
| |
| − | {{tp|p=32339157|t=2020. ACE2 correlated with immune infiltration serves as a prognostic biomarker in endometrial carcinoma and renal papillary cell carcinoma: implication for COVID-19.|pdf=|usr=008}}
| |
| − | {{tp|p=32395525|t=2020. A profiling analysis on the receptor ACE2 expression reveals the potential risk of different type of cancers vulnerable to SARS-CoV-2 infection.|pdf=|usr=008}}
| |
| − | {{ttp|p=32413319|t=2020. SARS-CoV-2 Receptor ACE2 Is an Interferon-Stimulated Gene in Human Airway Epithelial Cells and Is Detected in Specific Cell Subsets across Tissues.|pdf=|usr=008}}
| |
| − | {{tp|p=32499922|t=2020. ACE2 expression and sex disparity in COVID-19.|pdf=|usr=008}}
| |
| − | {{tp|p=32525565|t=2020. Elevated expression of ACE2 in tumor-adjacent normal tissues of cancer patients.|pdf=|usr=008}}
| |
| − | {{tp|p=32526012|t=2020. ACE2 Expression is Increased in the Lungs of Patients with Comorbidities Associated with Severe COVID-19.|pdf=|usr=008}}
| |
| | | | |
| | + | {{qt|PHA ACE2 regulation of ACE2}} |
| | + | {{qt|PHA ACE2 drug design}} |
| | {{qt|PHA ACE2 amplification}} | | {{qt|PHA ACE2 amplification}} |
| − | {{tp|p=32469114|t=2020. An update on ACE2 amplification and its therapeutic potential.|pdf=|usr=008}}
| |
| − |
| |
| | {{qt|PHA ACE2 soluble ace2}} | | {{qt|PHA ACE2 soluble ace2}} |
| − | {{tp|p=32391299|t=2020. COVID-19 Infection and Circulating ACE2 Levels: Protective Role in Women and Children.|pdf=|usr=008}} | + | {{qt|RSP - On RAS drugs}} |
| − | {{tp|p=32410690|t=2020. Age and sex differences in soluble ACE2 may give insights for COVID-19.|pdf=|usr=008}}
| + | |
| − | {{tp|p=32396773|t=2020. Truncated human angiotensin converting enzyme 2; a potential inhibitor of SARS-CoV-2 spike glycoprotein and potent COVID-19 therapeutic agent.|pdf=|usr=008}}
| + | |
| − | {{tp|p=32333836|t=ä. Inhibition of SARS-CoV-2 Infections in Engineered Human Tissues Using Clinical-Grade Soluble Human ACE2 |pdf=|usr=}}
| + | |
| − | {{tp|p=32398309|t=2020. Could the smoking gun in the fight against Covid-19 be the (rh) ACE2?|pdf=|usr=008}}
| + | |
| − | {{tp|p=32438383|t=2020. Inhaled modified angiotensin converting enzyme 2 (ACE2) as a decoy to mitigate SARS-CoV-2 infection.|pdf=|usr=007}}
| + | |
| | | | |
| − | | + | {{qt|PHA ACE2 ace2 species specificity clade specificity}} |
| − | {{qt|PHA ACE2 Structure spike-ace2}} | + | |
| − | {{ttp|p=32500793|t=2020. Repurposing Nimesulide, a Potent Inhibitor of the B0AT1 Subunit of the SARS-CoV-2 Receptor, as a Therapeutic Adjuvant of COVID-19.|pdf=|usr=007}}
| + | |
| − | {{ttp|p=32492195|t=2020. Functional prediction and frequency of coding variants in human ACE2 at binding sites with SARS-CoV-2 spike protein on different populations.|pdf=|usr=007}}
| + | |
| − | {{tp|p=32448098|t=2020. Structural and simulation analysis of hotspot residues interactions of SARS-CoV 2 with human ACE2 receptor.|pdf=|usr=007}}
| + | |
| − | {{tp|p=32401043|t=2020. Conserved High Free Energy Sites in Human Coronavirus Spike Glycoprotein Backbones.|pdf=|usr=007}}
| + | |
| − | {{ttp|p=32404529|t=2020. Comparison of SARS-CoV-2 spike protein binding to ACE2 receptors from human, pets, farm animals, and putative intermediate hosts.|pdf=|usr=007}} '''cattle and sheep...'''
| + | |
| − | {{tp|p=32478523|t=2020. Comparing the Binding Interactions in the Receptor Binding Domains of SARS-CoV-2 and SARS-CoV.|pdf=|usr=007}}
| + | |
| − | {{tp|p=32422996|t=2020. Highly Conserved Homotrimer Cavity Formed by the SARS-CoV-2 Spike Glycoprotein: A Novel Binding Site.|pdf=|usr=007}}
| + | |
| − | {{tp|p=32057769|t=2020. The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade |pdf=|usr=}}
| + | |
| − | {{tp|p=32512386|t=2020. Proteolytic Cleavage of the SARS-CoV-2 Spike Protein and the Role of the Novel S1/S2 Site.|pdf=|usr=007}}
| + | |
| − | {{tp|p=32503918|t=2020. Enhanced receptor binding of SARS-CoV-2 through networks of hydrogen-bonding and hydrophobic interactions.|pdf=|usr=007}}
| + | |
| − | {{tp|p=32155444|t=ä. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein |pdf=|usr=}}
| + | |
| − | {{tp|p=32178593|t=2020. Emerging WuHan (COVID-19) coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26 |pdf=|usr=}}
| + | |
| − | {{tp|p=32320687|t=ä. Phylogenetic Analysis and Structural Modeling of SARS-CoV-2 Spike Protein Reveals an Evolutionary Distinct and Proteolytically Sensitive Activation Loop |pdf=|usr=}}
| + | |
| − | {{tp|p=32009228|t=2020. Evolution of the novel coronavirus from the ongoing Wuhan outbreak and modeling of its spike protein for risk of human transmission |pdf=|usr=}}
| + | |
| − | {{tp|p=32075877|t=2020. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation |pdf=|usr=}}
| + | |
| − | {{tp|p=32081428|t=2020. Structure analysis of the receptor binding of 2019-nCoV |pdf=|usr=}}
| + | |
| − | {{tp|p=32142651|t=2020. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor |pdf=|usr=}}
| + | |
| − | {{tp|p=32203189|t=ä. Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine |pdf=|usr=}}
| + | |
| − | {{tp|p=32275855|t=ä. Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2 |pdf=|usr=}}
| + | |
| − | {{tp|p=32201080|t=ä. Spike protein recognition of mammalian ACE2 predicts the host range and an optimized ACE2 for SARS-CoV-2 infection |pdf=|usr=}}
| + | |
| − | {{tp|p=32210742|t=2020. Role of changes in SARS-CoV-2 spike protein in the interaction with the human ACE2 receptor: An in silico analysis |pdf=|usr=}}
| + | |
| − | {{tp|p=32327200|t=ä. Covid-19 and the angiotensin-converting enzyme (ACE2): Areas for research |pdf=|usr=}}
| + | |
| − | {{ttp|p=32274964|t=2020. A review on the cleavage priming of the spike protein on coronavirus by angiotensin-converting enzyme-2 and furin |pdf=|usr=}}
| + | |
| − | {{tp|p=31996437|t=2020. Receptor Recognition by the Novel Coronavirus from Wuhan: an Analysis Based on Decade-Long Structural Studies of SARS Coronavirus |pdf=|usr=}}
| + | |
| − | {{ttp|p=32362314|t=ä. A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells |pdf=|usr=}}
| + | |
| − | {{tp|p=32221306|t=2020. Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV |pdf=|usr=}}
| + | |
| − | {{ttp|p=32150576|t=2020. Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry |pdf=|usr=}}
| + | |
| − | {{tp|p=32245784|t=2020. A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV |pdf=|usr=}}
| + | |
| − | {{ttp|p=32366695|t=ä. Site-specific glycan analysis of the SARS-CoV-2 spike |pdf=|usr=}}
| + | |
| − | {{tp|p=32132184|t=2020. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2 |pdf=|usr=}}
| + | |
| − | {{tp|p=32198713|t=ä. A Unique Protease Cleavage Site Predicted in the Spike Protein of the Novel Pneumonia Coronavirus (2019-nCoV) Potentially Related to Viral Transmissibility |pdf=|usr=}}
| + | |
| − | {{tp|p=32365751|t=2020. The SARS-CoV-2 Exerts a Distinctive Strategy for Interacting with the ACE2 Human Receptor |pdf=|usr=}}
| + | |
| − | {{tp|p=32378705|t=2020. A virus that has gone viral: amino acid mutation in S protein of Indian isolate of Coronavirus COVID-19 might impact receptor binding, and thus, infectivity |pdf=|usr=}}
| + | |
| − | {{tp|p=32132669|t=2020. Novel antibody epitopes dominate the antigenicity of spike glycoprotein in SARS-CoV-2 compared to SARS-CoV |pdf=|usr=}}
| + | |
| − | {{tp|p=32338224|t=2020. Focus on Receptors for Coronaviruses with Special Reference to Angiotensin-converting Enzyme 2 as a Potential Drug Target - A Perspective |pdf=|usr=}}
| + | |
| − | {{tp|p=32363391|t=ä. Deducing the N- and O- glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2 |pdf=|usr=}}
| + | |
| − | {{ttp|p=32374903|t=2020. SARS-CoV-2 viral spike G614 mutation exhibits higher case fatality rate |pdf=|usr=}}
| + | |
| − | {{tp|p=32376714|t=2020. Gene of the month: the 2019-nCoV/SARS-CoV-2 novel coronavirus spike protein |pdf=|usr=}}
| + | |
| − | {{tp|p=32225176|t=2020. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor |pdf=|usr=}}
| + | |
| − | {{tp|p=32225175|t=2020. Structural basis of receptor recognition by SARS-CoV-2 |pdf=|usr=}}
| + | |
| − | {{tp|p=32329276|t=2020. Spike protein in the detection and treatment of novel coronavirus |pdf=|usr=}}
| + | |
| − | {{tp|p=C7190498|t=ä. The biological characteristics of SARS-CoV-2 spike protein Pro330-Leu650 |pdf=|usr=}}
| + | |
| − | {{tp|p=32125455|t=ä. Angiotensin-converting enzyme 2 (ACE2) as a SARS-CoV-2 receptor: molecular mechanisms and potential therapeutic target |pdf=|usr=}}
| + | |
| − | {{tp|p=32369402|t=2020. ANNALS EXPRESS: Coronavirus disease 2019 (COVID-19) and the renin-angiotensin system: a closer look at angiotensin-converting enzyme 2 (ACE2) |pdf=|usr=}}
| + | |
| − | {{tp|p=32354022|t=2020. ACE2: The key Molecule for Understanding the Pathophysiology of Severe and Critical Conditions of COVID-19: Demon or Angel?|pdf=|usr=}}
| + | |
| − | {{tp|p=32306452|t=2020. Angiotensin-converting enzyme 2 in severe acute respiratory syndrome coronavirus and SARS-CoV-2: A double-edged sword?|pdf=|usr=}}
| + | |
| − | {{tp|p=32464271|t=2020. Could the D614G substitution in the SARS-CoV-2 spike (S) protein be associated with higher COVID-19 mortality?|pdf=|usr=008}}
| + | |
| − | {{tp|p=32383269|t=2020. In silico studies on the comparative characterization of the interactions of SARS-CoV-2 spike glycoprotein with ACE-2 receptor homologs and human TLRs.|pdf=|usr=008}}
| + | |
| − | {{tp|p=32463239|t=2020. Is the Rigidity of SARS-CoV-2 Spike Receptor-Binding Motif the Hallmark for Its Enhanced Infectivity? Insights from All-Atom Simulations.|pdf=|usr=008}}
| + | |
| − | {{tp|p=32502733|t=2020. Exploring the genomic and proteomic variations of SARS-CoV-2 spike glycoprotein: A computational biology approach.|pdf=|usr=008}}
| + | |
| − | {{tp|p=32410735|t=2020. Interaction of the spike protein RBD from SARS-CoV-2 with ACE2: Similarity with SARS-CoV, hot-spot analysis and effect of the receptor polymorphism.|pdf=|usr=008}}
| + | |
| − | {{tp|p=32415260|t=2020. Key residues of the receptor binding motif in the spike protein of SARS-CoV-2 that interact with ACE2 and neutralizing antibodies.|pdf=|usr=008}}
| + | |
| − | {{tp|p=32518941|t=2020. Identification of 22 N-glycosites on spike glycoprotein of SARS-CoV-2 and accessible surface glycopeptide motifs: implications for vaccination and antibody therapeutics.|pdf=|usr=008}}
| + | |
| − | | + | |
| − | | + | |
| − | | + | |
| − | {{qt|PHA ACE2 drug design}}
| + | |
| − | {{ttp|p=32437749|t=2020. Human Intestinal Defensin 5 Inhibits SARS-CoV-2 Invasion by Cloaking ACE2.|pdf=|usr=008}}
| + | |
| − | {{ttp|p=C7151553|t=2020. COVID-19 Coronavirus spike protein analysis for synthetic vaccines, a peptidomimetic antagonist, and therapeutic drugs, and analysis of a proposed achilles? heel conserved region to minimize probability of escape mutations and drug resistance |pdf=|usr=}}
| + | |
| − | {{tp|p=32286790|t=ä. Computational Design of ACE2-Based Peptide Inhibitors of SARS-CoV-2 |pdf=|usr=}}
| + | |
| − | {{tp|p=32455942|t=2020. Potential Therapeutic Targeting of Coronavirus Spike Glycoprotein Priming.|pdf=|usr=007}}
| + | |
| − | {{tp|p=32527713|t=2020. In Silico computational screening of Kabasura Kudineer - Official Siddha Formulation and JACOM against SARS-CoV-2 spike protein.|pdf=|usr=008}}
| + | |
| − | {{tp|p=32231345|t=2020. Inhibition of SARS-CoV-2 infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion |pdf=|usr=}}
| + | |
| − | {{tp|p=32354636|t=ä. Blockade of SARS-CoV-2 infection by recombinant soluble ACE2 |pdf=|usr=}}
| + | |
| − | {{tp|p=32332922|t=ä. SARS-CoV-2 infection of kidney organoids prevented with soluble human ACE2 |pdf=|usr=}}
| + | |
| − | {{tp|p=32294562|t=ä. A search for medications to treat COVID-19 via in silico molecular docking models of the SARS-CoV-2 spike glycoprotein and 3CL protease |pdf=|usr=}}
| + | |
| − | {{tp|p=32359080|t=2020. Off-target ACE2 ligands: Possible therapeutic option for CoVid-19?|pdf=|usr=}}
| + | |
| − | {{tp|p=32167153|t=2020. Soluble angiotensin-converting enzyme 2: a potential approach for coronavirus infection therapy?|pdf=|usr=}}
| + | |
| − | {{tp|p=32373991|t=2020. In silico screening of natural compounds against COVID-19 by targeting Mpro and ACE2 using molecular docking |pdf=|usr=}}
| + | |
| − | {{tp|p=32232976|t=2020. CD-sACE2 inclusion compounds: An effective treatment for coronavirus disease 2019 (COVID-19) |pdf=|usr=}}
| + | |
| − | {{tp|p=32362217|t=2020. In silico study the inhibition of angiotensin converting enzyme 2 receptor of COVID-19 by Ammoides verticillata components harvested from Western Algeria |pdf=|usr=}}
| + | |
| − | {{tp|p=32345124|t=2020. An in-silico evaluation of different Saikosaponins for their potency against SARS-CoV-2 using NSP15 and fusion spike glycoprotein as targets |pdf=|usr=}}
| + | |
| − | {{tp|p=32379346|t=2020. ACE2 Activators for the Treatment of Covid 19 Patients |pdf=|usr=}}
| + | |
| − | {{tp|p=32332765|t=2020. Neutralization of SARS-CoV-2 spike pseudotyped virus by recombinant ACE2-Ig |pdf=|usr=}}
| + | |
| − | {{tp|p=32376627|t=2020. Design of potent membrane fusion inhibitors against SARS-CoV-2, an emerging coronavirus with high fusogenic activity |pdf=|usr=}}
| + | |
| − | {{tp|p=32380200|t=ä. In Silico Design of Antiviral Peptides Targeting the Spike Protein of SARS-CoV-2 |pdf=|usr=}}
| + | |
| − | {{ttp|p=C7197610|t=ä. Isolation of a human monoclonal antibody specific for the receptor binding domain of SARS-CoV-2 using a competitive phage biopanning strategy |pdf=|usr=}}
| + | |
| − | {{ttp|p=32231345|t=ä. Inhibition of SARS-CoV-2 infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion |pdf=|usr=}}''Here we generated a series of lipopeptides derived from EK1 and found that EK1C4 was the most potent fusion inhibitor against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection''
| + | |
| − | {{tp|p=32336762|t=2012. Design of Angiotensin?converting Enzyme 2 (ACE2) Inhibitors by Virtual Lead Optimization and Screening |pdf=|usr=}}
| + | |
| − | {{tp|p=32380200|t=2020. In silico design of antiviral peptides targeting the spike protein of SARS-CoV-2 |pdf=|usr=}}
| + | |
| − | {{tp|p=32065055|t=2020. Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody |pdf=|usr=}}
| + | |
| − | {{tp|p=32285293|t=ä. Searching therapeutic strategy of new coronavirus pneumonia from angiotensin-converting enzyme 2: the target of COVID-19 and SARS-CoV |pdf=|usr=}}
| + | |
| − | {{tp|p=32313207|t=ä. Human monoclonal antibodies block the binding of SARS-CoV-2 spike protein to angiotensin converting enzyme 2 receptor |pdf=|usr=}}
| + | |
| − | {{tp|p=32451080|t=ä. A possible strategy to fight COVID-19: Interfering with spike glycoprotein trimerization |pdf=|usr=}}
| + | |
| − | {{tp|p=32423095|t=2020. The Expression and Polymorphism of Entry Machinery for COVID-19 in Human: Juxtaposing Population Groups, Gender, and Different Tissues.|pdf=|usr=007}}
| + | |
| − | {{tp|p=32403995|t=2020. Development of multi-specific humanized llama antibodies blocking SARS-CoV-2/ACE2 interaction with high affinity and avidity.|pdf=|usr=007}}
| + | |
| − | {{tp|p=32592145|t=2020. Identification of a Potential Peptide Inhibitor of SARS-CoV-2 Targeting its Entry into the Host Cells.|pdf=|usr=010}}
| + | |
| − | {{tp|p=32551560|t=2020. Discovery of Aptamers Targeting Receptor-Binding Domain of the SARS-CoV-2 Spike Glycoprotein.|pdf=|usr=010}}
| + | |
| − | {{tp|p=32547694|t=2020. Blocking Coronavirus 19 Infection via the SARS-CoV-2 Spike Protein: Initial Steps.|pdf=|usr=011}}
| + | |
| − | {{tp|p=32593613|t=2020. Testing of natural products in clinical trials targeting the SARS-CoV-2 (Covid-19) Viral Spike Protein-Angiotensin Converting Enzyme-2 (ACE2) interaction.|pdf=|usr=011}}
| + | |
| − | {{tp|p=32540428|t=2020. Eltrombopag is a potential target for drug intervention in SARS-CoV-2 spike protein.|pdf=|usr=011}}
| + | |
| − | {{tp|p=32552462|t=2020. Identification of bioactive compounds from Glycyrrhiza glabra as possible inhibitor of SARS-CoV-2 spike glycoprotein and non-structural protein-15: a pharmacoinformatics study.|pdf=|usr=011}}
| + | |
| − | {{ttp|p=32565126|t=2020. Targeting the SARS-CoV-2 spike glycoprotein prefusion conformation: virtual screening and molecular dynamics simulations applied to the identification of potential fusion inhibitors.|pdf=|usr=011}}
| + | |
