PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33357843-3 2021 Several biochemical studies show strong binding of heparin and heparin-like molecules to the Spike protein, which resulted in inhibition of viral infection to cells. Heparin 51-58 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 93-98 33915212-8 2021 Exploring further, our in-silico analysis indicated that the heparin interacts with post-translational glycoconjugates present on spike proteins. Heparin 61-68 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 130-135 33915212-10 2021 Heparin-binding to the open conformation of spike structurally supports the state and may aid ACE2 binding as reported with cell surface-bound heparan sulfate. Heparin 0-7 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 44-49 33915212-11 2021 We also studied spike protein mutant variants" heparin interactions for possible resistance. Heparin 47-54 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 16-21 33789211-3 2021 SARS-CoV-2 Spike S1 protein receptor binding domain (SARS-CoV-2 S1 RBD) binds to heparin and heparin binding proteins. Heparin 81-88 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 11-16 33789211-3 2021 SARS-CoV-2 Spike S1 protein receptor binding domain (SARS-CoV-2 S1 RBD) binds to heparin and heparin binding proteins. Heparin 93-100 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 11-16 33968948-8 2021 Moreover, heparin may present anti-SARS-CoV-2 potential once it can impact viral infectivity and alter SARS-CoV-2 Spike protein architecture. Heparin 10-17 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 114-119 33357843-3 2021 Several biochemical studies show strong binding of heparin and heparin-like molecules to the Spike protein, which resulted in inhibition of viral infection to cells. Heparin 63-70 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 93-98 33968333-7 2021 Docking studies using GlycoTorch Vina and subsequent MD simulations of the spike trimer in the presence of dodecasaccharides of the GAGs heparin and heparan sulfate supported this possibility. Heparin 137-144 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 75-80 33368089-0 2020 Heparin Inhibits Cellular Invasion by SARS-CoV-2: Structural Dependence of the Interaction of the Spike S1 Receptor-Binding Domain with Heparin. Heparin 0-7 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 98-103 33368089-0 2020 Heparin Inhibits Cellular Invasion by SARS-CoV-2: Structural Dependence of the Interaction of the Spike S1 Receptor-Binding Domain with Heparin. Heparin 136-143 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 98-103 33368089-5 2020 Surface plasmon resonance and circular dichroism spectroscopy demonstrate that heparin and enoxaparin, a low-molecular-weight heparin which is a clinical anticoagulant, bind and induce a conformational change in the spike (S1) protein receptor-binding domain (S1 RBD) of SARS-CoV-2. Heparin 79-86 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 216-221 33368089-5 2020 Surface plasmon resonance and circular dichroism spectroscopy demonstrate that heparin and enoxaparin, a low-molecular-weight heparin which is a clinical anticoagulant, bind and induce a conformational change in the spike (S1) protein receptor-binding domain (S1 RBD) of SARS-CoV-2. Heparin 126-133 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 216-221 32970989-3 2020 Both ACE2 and heparin can bind independently to spike protein in vitro, and a ternary complex can be generated using heparin as a scaffold. Heparin 14-21 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 48-53 32970989-4 2020 Electron micrographs of spike protein suggests that heparin enhances the open conformation of the RBD that binds ACE2. Heparin 52-59 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 24-29 32970989-6 2020 Unfractionated heparin, non-anticoagulant heparin, heparin lyases, and lung heparan sulfate potently block spike protein binding and/or infection by pseudotyped virus and authentic SARS-CoV-2 virus. Heparin 15-22 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 107-112 32970989-6 2020 Unfractionated heparin, non-anticoagulant heparin, heparin lyases, and lung heparan sulfate potently block spike protein binding and/or infection by pseudotyped virus and authentic SARS-CoV-2 virus. Heparin 42-49 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 107-112 32970989-6 2020 Unfractionated heparin, non-anticoagulant heparin, heparin lyases, and lung heparan sulfate potently block spike protein binding and/or infection by pseudotyped virus and authentic SARS-CoV-2 virus. Heparin 42-49 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 107-112 34289657-8 2022 Moreover, SARS-CoV-2 spike proteins directly block complement factor H from binding to heparin, which may lead to complement dysregulation on the cell surface. Heparin 87-94 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 21-26 33298900-3 2020 We show that heparin/HS binds to Spike directly, and facilitates the attachment of Spike-bearing viral particles to the cell surface to promote viral entry. Heparin 13-20 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 33-38 33298900-3 2020 We show that heparin/HS binds to Spike directly, and facilitates the attachment of Spike-bearing viral particles to the cell surface to promote viral entry. Heparin 13-20 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 83-88 34929169-4 2022 Biochemical experiments corroborated the simulation results, showing that heparin inhibits the furin-mediated cleavage of spike by binding to the S1/S2 site. Heparin 74-81 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 122-127 34929169-6 2022 In simulations of the closed spike homotrimer, heparin binds the RBD and the N-terminal domain of two adjacent spike subunits and hinders opening. Heparin 47-54 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 29-34 34929169-6 2022 In simulations of the closed spike homotrimer, heparin binds the RBD and the N-terminal domain of two adjacent spike subunits and hinders opening. Heparin 47-54 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 111-116 34929169-7 2022 In simulations of open spike conformations, heparin induces stabilization of the hinge region and a change in RBD motion. Heparin 44-51 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 23-28 34929169-8 2022 Taken together, our results indicate that heparin can inhibit SARS-CoV-2 infection by three mechanisms: by allosterically hindering binding to the host cell receptor, by directly competing with binding to host heparan sulfate proteoglycan co-receptors, and by preventing spike cleavage by furin. Heparin 42-49 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 271-276 32699853-3 2020 In vitro, binding of ACE2 and heparin to spike protein ectodomains occurs independently and a ternary complex can be generated using heparin as a template. Heparin 30-37 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 41-46 32699853-3 2020 In vitro, binding of ACE2 and heparin to spike protein ectodomains occurs independently and a ternary complex can be generated using heparin as a template. Heparin 133-140 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 41-46 32699853-5 2020 Unfractionated heparin, non-anticoagulant heparin, treatment with heparin lyases, and purified lung heparan sulfate potently block spike protein binding and infection by spike protein-pseudotyped virus and SARS-CoV-2 virus. Heparin 15-22 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 131-136 32699853-5 2020 Unfractionated heparin, non-anticoagulant heparin, treatment with heparin lyases, and purified lung heparan sulfate potently block spike protein binding and infection by spike protein-pseudotyped virus and SARS-CoV-2 virus. Heparin 15-22 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 170-175 32699853-5 2020 Unfractionated heparin, non-anticoagulant heparin, treatment with heparin lyases, and purified lung heparan sulfate potently block spike protein binding and infection by spike protein-pseudotyped virus and SARS-CoV-2 virus. Heparin 42-49 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 131-136 32699853-5 2020 Unfractionated heparin, non-anticoagulant heparin, treatment with heparin lyases, and purified lung heparan sulfate potently block spike protein binding and infection by spike protein-pseudotyped virus and SARS-CoV-2 virus. Heparin 42-49 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 170-175 32699853-5 2020 Unfractionated heparin, non-anticoagulant heparin, treatment with heparin lyases, and purified lung heparan sulfate potently block spike protein binding and infection by spike protein-pseudotyped virus and SARS-CoV-2 virus. Heparin 42-49 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 131-136 32699853-5 2020 Unfractionated heparin, non-anticoagulant heparin, treatment with heparin lyases, and purified lung heparan sulfate potently block spike protein binding and infection by spike protein-pseudotyped virus and SARS-CoV-2 virus. Heparin 42-49 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 170-175 34743814-3 2021 Heparan sulfate (HS)/heparin, a key factor in coagulation process, was found to bind SARS-CoV-2 S protein with high affinity. Heparin 21-28 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 96-97 34940684-7 2021 RS inhibition of the interaction of heparin, a highly sulfated HS, with the SARS-CoV-2 spike protein (from wild type and different mutant variants) was studied using surface plasmon resonance (SPR). Heparin 36-43 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 87-92 34537241-6 2021 The dissociation constant (KD) values obtained by surface plasmon resonance (SPR) of the wild type SARS-CoV-2 spike (S)-protein receptor binding domain (RBD) and N501Y mutant RBD in interactions with the heparin-immobilized sensor chip were 94 and 1.8 x 103 nM, respectively. Heparin 204-211 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 110-115 34235261-4 2021 Surface plasmon resonance showed the SARS-CoV-2 spike protein binds with a much higher affinity to heparin (K D = 55 nM) compared to the RBD (K D = 1 muM) alone. Heparin 99-106 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 48-53 35194375-2 2022 Several studies have indicated that heparin and its derivatives interact to SARS-CoV-2 S-RBD and inhibits the binding of ACE2 which blocks the viral invasion. Heparin 36-43 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 87-88 34200372-0 2021 ACE2-Independent Interaction of SARS-CoV-2 Spike Protein with Human Epithelial Cells Is Inhibited by Unfractionated Heparin. Heparin 116-123 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 43-48 34200372-7 2021 As the spike protein has previously been shown to bind heparin, a soluble glycosaminoglycan, we tested the effects of various heparins on ACE2-independent spike protein interaction with cells. Heparin 55-62 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 7-12 34200372-8 2021 Unfractionated heparin inhibited spike protein interaction with an IC50 value of <0.05 U/mL, whereas two low-molecular-weight heparins were less effective. Heparin 15-22 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 33-38 34200372-9 2021 A mutant form of the spike protein, lacking the arginine-rich putative furin cleavage site, interacted only weakly with cells and had a lower affinity for unfractionated and low-molecular-weight heparin than the wild-type spike protein. Heparin 195-202 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 21-26 35169535-1 2022 The heparin polysaccharide nanoparticles block the interaction between heparan sulfate/S protein and inhibit the infection of both wild-type SARS-CoV-2 pseudovirus and the mutated strains through pulmonary delivery.Image 1. Heparin 4-11 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 87-88 35215371-9 2022 Both PPS and MPS showed stronger inhibition than heparin on the S-protein RBD or spike pseudotyped lentiviral particles binding to immobilized heparin. Heparin 49-56 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 81-86 35215371-9 2022 Both PPS and MPS showed stronger inhibition than heparin on the S-protein RBD or spike pseudotyped lentiviral particles binding to immobilized heparin. Heparin 143-150 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 81-86 35060381-0 2022 Structural Insights into the Cofactor Role of Heparin/Heparan Sulfate in Binding between the SARS-CoV-2 Spike Protein and Host Angiotensin-Converting Enzyme II. Heparin 46-53 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 104-109 35060381-1 2022 The viral entry process of the novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) requires heparin and heparan sulfates from the cell surface, functioning as a cofactor for human angiotensin-converting enzyme 2 (ACE2) for recognizing the receptor-binding domain (RBD) of the spike (S) protein on the surface of the virion. Heparin 107-114 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 291-296