PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34787160-4 2021 Thus, four potential drugs (bromhexine, camostat, gabexate, and nafamostat) were used to explore the mechanism of binding with TMPRSS2 in this work. nafamostat 64-74 transmembrane serine protease 2 Homo sapiens 127-134 34787160-6 2021 Through the results of calculating binding free energy by nine methods, the binding affinity of camostat, gabexate, and nafamostat to TMPRSS2 showed great advantages compared with bromhexine, where the nafamostat was surprisingly found to present two reasonable binding conformations (forward and reverse directions). nafamostat 120-130 transmembrane serine protease 2 Homo sapiens 134-141 34787160-6 2021 Through the results of calculating binding free energy by nine methods, the binding affinity of camostat, gabexate, and nafamostat to TMPRSS2 showed great advantages compared with bromhexine, where the nafamostat was surprisingly found to present two reasonable binding conformations (forward and reverse directions). nafamostat 202-212 transmembrane serine protease 2 Homo sapiens 134-141 34575594-2 2021 Nafamostat mesylate (NFM) suppresses transmembrane serine protease 2 and SARS-CoV-2 S protein-mediated fusion. nafamostat 0-19 transmembrane serine protease 2 Homo sapiens 37-68 34406864-11 2021 Therefore, this study revealed that, at least, TMPRSS2 is involved in HE cleavage and suggested that nafamostat could be a candidate for therapeutic drugs of ICV infection. nafamostat 101-111 transmembrane serine protease 2 Homo sapiens 47-54 34590967-7 2021 PCA discloses the evidence of the structural similarities to the corresponding complexes of L1, L2, and L6 with the complex of TMPRSS2(TM) and Nafamostat mesylate (TM-NAM). nafamostat 143-162 transmembrane serine protease 2 Homo sapiens 127-134 34406858-4 2021 Similarly, inhibition of TMPRSS2 protease activity by camostat mesylate or nafamostat mesylate prevents infection mediated by the TMPRSS2-dependent and cathepsin-independent pathway. nafamostat 75-94 transmembrane serine protease 2 Homo sapiens 25-32 34406858-4 2021 Similarly, inhibition of TMPRSS2 protease activity by camostat mesylate or nafamostat mesylate prevents infection mediated by the TMPRSS2-dependent and cathepsin-independent pathway. nafamostat 75-94 transmembrane serine protease 2 Homo sapiens 130-137 34100014-4 2021 Similarly, inhibition of TMPRSS2 protease activity by camostat mesylate or nafamostat mesylate prevents infection mediated by the TMPRSS2-dependent and cathepsin-independent pathway. nafamostat 75-94 transmembrane serine protease 2 Homo sapiens 25-32 34340553-0 2021 The TMPRSS2 Inhibitor Nafamostat Reduces SARS-CoV-2 Pulmonary Infection in Mouse Models of COVID-19. nafamostat 22-32 transmembrane serine protease 2 Homo sapiens 4-11 34100014-4 2021 Similarly, inhibition of TMPRSS2 protease activity by camostat mesylate or nafamostat mesylate prevents infection mediated by the TMPRSS2-dependent and cathepsin-independent pathway. nafamostat 75-94 transmembrane serine protease 2 Homo sapiens 130-137 34209110-6 2021 These results suggest that the proposed compounds, in addition to Camostat and Nafamostat, could be effective TMPRSS2 inhibitors for COVID-19 treatment by occupying the S1 pocket with the hallmark positively charged groups. nafamostat 79-89 transmembrane serine protease 2 Homo sapiens 110-117 35063125-6 2022 Moreover, entry of SARS-CoV-2 into BCECs could be reduced by anti-spike-, anti-angiotensin-converting enzyme 2 (ACE2)-, and anti-neuropilin-1 (NRP1)-specific antibodies or the transmembrane protease serine subtype 2 (TMPRSS2) inhibitor nafamostat. nafamostat 236-246 transmembrane serine protease 2 Homo sapiens 217-224 34075338-0 2021 Structural insights and inhibition mechanism of TMPRSS2 by experimentally known inhibitors Camostat mesylate, Nafamostat and Bromhexine hydrochloride to control SARS-coronavirus-2: A molecular modeling approach. nafamostat 110-120 transmembrane serine protease 2 Homo sapiens 48-55 34075338-5 2021 Hence, we have used a molecular dynamics (MD) simulated homology model of TMPRSS2 to study the inhibition mechanism of experimentally known inhibitors Camostat mesylate, Nafamostat and Bromhexine hydrochloride (BHH) using molecular modeling techniques. nafamostat 170-180 transmembrane serine protease 2 Homo sapiens 74-81 34075338-7 2021 Molecular docking analysis revealed that Camostat mesylate and its structural analogue Nafamostat interact strongly with residues His296 and Ser441 present in the catalytic triad of TMPRSS2, whereas BHH binds with Ala386 along with other residues. nafamostat 87-97 transmembrane serine protease 2 Homo sapiens 182-189 35215982-2 2022 Nafamostat, a potent TMPRSS2 inhibitor as well as a candidate for anti-SARS-CoV-2 drug, possesses the same acyl substructure as camostat, but is known to have a greater antiviral effect. nafamostat 0-10 transmembrane serine protease 2 Homo sapiens 21-28 35215982-3 2022 A unique aspect of the molecular binding of nafamostat has been recently reported to be the formation of a covalent bond between its acyl substructure and Ser441 in TMPRSS2. nafamostat 44-54 transmembrane serine protease 2 Homo sapiens 165-172 35215982-5 2022 In silico analysis showed that Asp435 significantly contributes to the binding of nafamostat and camostat to TMPRSS2, while Glu299 interacts strongly only with nafamostat. nafamostat 82-92 transmembrane serine protease 2 Homo sapiens 109-116 35215982-6 2022 The estimated binding affinity for each compound with TMPRSS2 was actually consistent with the higher activity of nafamostat; however, the evaluation of the newly synthesized nafamostat derivatives revealed that the predicted binding affinity did not correlate with their anti-SARS-CoV-2 activity measured by the cytopathic effect (CPE) inhibition assay. nafamostat 114-124 transmembrane serine protease 2 Homo sapiens 54-61 35215982-8 2022 These results strongly indicate that the ease of covalent bond formation with Ser441 in TMPRSS2 possibly plays a major role in the anti-SARS-CoV-2 effect of nafamostat and its derivatives. nafamostat 157-167 transmembrane serine protease 2 Homo sapiens 88-95 35294338-7 2022 The mechanism of the protease inhibitors nafamostat and camostat may extend beyond inhibition of TMPRSS2 to coagulation-induced spike cleavage. nafamostat 41-51 transmembrane serine protease 2 Homo sapiens 97-104 35072549-5 2022 Two known TMPRSS2 inhibitors, namely camostat and nafamostat, approved drugs for the treatment of pancreatitis, are under clinical trials as potential drugs against COVID-19. nafamostat 50-60 transmembrane serine protease 2 Homo sapiens 10-17 33821268-6 2021 The mechanism of the protease inhibitors nafamostat and camostat extend beyond inhibition of TMPRSS2 to coagulation-induced spike cleavage. nafamostat 41-51 transmembrane serine protease 2 Homo sapiens 93-100 33996911-1 2021 Camostat, nafamostat, and bromhexine are inhibitors of the transmembrane serine protease TMPRSS2. nafamostat 10-20 transmembrane serine protease 2 Homo sapiens 89-96 33996911-3 2021 However, while camostat and nafamostat inhibit TMPRSS2 by forming a covalent adduct, the mode of action of bromhexine remains unclear. nafamostat 28-38 transmembrane serine protease 2 Homo sapiens 47-54 33868970-10 2022 Among the drugs, the drug nafamostat may be more beneficial than the camostat in suppressing the activity of TMPRSS2. nafamostat 26-36 transmembrane serine protease 2 Homo sapiens 109-116 32532094-2 2020 We previously found that nafamostat mesylate, an existing drug used for disseminated intravascular coagulation (DIC), effectively blocked Middle East respiratory syndrome coronavirus (MERS-CoV) S protein-mediated cell fusion by targeting transmembrane serine protease 2 (TMPRSS2), and inhibited MERS-CoV infection of human lung epithelium-derived Calu-3 cells. nafamostat 25-35 transmembrane serine protease 2 Homo sapiens 238-269 32824674-6 2020 Clinical studies on TMPRSS2 inhibitors, such as camostat, nafamostat, and bromhexine, are ongoing. nafamostat 58-68 transmembrane serine protease 2 Homo sapiens 20-27 33382023-6 2020 Molecular docking score and MMGBSA Binding energy of Fisetin was better than Nafamostat, a known inhibitor of TMPRSS2. nafamostat 77-87 transmembrane serine protease 2 Homo sapiens 110-117 33505639-2 2021 Recent studies showed that two drugs, Camostat and Nafamostat, might be repurposed to treat COVID-19 by inhibiting human TMPRSS2 required for proteolytic activation of viral spike (S) glycoprotein. nafamostat 51-61 transmembrane serine protease 2 Homo sapiens 121-128 32532094-2 2020 We previously found that nafamostat mesylate, an existing drug used for disseminated intravascular coagulation (DIC), effectively blocked Middle East respiratory syndrome coronavirus (MERS-CoV) S protein-mediated cell fusion by targeting transmembrane serine protease 2 (TMPRSS2), and inhibited MERS-CoV infection of human lung epithelium-derived Calu-3 cells. nafamostat 25-35 transmembrane serine protease 2 Homo sapiens 271-278 32532094-3 2020 Here we established a quantitative fusion assay dependent on severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) S protein, angiotensin I converting enzyme 2 (ACE2) and TMPRSS2, and found that nafamostat mesylate potently inhibited the fusion while camostat mesylate was about 10-fold less active. nafamostat 202-221 transmembrane serine protease 2 Homo sapiens 178-185