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Johan Ledin

Researcher at Science for Life Laboratory

Publications -  28
Citations -  2679

Johan Ledin is an academic researcher from Science for Life Laboratory. The author has contributed to research in topics: Heparan sulfate & Zebrafish. The author has an hindex of 16, co-authored 27 publications receiving 2378 citations. Previous affiliations of Johan Ledin include Swedish University of Agricultural Sciences & Uppsala University.

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Abnormal mast cells in mice deficient in a heparin-synthesizing enzyme

TL;DR: The results indicate that one site of physiological action for heparin could be inside connective-tissue-type mast cells, where its absence results in severe defects in the secretory granules.
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High-throughput gene targeting and phenotyping in zebrafish using CRISPR/Cas9

TL;DR: A cloning-free single-guide RNA (sgRNA) synthesis, coupled with streamlined mutant identification methods utilizing fluorescent PCR and multiplexed, high-throughput sequencing is described, which shows that efficiency of CRISPR/Cas9 is sixfold more efficient than other techniques.
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Heparan Sulfate Structure in Mice with Genetically Modified Heparan Sulfate Production

TL;DR: Using a high throughput heparan sulfate (HS) isolation and characterization protocol, HS structure in several tissues from mice/mouse embryos deficient in HS biosynthesis enzymes and in mice lacking syndecan-1 are analyzed.
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Defective heparan sulfate biosynthesis and neonatal lethality in mice lacking N-deacetylase/N-sulfotransferase-1

TL;DR: It is reported that targeted gene disruption of NDST-1 in the mouse results in a structural alteration of heparan sulfate in most basement membranes as revealed by immunohistochemical staining of fetal tissue sections using antibodies raised against heparin sulfate.
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Defective N-sulfation of heparan sulfate proteoglycans limits PDGF-BB binding and pericyte recruitment in vascular development

TL;DR: It is concluded that pericyte recruitment requires HS with sufficiently extended and appropriately spaced N-sulfated domains to retain PDGF-BB and activate PDGF receptor beta (PDGFRbeta) signaling, whereas the detailed sequence of monosaccharide and sulfate residues does not appear to be important for this interaction.