Cited by 82Proteoglycans and glycosaminoglycans researchBlood Coagulation and Thrombosis MechanismsPlatelet Disorders and Treatments

The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.

Mice deficient in heparan sulfate 3-O-sulfotransferase-1: Normal hemostasis with unexpected perinatal phenotypes

Shworak, Nicholas W., HajMohammadi, Sassan, de Agostini, Ariane I., Rosenberg, Robert D.·2002·Glycoconjugate Journal

DOI 10.1023/a:1025377206600

Open this paper in CoChat — free account

Abstract

Heparan sulfate that contains antithrombin binding sites is designated as anticoagulant heparan sulfate (HS(act)) since, in vitro, it dramatically enhances the neutralization of coagulation proteases by antithrombin. Endothelial cell production of HS(act) is controlled by the Hs3st1 gene, which encodes the rate limiting enzyme-heparan sulfate 3-O-sulfotransferase-1 (Hs3st1). It has long been proposed that levels of endothelial HS(act) may tightly regulate hemostatic tone. This potential in vivo role of HS(act) was assessed by generating Hs3st1(-/-) knockout mice. Hs3st1(-/-) and Hs3st1(+/+) mice were evaluated with a variety of methods, capable of detecting altered hemostatic tone. However, both genotypes were indistinguishable. Instead, Hs3st1(-/-) mice exhibited lethality on a specific genetic background and also showed intrauterine growth retardation. Neither phenotypes result from a gross coagulopathy. So although this enzyme produces the majority of tissue HS(act), Hs3st1(-/-) mice do not show an obvious procoagulant phenotype. These results suggest that the bulk of HS(act) is not essential for normal hemostasis and that hemostatic tone is not tightly regulated by total levels of HS(act). Moreover, the unanticipated non-thrombotic phenotypes suggest structure(s) derived from this enzyme might serve additional/alternative biologic roles.

Integrity signals

Registry

Crossref · 10.1023/a:1025377206600

Cites

54 of 54 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Increased Frequency of Genetic Thrombophilia in Women with Complications of Pregnancy
Kupferminc, M. J., Eldor, A., Steinman, N., Many, A., Bar-Am, A., Jaffa, A. J., Fait, G., & Lessing, J. B. (1999) · New England Journal of Medicine · doi:10.1056/nejm199901073400102 · Cited by 977
Increased frequency of genetic thrombophilia in women with complications of pregnancy
(1999) · Transfusion Medicine Reviews · doi:10.1016/s0887-7963(99)80075-3 · Cited by 834
Structure-activity relationship in heparin: A synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity
Choay, J., Petitou, M., Lormeau, J. C., Sînaÿ, P., Casu, B., & Gatti, G. (1983) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(83)90550-8 · Cited by 641
Targeted disruption of cd39/ATP diphosphohydrolase results in disordered hemostasis and thromboregulation
Enjyoji, K., Sévigny, J., Lin, Y., Frenette, P. S., Christie, P. D., Esch, J. S. A., Imai, M., Edelberg, J. M., Rayburn, H., Lech, M., et al. (1999) · Nature Medicine · doi:10.1038/12447 · Cited by 565
Self-citation
Anticoagulant Action of Heparin
Damus, P. S., HICKS, M., & ROSENBERG, R. D. (1973) · Nature · doi:10.1038/246355a0 · Cited by 550
Self-citation
Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin.
Lindahl, U., Bäckström, G., Thunberg, L., & Leder, I. G. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.11.6551 · Cited by 498
Cloned bovine aortic endothelial cells synthesize anticoagulantly active heparan sulfate proteoglycan.
Marcum, J. A., Atha, D. H., Fritze, L. M. S., Nawroth, P. P., Stern, D., & ROSENBERG, R. D. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38421-1 · Cited by 336
Self-citation
Acceleration of thrombin-antithrombin complex formation in rat hindquarters via heparinlike molecules bound to the endothelium.
Marcum, J. A., McKenney, J. B., & ROSENBERG, R. D. (1984) · Journal of Clinical Investigation · doi:10.1172/jci111429 · Cited by 327
Self-citation
Correlation between structure and function of heparin
Rosenberg, R. D., & Lam, L. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.3.1218 · Cited by 281
Self-citation
Contribution of monosaccharide residues in heparin binding to antithrombin III
Atha, D. H., Lormeau, J. C., Petitou, M., ROSENBERG, R. D., & Choay, J. (1985) · Biochemistry · doi:10.1021/bi00344a063 · Cited by 256
Self-citation

Show all 52 references

Research works printed but not linked: 2

Marcum JA, Rosenberg RD, The biochemistry, cell biology, and pathophysiology of anticoagulantly active heparin-like molecules of the vessel wall. In Heparin, Chemical and Biological Properties: Clinical Applications, edited by Lane DA, Lindahl U (London, Edward Arnold, 1999), pp. 275–94.
de Agostini AI, Watkins SC, Slater HS, Youssoufian H, Rosenberg RD, Localization of anticoagulantly active heparan sulfate proteoglycans in vascular endothelium: Antithrombin binding on cultured endothelial cells and perfused rat aorta, Journal of Cell Biology 111, 1293–304 (1990). · DOI

Biological roles of glycans
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
“As an example, null alleles preventing the synthesis of the core glycosaminoglycan backbone of heparan sulfate causes embryonic lethality (421) (422) , but the prevention of proper sulfation of this backbone can give living mice with specific defects (422) (423) (424) (425) (426) (427) .”
Background
Heparan sulphate proteoglycans fine-tune mammalian physiology
Bishop, J. R., Schuksz, M., & Esko, J. D. (2007) · Nature · doi:10.1038/nature05817 · Cited by 1,631
Heparan Sulfate ProteoglycansPreprint
Sarrazin, S., Lamanna, W. C., & Esko, J. D. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004952 · Cited by 1,610
Glycosaminoglycans and their proteoglycans: host‐associated molecular patterns for initiation and modulation of inflammation
Taylor, K. R., & Gallo, R. L. (2006) · The FASEB Journal · doi:10.1096/fj.05-4682rev · Cited by 639
Heparan Sulfate: A Complex Polymer Charged with Biological Activity
Whitelock, J. M., & Iozzo, R. V. (2005) · Chemical Reviews · doi:10.1021/cr010213m · Cited by 419
Spatial and temporal dynamics of the endothelium
Aird, W. C. (2005) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2005.01328.x · Cited by 361
Blood Coagulation: Hemostasis and Thrombin Regulation
Tanaka, K. A., Key, N. S., & Levy, J. H. (2009) · Anesthesia & Analgesia · doi:10.1213/ane.0b013e31819bcc9c · Cited by 357
The Molecular Diversity of Glycosaminoglycans Shapes Animal Development
Bülow, H. E., & Hobert, O. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010605.093433 · Cited by 358
Heparan Sulfate: Biosynthesis, Structure, and Function
Li, J.-P., & Kusche‐Gullberg, M. (2016) · International review of cytology · doi:10.1016/bs.ircmb.2016.02.009 · Cited by 315
Salivary gland branching morphogenesis
Patel, V. N., Rebustini, I. T., & Hoffman, M. P. (2006) · Differentiation · doi:10.1111/j.1432-0436.2006.00088.x · Cited by 291
Differential Sulfations and Epimerization Define Heparan Sulfate Specificity in Nervous System Development
Bülow, H. E., & Hobert, O. (2004) · Neuron · doi:10.1016/s0896-6273(04)00084-4 · Cited by 262
Maintenance of chondroitin sulfation balance by chondroitin-4-sulfotransferase 1 is required for chondrocyte development and growth factor signaling during cartilage morphogenesis
Klüppel, M., Wight, T. N., Chan, C. K., Hinek, A., & Wrana, J. L. (2005) · Development · doi:10.1242/dev.01948 · Cited by 205
The heparanome—The enigma of encoding and decoding heparan sulfate sulfation
Lamanna, W. C., Kalus, I., Padva, M., Baldwin, R. J., Merry, C. L. R., & Dierks, T. (2007) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2007.01.022 · Cited by 187
The potential role of heparin in assisted conception
Nelson, S. M., & Greer, I. A. (2008) · Human Reproduction Update · doi:10.1093/humupd/dmn031 · Cited by 162
Heparan sulfate proteoglycans: a sugar code for vertebrate development?
Poulain, F. E., & Yost, H. J. (2015) · Development · doi:10.1242/dev.098178 · Cited by 139
Intracellular proteoglycans
Kolset, S. O., Prydz, K., & Pejler, G. (2004) · Biochemical Journal · doi:10.1042/bj20031230 · Cited by 136
Reduced mucin sulfonation and impaired intestinal barrier function in the hyposulfataemic NaS1 null mouse
Dawson, P. A., Huxley, S., Gardiner, B., Tran, T., McAuley, J., Grimmond, S. M., McGuckin, M. A., & Markovich, D. (2009) · Gut · doi:10.1136/gut.2007.147595 · Cited by 128
When sugars guide axons: insights from heparan sulphate proteoglycan mutants
Lee, J.-S., & Chien, C.-B. (2004) · Nature Reviews Genetics · doi:10.1038/nrg1490 · Cited by 119
Multifunctionality of extracellular and cell surface heparan sulfate proteoglycans
Kirn‐Safran, C. B., Farach‐Carson, M. C., & Carson, D. D. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0096-1 · Cited by 105
Fetomaternal cross talk in the placental vascular bed: control of coagulation by trophoblast cells
Sood, R., Kalloway, S., Mast, A. E., Hillard, C. J., & Weiler-Guettler, H. (2005) · Blood · doi:10.1182/blood-2005-10-4111 · Cited by 100
Gene Trap Disruption of the Mouse Heparan Sulfate 6- O -Endosulfatase Gene, Sulf2
Lum, D. H., Tan, J., Rosen, S. D., & Werb, Z. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01279-06 · Cited by 97
The importance of heparan sulfate in herpesvirus infection
O'Donnell, C. D., & Shukla, D. (2008) · Virologica Sinica · doi:10.1007/s12250-008-2992-1 · Cited by 93
Differential involvement of the extracellular 6‐O‐endosulfatases Sulf1 and Sulf2 in brain development and neuronal and behavioural plasticity
Kalus, I., Salmen, B., Viebahn, C., FIGURA, K. V., Schmitz, D., D’Hooge, R., & Dierks, T. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00558.x · Cited by 87
Heparin Biosynthesis
Carlsson, P., & Kjellén, L. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-23056-1_2 · Cited by 70
Role of Glycosaminoglycans in Infectious Disease
Jinno, A., & Park, P. W. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-1714-3_45 · Cited by 65
Heparan sulfate in the regulation of neural differentiation and glioma development
Xiong, A., Kundu, S., & Forsberg‐Nilsson, K. (2014) · FEBS Journal · doi:10.1111/febs.13097 · Cited by 64
Combinatorial expression patterns of heparan sulfate sulfotransferases in zebrafish: I. The 3‐O‐sulfotransferase family
Cadwallader, A. B., & Yost, H. J. (2006) · Developmental Dynamics · doi:10.1002/dvdy.20991 · Cited by 64
Anticoagulant Heparan Sulfate
Shworak, N. W., Kobayashi, T., de Agostini, A. I., & Smits, N. C. (2010) · Progress in molecular biology and translational science · doi:10.1016/s1877-1173(10)93008-1 · Cited by 60
Self-citation
Impairment of glycosaminoglycan synthesis in mucopolysaccharidosis type IIIA cells by using siRNA: a potential therapeutic approach for Sanfilippo disease
Dziedzic, D., Węgrzyn, G., & Jakóbkiewicz‐Banecka, J. (2009) · European Journal of Human Genetics · doi:10.1038/ejhg.2009.144 · Cited by 53
Heparan sulfate proteoglycans: Coordinators of multiple signaling pathways during chondrogenesis
Kirn‐Safran, C. B., Gomes, R. R., Brown, A. J., & Carson, D. D. (2004) · Birth Defects Research Part C Embryo Today Reviews · doi:10.1002/bdrc.20005 · Cited by 51
Distinct 3-O-Sulfated Heparan Sulfate Modification Patterns Are Required forkal-1−Dependent Neurite Branching in a Context-Dependent Manner inCaenorhabditis elegans
Tecle, E., Díaz-Balzac, C. A., & Bülow, H. E. (2013) · G3 Genes Genomes Genetics · doi:10.1534/g3.112.005199 · Cited by 48
Strategies for drug discovery by targeting sulfation pathways
Hemmerich, S., Verdugo, D. E., & Rath, V. L. (2004) · Drug Discovery Today · doi:10.1016/s1359-6446(04)03261-1 · Cited by 45
Distinctive regulation of contact activation by antithrombin and C1-inhibitor on activated platelets and material surfaces
Bäck, J., Lang, M. H., Elgue, G., Kalbitz, M., Sánchez, J., Ekdahl, K. N., & Nilsson, B. (2009) · Biomaterials · doi:10.1016/j.biomaterials.2009.07.052 · Cited by 38
Heparan Sulfates in the Lung: Structure, Diversity, and Role in Pulmonary Emphysema
Smits, N. C., Shworak, N. W., Dekhuijzen, P. N. R., & Kuppevelt, T. H. V. (2010) · The Anatomical Record · doi:10.1002/ar.20895 · Cited by 36
Self-citation
Bioengineered Chinese Hamster Ovary Cells with Golgi-targeted 3-O-Sulfotransferase-1 Biosynthesize Heparan Sulfate with an Antithrombin-binding Site
Datta, P., Li, G., Yang, B., Zhao, X., Baik, J. Y., Gemmill, T. R., Sharfstein, S. T., & Linhardt, R. J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.519033 · Cited by 35
Effect of dalteparin sodium administration on IVF outcome in non-thrombophilic young women: a pilot study
Noci, I., Milanini, M. N., Ruggiero, M. R., Papini, F., Fuzzi, B., & Artini, P. G. (2011) · Reproductive BioMedicine Online · doi:10.1016/j.rbmo.2011.03.016 · Cited by 34
Epigenetic Regulation of the Biosynthesis & Enzymatic Modification of Heparan Sulfate Proteoglycans: Implications for Tumorigenesis and Cancer Biomarkers
Hull, E. E., Montgomery, M. R., & Leyva, K. J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071361 · Cited by 30
Hs2st mediated kidney mesenchyme induction regulates early ureteric bud branching
Shah, M. M., Sakurai, H., Sweeney, D. E., Gallegos, T. F., Bush, K. T., Esko, J. D., & Nigám, S. K. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2009.12.033 · Cited by 29
Assays and reference materials for current and future applications of heparins
Mulloy, B., Hogwood, J., & Gray, E. (2010) · Biologicals · doi:10.1016/j.biologicals.2010.02.010 · Cited by 27
Podocyte-specific deletion of NDST1, a key enzyme in the sulfation of heparan sulfate glycosaminoglycans, leads to abnormalities in podocyte organization in vivo
Sugar, T., Wassenhove-McCarthy, D. J., Esko, J. D., Kuppevelt, T. H. V., Holzman, L. B., & McCarthy, K. J. (2013) · Kidney International · doi:10.1038/ki.2013.281 · Cited by 27
Analysis of axon guidance defects at the optic chiasm in heparan sulphate sulphotransferase compound mutant mice
Conway, C. D., Price, D. J., Pratt, T., & Mason, J. O. (2011) · Journal of Anatomy · doi:10.1111/j.1469-7580.2011.01432.x · Cited by 24
A synthetic heparan sulfate oligosaccharide library reveals the novel enzymatic action of d -glucosaminyl 3- O -sulfotransferase-3a
Nguyen, T. K. N., Arungundram, S., Tran, V. M., Raman, K., Al-Mafraji, K., Venot, A. P., Boons, G., & Kuberan, B. (2011) · Molecular BioSystems · doi:10.1039/c1mb05221g · Cited by 23
Glycans in Diseases and Therapeutics
Pavão, M. S. G. (2011) · Springer eBooks · doi:10.1007/978-3-642-16833-8 · Cited by 22
Insights into the role of 3-O-sulfotransferase in heparan sulfate biosynthesis
Meneghetti, M. C. Z., Gesteira, T. F., Tashima, A. K., Chavante, S. F., Yates, E. A., Liu, J., Nader, H. B., & de Lima, M. A. (2017) · Organic & Biomolecular Chemistry · doi:10.1039/c7ob01533j · Cited by 20
Involvement of Heparan Sulfate and Heparanase in Neural Development and Pathogenesis of Brain Tumors
Xiong, A., Spyrou, A., & Forsberg‐Nilsson, K. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-34521-1_14 · Cited by 16
Heparan Sulfate Biosynthesis Enzymes in Embryonic Stem Cell Biology
Tamm, C., Kjellén, L., & Li, J. (2012) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155412465090 · Cited by 14
Role of HSPGs in Systemic Bacterial Infections
Aquino, R. S., Hayashida, K., Hayashida, A., & Park, P. W. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1398-6_46 · Cited by 10
Specific 3-O-sulfated heparan sulfate domains regulate salivary gland basement membrane metabolism and epithelial differentiation
Patel, V. N., Aure, M. H., Choi, S. H., Ball, J. R., Lane, E. D., Wang, Z., Xu, Y., Zheng, C., Liu, X., Martín, D., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51862-0 · Cited by 9
Antithrombin-binding heparan sulfate is ubiquitously expressed in epithelial cells and suppresses pancreatic tumorigenesis
Clausen, T. M., Weiss, R. J., Tremblay, J. R., Kellman, B. P., Coker, J. K. C., Dworkin, L. A., Rodriguez, J. W., Chang, I. R., Chen, T.-H. T., Padala, V., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci184172 · Cited by 8
Bioengineered heparin
Lord, M. S., & Whitelock, J. M. (2014) · Bioengineered · doi:10.4161/bioe.29388 · Cited by 8
Diverse functions of uterine proteoglycans in human reproduction (Review)
Kitaya, K. (2012) · Molecular Medicine Reports · doi:10.3892/mmr.2012.826 · Cited by 8
Spatiotemporal distribution of heparan sulfate epitopes during murine cartilage growth plate development
Gomes, R. R., Kuppevelt, T. H. V., Farach‐Carson, M. C., & Carson, D. D. (2006) · Histochemistry and Cell Biology · doi:10.1007/s00418-006-0203-4 · Cited by 8
Embryogenesis and gene targeting of coagulation factors in mice
Sood, R., & Weiler-Guettler, H. (2003) · Best Practice & Research Clinical Haematology · doi:10.1016/s1521-6926(02)00092-0 · Cited by 7
Genetic variability in proteoglycan biosynthetic genes reveals new facets of heparan sulfate diversity.
Ouidja, M. O., Biard, D. S. F., Huynh, M. B., Laffray, X., Gómez-Henao, W., Chantepie, S., Douaron, G. L., Rebergue, N., Maïza, A., Merrick, H., et al. (2024) · PubMed Central · doi:10.1042/ebc20240106 · Cited by 5
A comprehensive study of antithrombin deficiency in a large cohort of Chinese thrombophilia pedigrees: uncovering 4 SERPINC1 pathogenic variants merely impaired progressive activities
Chen, C., Wu, X., Li, L., Xiang, Y., Zhang, H., Song, Y., Ding, Q., Wang, X., Hu, X., & Dai, J. (2025) · Journal of Thrombosis and Haemostasis · doi:10.1016/j.jtha.2025.04.022 · Cited by 5
The Role of Placental Glycosaminoglycans in the Prevention of Pre-Eclampsia
Gunatillake, T., Chui, A., & Said, J. M. (2013) · Journal of Glycobiology · doi:10.4172/2168-958x.1000105 · Cited by 4
Variability in proteoglycan biosynthetic genes reveals new facets of heparan sulfates diversity. A systematic review and analysisPreprint
Ouidja, M. O., Biard, D. S. F., Chantepie, S., Laffray, X., Douaron, G. L., Huynh, M. B., Rebergue, N., Maïza, A., Rubio, K., González-Velasco, Ó., et al. (2022) · medRxiv · doi:10.1101/2022.04.18.22273971 · Cited by 4
Bacterial Glycosyltransferases Involved in Molecular Mimicry of Mamm alian Glycans
Wakarchuk, W. W. (2011) · Pan Stanford Publishing eBooks · doi:10.1201/b11409-9 · Cited by 3
Loss of 3-O-sulfotransferase enzymes, Hs3st3a1 and Hs3st3b1, reduces kidney and glomerular size and disrupts glomerular architecture
Patel, V. N., Ball, J. R., Choi, S. H., Lane, E. D., Wang, Z., Aure, M. H., Villapudua, C. U., Zheng, C., Bleck, C. K. E., Mohammed, H., et al. (2024) · Matrix Biology · doi:10.1016/j.matbio.2024.06.006 · Cited by 3
Heparan Sulfate (Glucosamine) 3-O-Sulfotransferase 1-6 (HS3ST1-6)
Liu, J., & O’Leary, T. R. (2014) · Springer eBooks · doi:10.1007/978-4-431-54240-7_117 · Cited by 2
The Glycocode: Translating Heparan Sulfate Fine Structure into Developmental Function
Cadwallader, A. B., & Yost, H. J. (2013) · Biology of extracellular matrix · doi:10.1007/978-3-642-35935-4_1 · Cited by 2
Glycans in Embryonic Stem Cells
Pickford, C. E., Holley, R. J., Meade, K. A., & Merry, C. L. R. (2011) · Springer eBooks · doi:10.1007/978-3-642-16833-8_5 · Cited by 1
Biological function of mast cell chymase
Chugunova, E. (2004) · Epsilon Open Archive (Sveriges lantbruksuniversitet biblioteket (Swedish University of Agricultural Sciences))
Targets of Elf5 in Mouse Trophoblast Stem Cells
Deane, J. R. (2007) · Research Commons (University of Waikato)
Novel Regulators of Brain Tumor Development : – From neural stem cell differentiation to in vivo models
Xiong, A. (2015) · Uppsala University Publications (Uppsala University)
Biological Function of Mast Cell Chymase In vitro and in vivo studies: a thorny pathway
Chugunova, E. (2004)
Regulation of Heparan Sulfate 6-O-Sulfation Patterns
Do, A.-T. (2006) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
The preparation and characterization of a heparin-derived oligosaccharide that binds to herpes simplex virus type 1 glycoprotein D
Copeland, R. J. (2006) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/3g0j-3d77
Héparanes sulfate : Structure, fonctions, régulation
Vivès, R. R. (2011) · HAL
Sulfotransferases and Sulfatases
Chapman, E., & Hanson, S. R. (2011) · Pan Stanford Publishing eBooks · doi:10.1201/b11409-10
N-Sulfation and Polymerization in Heparan Sulfate Biosynthesis
Presto, J. (2006) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
In vitro studies of the substrate specificities of heparan sulfate 2-O- and 6-O-sulfotransferases.
Smeds, E. (2004) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Rôle des glucosaminyl sulfotransférases dans la biosynthèse de motifs héparanes sulfates impliqués dans la fixation et l’activité de facteurs inflammatoires
Deligny, A. (2009) · theses.fr (ABES) · doi:10.70675/624d6bb3z81caz4da5z86d2ze293c5e9ae31
Développement d’une antithrombine modifiée inactive comme antidote des anticoagulants hépariniques
Fazavana, J. (2012) · theses.fr (ABES) · doi:10.70675/4324ca83z6c5bz49ecz80b8z3504ebd533a0
Importance des glycosaminoglycanes de surface dans les phénomènes inflammatoires liés au cancer
Martinez, P. (2014) · theses.fr (ABES) · doi:10.70675/d8d46778ze3baz4df0z9270z4a2656f165d0
Étude de la régulation d’expression et des activités des héparanes 3-O-sulfotransférases 2, 3A et 3B dans les macrophages
Delos, M. (2016) · theses.fr (ABES) · doi:10.70675/4692701fzdf3dz49e7z89ecz0adfd2832ad6
Étude de la régulation des enzymes de modification des héparanes sulfates en condition inflammatoire
Sikora, A. (2015) · theses.fr (ABES) · doi:10.70675/46b84622z2269z4e58za336z16b00b6cfcfa
Caractérisation biochimique et fonctionnelle de l'enzyme HSULF
Seffouh, A. (2016) · theses.fr (ABES) · doi:10.70675/5bf677b8z1ba5z4350z99b3zec619fad83b1
L’héparane sulfate 3-O-sulfotransférase 3A (3-OST3A) : une enzyme de maturation des glycosaminoglycanes en tant que nouveau régulateur tumoral dans le cancer du sein
Gauche, C. (2016) · theses.fr (ABES) · doi:10.70675/dbd9f613z4083z46f5z913fzaec1e6a74fe4
Implication of 3S-HS and HS3ST2 in synaptic stability under physiological conditions and in Alzheimer's disease-related tauopahty
Maïza, A. (2019) · theses.fr (ABES) · doi:10.70675/85b6b166z912fz42acza589z62dfb17d5a4e
Study of 3-O-sulfated heparan sulfates on tauopathy development in AD : neuropathologic and cellular approach
Rebergue, N. (2022) · theses.fr (ABES) · doi:10.70675/1625c958z4f5az4c53zb053z9743a765c9ac
Genome-Wide Association Study to Identify Novel Genetic Variants Associated With Primary Budd–Chiari Syndrome
Kumar, S., Biswas, S., Agarwal, S., Agarwal, A., Sheikh, S. S., Ashraf, A., Goyal, M., Trehan, C., Taneja, S., Shukla, A., et al. (2026) · Journal of Clinical and Experimental Hepatology · doi:10.1016/j.jceh.2026.103552

Authors: Shworak, N. W., HajMohammadi, S., de Agostini, A. I., & Rosenberg, R. D.
Affiliations: Dartmouth College (US)
Massachusetts Institute of Technology (US)
Corresponding author: Shworak, Nicholas W.
ORCID: Shworak, Nicholas W.
Rosenberg, Robert D.
Venue: Glycoconjugate Journal
Publisher: Springer Science and Business Media LLC
Published: 2002-05
Volume: 19
Issue: 4-5
Pages: 355-361
ISSN: 0282-0080 (ISSN-L)
1573-4986
DOI: 10.1023/a:1025377206600
OpenAlex: W2082080310
Cited by: 77
References: 52
Citations by year: 2026: 1 · 2025: 1 · 2024: 3 · 2022: 2 · 2021: 1 · 2020: 1 · 2019: 2 · 2017: 2 · 2016: 4 · 2015: 3 · 2014: 5 · 2013: 5 · 2012: 2
FWCI: 1.58
Type: journal article
Language: en
Open access: closed
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Glycoconjugate Journal (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
Health Sciences › Medicine › Hematology › Platelet Disorders and Treatments
Keywords: hemostasis, knockout mice, perinatal lethality, fetal growth restriction, coagulation, genetic background
MeSH terms: Animals, Animals, Newborn, Anticoagulants, Binding Sites, Blood Coagulation, Carbohydrate Sequence, Hemostasis, Heparan Sulfate, Molecular Sequence Data, Phenotype, Sulfotransferases, Mice, Knockout, Mice

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.

Mice deficient in heparan sulfate 3-O-sulfotransferase-1: Normal hemostasis with unexpected perinatal phenotypes

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Citations

Cites

Cited by

Related

Metadata

Record

About these checks

Data sources