Journal of Molecular Biology
Structural Characterization of Two Variants of Fibulin-1 that Differ in Nidogen Affinity
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Cited by (93)
Vertebrate extracellular matrix protein hemicentin-1 interacts physically and genetically with basement membrane protein nidogen-2
2022, Matrix BiologyCitation Excerpt :Of note, however, NID2 binds HMCN1 with an approximately 30x higher affinity than NID1. This is in striking contrast to former results obtained for fibulin-1 (FBLN1), which only binds NID1 [28–30], but not NID2 [62]. Furthermore, we identified the G2F-EGF unit of HMCN1 (which is absent in FBLN1) to be involved in NID2 binding, whereas NID1 – FBLN1 binding is mediated via the EGF-FC unit of FBLN1 (which is also present in HMCN1).
Matricellular Proteins
2021, Encyclopedia of Respiratory Medicine, Second EditionExpression and purification of recombinant fibulins in mammalian cells
2018, Methods in Cell BiologyFibulin-1 purification from human plasma using affinity chromatography on Factor H-Sepharose
2016, Protein Expression and PurificationCitation Excerpt :The mosaic nature of Fibulin-1 creates an elongated molecule as visualized by electron microscopy after rotary shadowing. Recombinant Fibulin-1 is seen to have a dumbbell shape of ∼330 Å in length [14]. From a biological perspective the Fibulins are of interest because they are constituents of the Extracellular Matrix (ECM), and consistent with this Fibulin-1 has important functions for vascular development, wound healing, elastogenesis, angiogenesis, and hemostasis [1,2,15].
Control of the basement membrane and cell migration by ADAMTS proteinases: Lessons from C. elegans genetics
2015, Matrix BiologyCitation Excerpt :Therefore, it is likely that MIG-17 does not function in recruitment of LET-2 to the gonadal surface but may function in the activation of localized LET-2 to induce directed DTC migration. Mammalian nidogen specifically binds both type IV collagen and fibulin-1 in vitro [23,24]. We therefore examined whether suppression of mig-17 mutations by mutant LET-2(gf) or FBL-1(gf) proteins depends on NID-1, the nidogen homolog in C. elegans.
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