PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29343861-3 2018 Upon changing from a non-reducing to a reducing condition, ion-current blockage events from the monomeric state dominate, consistent with the expected reduction of the two inter-chain VEGF disulfide bonds. Disulfides 189-198 vascular endothelial growth factor A Homo sapiens 184-188 24210874-3 2014 VEGF was successfully encapsulated into microcrystals derived from insect cypovirus with overexpression of protein disulfide bond isomerase. Disulfides 115-124 vascular endothelial growth factor A Homo sapiens 0-4 29299985-1 2018 The vascular endothelial growth factor (VEGF) is a homodimeric disulfide bound glycoprotein that promotes endothelial growth, accompanied by higher vascular permeability, and therefore represents an important factor for angiogenesis and vascularization. Disulfides 63-72 vascular endothelial growth factor A Homo sapiens 4-38 29299985-1 2018 The vascular endothelial growth factor (VEGF) is a homodimeric disulfide bound glycoprotein that promotes endothelial growth, accompanied by higher vascular permeability, and therefore represents an important factor for angiogenesis and vascularization. Disulfides 63-72 vascular endothelial growth factor A Homo sapiens 40-44 26989723-2 2014 VEGF is a highly conserved, disulfide-bonded dimeric glycoprotein of 34 to 45 kDa produced by several cell types including fibroblasts, neutrophils, endothelial cells, and peripheral blood mononuclear cells, particularly T lymphocytes and macrophages. Disulfides 28-37 vascular endothelial growth factor A Homo sapiens 0-4 23741766-1 2004 VEGF-A is composed of VEGF121, VEGF165, and VEGF189 isoforms, which are secreted by most cell types and are active as homodimers linked by disulfide bonds. Disulfides 139-148 vascular endothelial growth factor A Homo sapiens 0-6 23537207-3 2013 Peptide ligands specific for the VEGFA binding site on neuropilin-1 were identified by screening a library of disulfide-rich peptides derived from the thermostable, protease-resistant cyclotide kalata B1. Disulfides 110-119 vascular endothelial growth factor A Homo sapiens 33-38 23534080-1 2004 VEGF-A is composed of VEGF121, VEGF165, and VEGF189 isoforms, which are secreted by most cell types and are active as homodimers linked by disulfide bonds. Disulfides 139-148 vascular endothelial growth factor A Homo sapiens 0-6 22103127-2 2011 Branched polyethylenimine cross-linked via disulfide bonds (ssPEI) complexed with vascular endothelial growth factor (VEGF) were immobilized on electrospun polycaprolactone (PCL)/polyethylenimine (PEI) nanofibers for the local expression of VEGF angiogenic factor. Disulfides 43-52 vascular endothelial growth factor A Homo sapiens 82-116 23176598-4 2012 Disulfide-linked dimers produced by Cu(2+) oxidation of the free-thiol form of the protein demonstrated picomolar affinity for VEGF in solution, comparable to that of a D2-Fc fusion (sFLT01) and ~50-fold higher than monomeric D2, suggesting the 26 a.a. tag length between the two D2 domains permits simultaneous interaction of both faces of the VEGF homodimer. Disulfides 0-9 vascular endothelial growth factor A Homo sapiens 127-131 23176598-4 2012 Disulfide-linked dimers produced by Cu(2+) oxidation of the free-thiol form of the protein demonstrated picomolar affinity for VEGF in solution, comparable to that of a D2-Fc fusion (sFLT01) and ~50-fold higher than monomeric D2, suggesting the 26 a.a. tag length between the two D2 domains permits simultaneous interaction of both faces of the VEGF homodimer. Disulfides 0-9 vascular endothelial growth factor A Homo sapiens 345-349 20424732-0 2010 Signal sequence as a determinant in expressing disulfide-stabilized single chain antibody variable fragments (sc-dsFv) against human VEGF. Disulfides 47-56 vascular endothelial growth factor A Homo sapiens 133-137 21433411-1 2004 VEGF-A is composed of VEGF121, VEGF165, and VEGF189 isoforms, which are secreted by most cell types and are active as homodimers linked by disulfide bonds. Disulfides 139-148 vascular endothelial growth factor A Homo sapiens 0-6 20424732-7 2010 The utility of the phagemid systems was demonstrated in generating anti-VEGF sc-dsFv with VEGF-binding affinity one order of magnitude higher than the corresponding scFv, due only to the interface disulfide bond in the sc-dsFv. Disulfides 197-206 vascular endothelial growth factor A Homo sapiens 72-76 20424732-7 2010 The utility of the phagemid systems was demonstrated in generating anti-VEGF sc-dsFv with VEGF-binding affinity one order of magnitude higher than the corresponding scFv, due only to the interface disulfide bond in the sc-dsFv. Disulfides 197-206 vascular endothelial growth factor A Homo sapiens 90-94 20308796-5 2010 Disruption of kringle structures by reduction of disulfide bonds resulted in the loss of the inhibitory effect of AS on VEGF-stimulated NO production. Disulfides 49-58 vascular endothelial growth factor A Homo sapiens 120-124 20068035-0 2010 Engineering anti-vascular endothelial growth factor single chain disulfide-stabilized antibody variable fragments (sc-dsFv) with phage-displayed sc-dsFv libraries. Disulfides 65-74 vascular endothelial growth factor A Homo sapiens 17-51 20068035-6 2010 Comparison of the scFv and sc-dsFv variants selected from the phage-displayed libraries for vascular endothelial growth factor binding revealed the sequence preference differences resulting from the interdomain disulfide bond. Disulfides 211-220 vascular endothelial growth factor A Homo sapiens 92-126 19592043-1 2009 Vascular endothelial growth factor (VEGF) is a disulfide-linked dimeric glycoprotein that enhances vascular permeability, induces chemotaxis and activation of monocytes/macrophages, and promotes growth of vascular endothelial cells. Disulfides 47-56 vascular endothelial growth factor A Homo sapiens 0-34 19592043-1 2009 Vascular endothelial growth factor (VEGF) is a disulfide-linked dimeric glycoprotein that enhances vascular permeability, induces chemotaxis and activation of monocytes/macrophages, and promotes growth of vascular endothelial cells. Disulfides 47-56 vascular endothelial growth factor A Homo sapiens 36-40 16831481-2 2006 Vascular endothelial growth factor (VEGF) siRNA was conjugated to poly(ethylene glycol) (PEG) via a disulfide linkage (siRNA-PEG). Disulfides 100-109 vascular endothelial growth factor A Homo sapiens 0-34 16831481-2 2006 Vascular endothelial growth factor (VEGF) siRNA was conjugated to poly(ethylene glycol) (PEG) via a disulfide linkage (siRNA-PEG). Disulfides 100-109 vascular endothelial growth factor A Homo sapiens 36-40 19366703-4 2009 However, the mature form of VEGF-D (VEGF-D(DeltaNDeltaC)) is predominantly a non-covalent dimer even though the cysteine residues (Cys-44 and Cys-53) forming the intersubunit disulfide bridges in the other members of the VEGF family are also conserved in VEGF-D. Disulfides 175-184 vascular endothelial growth factor A Homo sapiens 28-32 15592500-2 2005 We show that secretion of vascular endothelial growth factor (VEGF), a protein with multiple disulfide bonds, was indeed impeded under hypoxia and was partially restored by artificial increase of oxidizing equivalents with diamide. Disulfides 93-102 vascular endothelial growth factor A Homo sapiens 26-60 15592500-2 2005 We show that secretion of vascular endothelial growth factor (VEGF), a protein with multiple disulfide bonds, was indeed impeded under hypoxia and was partially restored by artificial increase of oxidizing equivalents with diamide. Disulfides 93-102 vascular endothelial growth factor A Homo sapiens 62-66 12061718-1 2002 Previous NMR structural studies of the heparin-binding domain of vascular endothelial growth factor (VEGF165) revealed a novel fold comprising two subdomains, each containing two disulfide bridges and a short two-stranded antiparallel beta-sheet. Disulfides 179-188 vascular endothelial growth factor A Homo sapiens 65-99 12127077-3 2002 In this study, we determined that human VEGF(121) contains a third interchain disulfide bond between Cys116 of each monomer. Disulfides 78-87 vascular endothelial growth factor A Homo sapiens 40-44 12127077-6 2002 In fact, selective reduction of the Cys116 interchain disulfide bond yielded an unstable VEGF(121) molecule, which reoxidized quickly. Disulfides 54-63 vascular endothelial growth factor A Homo sapiens 89-93 12967471-5 2003 Transgenic mice expressing VEGF-E(NZ-7) showed a dramatic increase in angiogenesis with very few side effects (such as edema and hemorrhagic spots), suggesting strong angiogenic signaling and a potential clinical utility of VEGF-E. VEGF family members bear three loops produced via three intramolecular disulfide bonds, and cooperation between loop-1 and loop-3 is necessary for the specific binding and activation of VEGFR-2 for angiogenesis. Disulfides 303-312 vascular endothelial growth factor A Homo sapiens 27-31 12967471-5 2003 Transgenic mice expressing VEGF-E(NZ-7) showed a dramatic increase in angiogenesis with very few side effects (such as edema and hemorrhagic spots), suggesting strong angiogenic signaling and a potential clinical utility of VEGF-E. VEGF family members bear three loops produced via three intramolecular disulfide bonds, and cooperation between loop-1 and loop-3 is necessary for the specific binding and activation of VEGFR-2 for angiogenesis. Disulfides 303-312 vascular endothelial growth factor A Homo sapiens 224-228 12207021-5 2002 When assuming that the sequential order of the disulfide bridge formation is conserved between VEGF and glycoprotein alpha-subunit, the crystal structure of the mutant C61A-C104A, which deviates by a root mean square deviation of more than 2.2 A from wild-type VEGF, identifies a true folding intermediate of VEGF. Disulfides 47-56 vascular endothelial growth factor A Homo sapiens 95-99 9244387-0 1997 Disulfide structure of the heparin binding domain in vascular endothelial growth factor: characterization of posttranslational modifications in VEGF. Disulfides 0-9 vascular endothelial growth factor A Homo sapiens 53-87 10077638-7 1999 ORFV2-VEGF was found to be a disulfide-linked homodimer with a subunit of approximately 25 kDa. Disulfides 29-38 vascular endothelial growth factor A Homo sapiens 6-10 9922141-2 1998 Libraries of short disulfide-constrained peptides yielded three distinct classes of peptides that bind to the receptor-binding domain of VEGF with micromolar affinities. Disulfides 19-28 vascular endothelial growth factor A Homo sapiens 137-141 11866530-3 2002 Three classes of disulfide-constrained peptides that antagonize binding of the VEGF dimer to its receptors, KDR and Flt-1, were identified previously using phage display methods. Disulfides 17-26 vascular endothelial growth factor A Homo sapiens 79-83 11106176-8 2000 The resulting purified disulfide-linked homodimer was demonstrated to bind to VEGF-R1 and to compete with VEGF-A for binding to this receptor. Disulfides 23-32 vascular endothelial growth factor A Homo sapiens 106-112 7806514-5 1994 Cysteine residues 2 and 4 in VPF were found to be directly involved in anti-parallel interchain disulfide bonds, as in PDGF. Disulfides 96-105 vascular endothelial growth factor A Homo sapiens 29-32 8637916-3 1996 VEGF-B formed cell-surface-associated disulfide-linked homodimers and heterodimerized with VEGF when coexpressed. Disulfides 38-47 vascular endothelial growth factor A Homo sapiens 0-4 8527160-1 1995 Vascular endothelial growth factor (VEGF) is a glycoprotein consisting of two identical polypeptide chains linked by a disulfide bond. Disulfides 119-128 vascular endothelial growth factor A Homo sapiens 0-34 8527160-1 1995 Vascular endothelial growth factor (VEGF) is a glycoprotein consisting of two identical polypeptide chains linked by a disulfide bond. Disulfides 119-128 vascular endothelial growth factor A Homo sapiens 36-40 8841458-1 1996 Vascular permeability factor, also known as vascular endothelial growth factor (VPF/VEGF), is a disulfide-linked dimeric glycoprotein of about 40 kDa that enhances vascular permeability, induces chemotaxis and activation of monocytes/macrophages, and promotes growth of vascular endothelial cells. Disulfides 96-105 vascular endothelial growth factor A Homo sapiens 0-28 8841458-1 1996 Vascular permeability factor, also known as vascular endothelial growth factor (VPF/VEGF), is a disulfide-linked dimeric glycoprotein of about 40 kDa that enhances vascular permeability, induces chemotaxis and activation of monocytes/macrophages, and promotes growth of vascular endothelial cells. Disulfides 96-105 vascular endothelial growth factor A Homo sapiens 44-78 8841458-1 1996 Vascular permeability factor, also known as vascular endothelial growth factor (VPF/VEGF), is a disulfide-linked dimeric glycoprotein of about 40 kDa that enhances vascular permeability, induces chemotaxis and activation of monocytes/macrophages, and promotes growth of vascular endothelial cells. Disulfides 96-105 vascular endothelial growth factor A Homo sapiens 80-83 8841458-1 1996 Vascular permeability factor, also known as vascular endothelial growth factor (VPF/VEGF), is a disulfide-linked dimeric glycoprotein of about 40 kDa that enhances vascular permeability, induces chemotaxis and activation of monocytes/macrophages, and promotes growth of vascular endothelial cells. Disulfides 96-105 vascular endothelial growth factor A Homo sapiens 84-88 3134521-9 1988 Treatment with dithiothreitol inhibited VPF activity, indicating the presence of at least one essential disulfide bond in this molecule. Disulfides 104-113 vascular endothelial growth factor A Homo sapiens 40-43 8264155-1 1993 Vascular permeability factor, or vascular endothelial growth factor (VPF/VEGF) is a disulfide-linked dimeric glycoprotein of about 40 kD that promotes fluid and protein leakage from blood vessels. Disulfides 84-93 vascular endothelial growth factor A Homo sapiens 0-67 8264155-1 1993 Vascular permeability factor, or vascular endothelial growth factor (VPF/VEGF) is a disulfide-linked dimeric glycoprotein of about 40 kD that promotes fluid and protein leakage from blood vessels. Disulfides 84-93 vascular endothelial growth factor A Homo sapiens 69-72 8264155-1 1993 Vascular permeability factor, or vascular endothelial growth factor (VPF/VEGF) is a disulfide-linked dimeric glycoprotein of about 40 kD that promotes fluid and protein leakage from blood vessels. Disulfides 84-93 vascular endothelial growth factor A Homo sapiens 73-77 1719968-1 1991 Vascular permeability factor (VPF) is an approximately 40-kDa disulfide-linked dimeric glycoprotein that is active in increasing blood vessel permeability, endothelial cell growth and angiogenesis. Disulfides 62-71 vascular endothelial growth factor A Homo sapiens 0-28 1719968-1 1991 Vascular permeability factor (VPF) is an approximately 40-kDa disulfide-linked dimeric glycoprotein that is active in increasing blood vessel permeability, endothelial cell growth and angiogenesis. Disulfides 62-71 vascular endothelial growth factor A Homo sapiens 30-33 2584205-4 1989 hVPF was purified from serum-free conditioned medium of the human histiocytic lymphoma cell line U937 as a disulfide-linked dimeric 40-kDa protein that promoted dermal blood vessel leakage in guinea pigs at a dose of 20 ng (3 x 10(-9) M) and promoted in vitro endothelial cell growth at concentrations as low as 50 PM. Disulfides 107-116 vascular endothelial growth factor A Homo sapiens 0-4