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Covalent dimerization of vascular permeability factor/vascular endothelial growth factor is essential for its biological activity. Evidence from Cys to Ser mutations

https://doi.org/10.1016/s0021-9258(20)30073-9
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32/32 checkable references clean · checked 2026-07-23

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

5 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.

The 32 checked references that resolve
resolves10.1126/science.6823562
Tumor Cells Secrete a Vascular Permeability Factor That Promotes Accumulation of Ascites Fluid
resolves10.1126/science.2479987
Vascular Permeability Factor, an Endothelial Cell Mitogen Related to PDGF
resolves10.1126/science.2479986
Vascular Endothelial Growth Factor Is a Secreted Angiogenic Mitogen
resolves10.1084/jem.172.6.1535
Vascular permeability factor: a tumor-derived polypeptide that induces endothelial cell and monocyte procoagulant activity, and promotes monocyte migration.
resolves10.1016/0006-291X(91)91276-I
Vascular endothelial growth factor (VEGF) induces plasminogen activators and plasminogen activator inhibitor-1 in microvascular endothelial cells
resolves10.1002/jcp.1041530317
Vascular endothelial growth factor induces interstitial collagenase expression in human endothelial cells
resolves10.1182/blood.V81.10.2767.bloodjournal81102767
Characterization of vascular permeability factor/vascular endothelial growth factor receptors on mononuclear phagocytes
resolves10.1016/0006-291X(91)91752-X
Glycosylation is essential for efficient secretion but not for permeability-enhancing activity of vascular permeability factor (vascular endothelial growth factor)
resolves10.1210/mend-5-12-1806
The Vascular Endothelial Growth Factor Family: Identification of a Fourth Molecular Species and Characterization of Alternative Splicing of RNA
resolves10.1126/science.1312256
The <i>fms</i> -Like Tyrosine Kinase, a Receptor for Vascular Endothelial Growth Factor
resolves10.1016/0092-8674(93)90573-9
High affinity VEGF binding and developmental expression suggest Flk-1 as a major regulator of vasculogenesis and angiogenesis
resolves10.1091/mbc.3.2.211
Vascular permeability factor (vascular endothelial growth factor) gene is expressed differentially in normal tissues, macrophages, and tumors.
resolves10.1172/JCI116450
Patterns of expression of vascular endothelial growth factor (VEGF) and VEGF receptors in mice suggest a role in hormonally regulated angiogenesis.
resolves10.1006/bbrc.1993.1671
Synthesis and Secretion of Vascular Permeability Factor/Vascular Endothelial Growth Factor by Human Retinal Pigment Epithelial Cells
resolves10.1242/dev.114.2.521
Expression of vascular endothelial growth factor during embryonic angiogenesis and endothelial cell differentiation
resolves10.1084/jem.176.5.1375
Expression of vascular permeability factor (vascular endothelial growth factor) by epidermal keratinocytes during wound healing.
resolves10.1006/bbrc.1993.1955
Significance of Vascular Endothelial Growth Factor/Vascular Permeability Factor for Solid Tumor Growth, and Its Inhibition by the Antibody
resolves10.1038/362841a0
Inhibition of vascular endothelial growth factor-induced angiogenesis suppresses tumour growth in vivo
resolves10.1038/367576a0
Glioblastoma growth inhibited in vivo by a dominant-negative Flk-1 mutant
resolves10.1016/S0021-9258(19)49905-5
Assignment of interchain disulfide bonds in platelet-derived growth factor (PDGF) and evidence for agonist activity of monomeric PDGF.
resolves10.1002/j.1460-2075.1992.tb05485.x
Crystal structure of human platelet‐derived growth factor BB.
resolves10.1016/S0021-9258(17)32723-0
Formation of mitogenically active PDGF-B dimer does not require interchain disulfide bonds.
resolves10.1038/354411a0
New protein fold revealed by a 2.3-Å resolution crystal structure of nerve growth factor
resolves10.1038/358430a0
An unusual feature revealed by the crystal structure at 2.2 Å resolution of human transforming growth fact or-β2
resolves10.1016/0092-8674(93)90127-C
A structural superfamily of growth factors containing a cystine knot motif
resolves10.1126/science.3035718
The Role of Individual Cysteine Residues in the Structure and Function of the v- <i>sis</i> Gene Product
resolves10.1016/0003-2697(92)90280-K
Site-directed mutagenesis of virtually any plasmid by eliminating a unique site
resolves10.1002/jcb.240540107
Differential expression of the two VEGF receptors flt and KDR in placenta and vascular endothelial cells
resolves10.3181/00379727-133-34695
Simple Method for Quantitation of Enhanced Vascular Permeability
resolves10.1172/JCI107470
Culture of Human Endothelial Cells Derived from Umbilical Veins. IDENTIFICATION BY MORPHOLOGIC AND IMMUNOLOGIC CRITERIA
resolves10.1016/0092-8674(94)90381-6
Dual mode of signal transduction by externally added acidic fibroblast growth factor
resolves10.1073/pnas.90.6.2165
Schwannoma-derived growth factor must be transported into the nucleus to exert its mitogenic activity.
The 5 references without a DOI — listed, not checked
no DOI — not checked10.1016/S0021-9258(20)30073-9_bib27
no DOI — not checked10.1016/S0021-9258(20)30073-9_bib28
no DOI — not checked10.1016/S0021-9258(20)30073-9_bib30
no DOI — not checked10.1016/S0021-9258(20)30073-9_bib31
no DOI — not checked10.1016/S0021-9258(20)30073-9_bib37
What this badge says. CiteStamped means the CHECKABLE references of this work were clean at the dated check: each resolved to a known work in a public registry, and none carried a retraction notice at that time. It says nothing about the quality, findings, or importance of the work itself, and nothing about references deposited without a DOI.

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