L
Linda M.S. Fritze
Researcher at Massachusetts Institute of Technology
Publications - 11
Citations - 967
Linda M.S. Fritze is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Heparan sulfate & Growth factor. The author has an hindex of 11, co-authored 11 publications receiving 958 citations. Previous affiliations of Linda M.S. Fritze include Beth Israel Deaconess Medical Center.
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Journal ArticleDOI
Expression of Heparan Sulfate d-Glucosaminyl 3-O-Sulfotransferase Isoforms Reveals Novel Substrate Specificities
Jian Liu,Nicholas W. Shworak,Nicholas W. Shworak,Pierre Sinaÿ,John J. Schwartz,Lijuan Zhang,Linda M.S. Fritze,Linda M.S. Fritze,Robert D. Rosenberg,Robert D. Rosenberg +9 more
TL;DR: This research has provided evidence for a new cellular mechanism for generating a defined saccharide sequence in structurally complex HS polysaccharide using heparan sulfate d-glucosaminyl 3-O-sulfotransferases.
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Molecular Cloning and Expression of Mouse and Human cDNAs Encoding Heparan Sulfate D-Glucosaminyl 3-O-Sulfotransferase*
Nicholas W. Shworak,Nicholas W. Shworak,Jian Liu,Linda M.S. Fritze,Linda M.S. Fritze,John J. Schwartz,Lijuan Zhang,Delphine Logeart,Robert D. Rosenberg,Robert D. Rosenberg +9 more
TL;DR: The expression of wild-type mouse 3-OST as well as protein A-tagged mouse enzyme by transient transfection of COS-7 cells and the expression of both wild- type mouse and human 3-host by in vitrotranscription/translation demonstrate that the two cDNAs directly encode both HSact conversion and 3-ost activities.
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Human thrombomodulin gene is intron depleted: nucleic acid sequences of the cDNA and gene predict protein structure and suggest sites of regulatory control
TL;DR: The nucleotide sequence of the thrombomodulin cDNA suggests areas within the putative promoter domain that may be critical for regulating expression of the human endothelial cell receptor, indicates a potential signal peptide, and shows that no introns are present within the coding region.
Journal ArticleDOI
Heparin inhibition of smooth muscle cell proliferation: a cellular site of action.
Christopher F. Reilly,Christopher F. Reilly,Christopher F. Reilly,Linda M.S. Fritze,Linda M.S. Fritze,Robert D. Rosenberg +5 more
TL;DR: The data suggest that heparin is slowly internalized by SMC following binding to specific, non‐PF4 dissociable sites, and may accumulate intracellularly and block a crucial point in the proliferative machinery of SMC.
Journal ArticleDOI
Purification of Heparan Sulfate D-Glucosaminyl 3-O-Sulfotransferase
Jian Liu,Nicholas W. Shworak,Nicholas W. Shworak,Linda M.S. Fritze,Linda M.S. Fritze,Jay M. Edelberg,Jay M. Edelberg,Robert D. Rosenberg,Robert D. Rosenberg +8 more
TL;DR: The observation that purified 3-O-sulfotransferase catalyzes sulfation of HSact precursor and HSinact precursor in conjunction with a documented discordant regulation of 3-Sulfate content in HSinAct and HSact suggests that two discrete forms of the enzyme may exist.