PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33619331-0 2021 Serine 477 plays a crucial role in the interaction of the SARS-CoV-2 spike protein with the human receptor ACE2. Serine 0-6 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 69-74 33164230-10 2021 There is growing evidence that androgen-enabled expression of ACE2 receptors and the serine protease TMPRSS2, two permissive elements engaging the SARS-CoV-2 spike protein for infection, may contribute to severe COVID-19 in men. Serine 85-91 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 158-163 33741941-5 2021 We further demonstrate that alpha1AT binds and inactivates the serine protease TMPRSS2, which enzymatically primes the SARS-CoV-2 spike protein for membrane fusion. Serine 63-69 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 130-135 33706067-1 2021 While the angiotensin converting enzyme 2 (ACE2) protein is defined as the primary severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) receptor, the viral serine molecule might be mobilized by the host"s transmembrane protease serine subtype 2 (TMPRSS2) enzyme from the viral spike (S) protein and hijack the host"s N-acetyl-D-galactosamine (GalNAc) metabolism. Serine 164-170 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 285-290 33821268-5 2021 A drug-repurposing screen identified a subset of protease inhibitors that promiscuously inhibited spike cleavage by both transmembrane serine proteases as well as coagulation factors. Serine 135-141 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 98-103 33467896-4 2021 It is now known that the structural spike (S) protein of the SARS-CoV-2 undergoes proteolytic priming by the host serine proteases for entry into the host cells, and N- and O-glycosylation by the host cell enzymes during virion packaging, which enable the virus to spread. Serine 114-120 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 36-41 33467896-4 2021 It is now known that the structural spike (S) protein of the SARS-CoV-2 undergoes proteolytic priming by the host serine proteases for entry into the host cells, and N- and O-glycosylation by the host cell enzymes during virion packaging, which enable the virus to spread. Serine 114-120 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 43-44 33737214-6 2021 Spike (S) glycoprotein initiates the attachment of SARS-CoV-2 with a widely expressed cellular receptor angiotensin-converting enzyme 2 (ACE2), and subsequent S glycoprotein priming via serine protease TMPRSS2. Serine 186-192 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 0-5 33290397-2 2020 The host serine protease TMPRSS2 and cysteine proteases Cathepsin B/L can activate S, making two independent entry pathways accessible to SARS-CoV-2. Serine 9-15 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 29-30 32972339-6 2021 The priming of the spike (S) protein of the virus by proteolytic cleavage by the trans-membrane serine protease-2 (TMPRSS2) is necessary for fusion of the virus to the host cell after it binds to its receptor angiotensin converting enzyme-2 (ACE2). Serine 96-102 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 19-24 32972339-6 2021 The priming of the spike (S) protein of the virus by proteolytic cleavage by the trans-membrane serine protease-2 (TMPRSS2) is necessary for fusion of the virus to the host cell after it binds to its receptor angiotensin converting enzyme-2 (ACE2). Serine 96-102 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 26-27 33293627-6 2020 Serine proteases are known to be involved in the infection process by priming the virus spike protein. Serine 0-6 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 88-93 33239231-5 2021 First, AAT is a serine protease inhibitor (SERPIN) shown to inhibit TMPRSS-2, the host serine protease that cleaves the spike protein of SARS-CoV-2, a necessary preparatory step for the virus to bind its cell surface receptor ACE2 to gain intracellular entry. Serine 87-93 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 120-125 32638018-7 2020 Inversely, the most important S protein cleavage protease TMPRSS2 (transmembrane protease serine protease-2) in the heart exhibits an extremely lower expression than that in the lung (adjusted P < 0.0001), which may restrict entry of SARS-CoV-2 into cardiac cells. Serine 90-96 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 30-31 32741259-3 2020 SARS-CoV and SARS-CoV-2 employ the host cellular serine protease TMPRSS2 for spike (S) protein priming for viral entry into host cells. Serine 49-55 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 77-82 32741259-3 2020 SARS-CoV and SARS-CoV-2 employ the host cellular serine protease TMPRSS2 for spike (S) protein priming for viral entry into host cells. Serine 49-55 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 0-1 33278189-4 2020 The virus requires proteolytic processing of its spike protein by transmembrane protease receptor serine type 2 (TMPRSS2) to enable binding to cellular ACE2. Serine 98-104 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 49-54 33268377-7 2021 I hypothesize that several membrane-associated serine proteinases (MASPs), in synergy with or in place of TMPRSS2, contribute to activate the SARS-CoV-2 spike protein. Serine 47-53 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 153-158 33299610-7 2020 However, it appears that S protein proteolytic cleavage is dependent on (1) furin and (2) serine protease transmembrane protease serine 2 proteases acting in tandem. Serine 90-96 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 25-26 33299610-7 2020 However, it appears that S protein proteolytic cleavage is dependent on (1) furin and (2) serine protease transmembrane protease serine 2 proteases acting in tandem. Serine 129-135 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 25-26 34393265-4 2021 Here, we performed a theoretical investigation of the same by studying the binding of the molecules with SARS-COV-2 Spike protein, the complex formed by Spike and ACE2 human receptor and a human serine protease TMPRSS2 which aids in cleavage of the Spike protein to initiate the viral activation in the body. Serine 195-201 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 116-121 32589459-1 2020 PURPOSE: The spike proteins of SARS-CoV-2 interact with ACE2 or basigin/CD147 receptors, regulating human-to-human transmissions of COVID-19 together with serine protease TMPRSS2. Serine 155-161 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 13-18 34826419-2 2022 Its infection depends on the binding of spike protein to the host cell receptor angiotensin-converting enzyme 2 (ACE2), type II transmembrane serine protease (TMPRSS2) and neuropilin-1 (NRP1). Serine 142-148 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 40-45 34561887-5 2022 The viral particle incorporates the S protein, which has already undergone S1/S2 cleavage by furin, and then undergoes further cleavage at the S2" site, mediated by the type II transmembrane serine protease TMPRSS2, after binding to the receptor ACE2 to facilitate membrane fusion at the plasma membrane. Serine 191-197 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 36-37 32404436-4 2020 Expression of two mucosa-specific serine proteases, TMPRSS2 and TMPRSS4, facilitated SARS-CoV-2 spike fusogenic activity and promoted virus entry into host cells. Serine 34-40 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 96-101 34393265-4 2021 Here, we performed a theoretical investigation of the same by studying the binding of the molecules with SARS-COV-2 Spike protein, the complex formed by Spike and ACE2 human receptor and a human serine protease TMPRSS2 which aids in cleavage of the Spike protein to initiate the viral activation in the body. Serine 195-201 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 249-254 34449057-2 2021 Interestingly, identified mutations mainly occur in the spike (S) protein which interacts with the ACE2 receptor and is cleaved via serine protease TMPRSS2. Serine 132-138 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 56-61 35344983-4 2022 Attractive pharmacological targets to impede viral entry include type-II transmembrane serine proteases (TTSPs), such as TMPRSS2, whose essential role in the virus lifecycle is to cleave the viral spike protein to expose the fusion peptide for cell entry5,6. Serine 87-93 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 197-202 34336361-2 2021 Recent studies have shown that transmembrane serine protease 2 (TMPRSS2), a protease known for similar role in previous coronavirus infections, severe acute respiratory syndrome (SARS), and Middle East respiratory syndrome (MERS), is responsible for the proteolytic cleavage of the SARS-CoV-2 spike protein, enabling host cell fusion of the virus. Serine 45-51 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 293-298 34127969-3 2021 Serine proteases (SPs) including furin and TMPRSS2 cleave SARS-CoV-2 spike protein, facilitating viral entry. Serine 0-6 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 69-74 34541574-2 2021 Here, we evaluate nafamostat mesylate, a potent broad-spectrum serine protease inhibitor that blocks host protease activation of the viral spike protein. Serine 63-69 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 139-144 35104687-1 2022 BACKGROUND: The human protein transmembrane protease serine type 2 (TMPRSS2) plays a key role in SARS-CoV-2 infection, as it is required to activate the virus" spike protein, facilitating entry into target cells. Serine 53-59 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 160-165 35338216-1 2022 The cell surface serine protease Transmembrane Protease 2 (TMPRSS2) is required to cleave the spike protein of SARS-CoV-2 for viral entry into cells. Serine 17-23 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 94-99 35631327-2 2022 Binding of the severe acute respiratory syndrome coronavirus 2 spike protein (SARS-CoV-2 S protein) to angiotensin-converting enzyme 2 (ACE2), along with proteolytic digestion of the S protein by furin and transmembrane protease serine subtype 2 (TMPRSS2), provokes internalization of SARS-CoV-2 into the host cell. Serine 229-235 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 63-68 35294338-6 2022 A drug-repurposing screen identified a subset of protease inhibitors that promiscuously inhibited spike cleavage by both transmembrane serine proteases and coagulation factors. Serine 135-141 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 98-103 35170548-1 2022 Transmembrane serine proteinase 2 (TMPRSS2), which is an essential serine protease for priming spike protein of SARS-CoV-2, was found in low expression in many cancer tissue including lung cancer. Serine 14-20 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 95-100 35128036-2 2022 Because the androgen-responsive serine protease TMPRSS2 is involved in cleaving the SARS-CoV-2 spike protein allowing the virus to enter the cell, therefore, direct TMPRSS2 inhibition will inhibit virus activation and disease progression which make it an important target for drug discovery. Serine 32-38 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 95-100