Journal articles on the topic 'Heparin'
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Zvibel, I., E. Halay, and L. M. Reid. "Heparin and hormonal regulation of mRNA synthesis and abundance of autocrine growth factors: relevance to clonal growth of tumors." Molecular and Cellular Biology 11, no. 1 (1991): 108–16. http://dx.doi.org/10.1128/mcb.11.1.108-116.1991.
Full textZvibel, I., E. Halay, and L. M. Reid. "Heparin and hormonal regulation of mRNA synthesis and abundance of autocrine growth factors: relevance to clonal growth of tumors." Molecular and Cellular Biology 11, no. 1 (1991): 108–16. http://dx.doi.org/10.1128/mcb.11.1.108.
Full textBar-Ner, M., A. Eldor, L. Wasserman, et al. "Inhibition of heparanase-mediated degradation of extracellular matrix heparan sulfate by non-anticoagulant heparin species." Blood 70, no. 2 (1987): 551–57. http://dx.doi.org/10.1182/blood.v70.2.551.551.
Full textBar-Ner, M., A. Eldor, L. Wasserman, et al. "Inhibition of heparanase-mediated degradation of extracellular matrix heparan sulfate by non-anticoagulant heparin species." Blood 70, no. 2 (1987): 551–57. http://dx.doi.org/10.1182/blood.v70.2.551.bloodjournal702551.
Full textFareed, Jawed, Adrian Sonevytsky, Omer Iqbal, Walter P. Jeske, Massimo Iacobelli, and Debra Hoppensteadt. "Inhibition of Heparinase I by Defibrotide with Potential Clinical Implications." Blood 108, no. 11 (2006): 1626. http://dx.doi.org/10.1182/blood.v108.11.1626.1626.
Full textPinhal, Maria A. S., Isabel A. N. Santos, Irani F. Silva, Carl P. Dietrich, and Helena B. Nader. "Minimum Fragments of the Heparin Molecule Able to Produce the Accumulation and Change of the Sulfation Pattern of an Antithrombotic Heparan Sulfate from Endothelial Cells." Thrombosis and Haemostasis 74, no. 04 (1995): 1169–74. http://dx.doi.org/10.1055/s-0038-1649898.
Full textHovingh, P., M. Piepkorn, and A. Linker. "Biological implications of the structural, antithrombin affinity and anticoagulant activity relationships among vertebrate heparins and heparan sulphates." Biochemical Journal 237, no. 2 (1986): 573–81. http://dx.doi.org/10.1042/bj2370573.
Full textSieme, Daniel, Christian Griesinger, and Nasrollah Rezaei-Ghaleh. "Metal Binding to Sodium Heparin Monitored by Quadrupolar NMR." International Journal of Molecular Sciences 23, no. 21 (2022): 13185. http://dx.doi.org/10.3390/ijms232113185.
Full textDiamond, M. S., R. Alon, C. A. Parkos, M. T. Quinn, and T. A. Springer. "Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/CD1)." Journal of Cell Biology 130, no. 6 (1995): 1473–82. http://dx.doi.org/10.1083/jcb.130.6.1473.
Full textZhang, Fuming, Lanhong Zheng, Shuihong Cheng, et al. "Comparison of the Interactions of Different Growth Factors and Glycosaminoglycans." Molecules 24, no. 18 (2019): 3360. http://dx.doi.org/10.3390/molecules24183360.
Full textAdler, S. "Inhibition of rat glomerular visceral epithelial cell growth by heparin." American Journal of Physiology-Renal Physiology 255, no. 4 (1988): F781—F786. http://dx.doi.org/10.1152/ajprenal.1988.255.4.f781.
Full textvon Hugo, R. "Ist niedermolekulares Heparin plazentagängig?" Hämostaseologie 09, no. 05 (1989): 244–47. http://dx.doi.org/10.1055/s-0038-1655277.
Full textBeurskens, Danielle M. H., Joram P. Huckriede, Roy Schrijver, H. Coenraad Hemker, Chris P. Reutelingsperger, and Gerry A. F. Nicolaes. "The Anticoagulant and Nonanticoagulant Properties of Heparin." Thrombosis and Haemostasis 120, no. 10 (2020): 1371–83. http://dx.doi.org/10.1055/s-0040-1715460.
Full textBanik, Nipa, Seong-Bin Yang, Tae-Bong Kang, Ji-Hong Lim, and Jooho Park. "Heparin and Its Derivatives: Challenges and Advances in Therapeutic Biomolecules." International Journal of Molecular Sciences 22, no. 19 (2021): 10524. http://dx.doi.org/10.3390/ijms221910524.
Full textShaughnessy, SG, E. Young, P. Deschamps, and J. Hirsh. "The effects of low molecular weight and standard heparin on calcium loss from fetal rat calvaria." Blood 86, no. 4 (1995): 1368–73. http://dx.doi.org/10.1182/blood.v86.4.1368.bloodjournal8641368.
Full textColtrini, D., M. Rusnati, G. Zoppetti, et al. "Different effects of mucosal, bovine lung and chemically modified heparin on selected biological properties of basic fibroblast growth factor." Biochemical Journal 303, no. 2 (1994): 583–90. http://dx.doi.org/10.1042/bj3030583.
Full textPahl, M. V., N. D. Vaziri, F. Oveisi, J. Wang, and Y. Ding. "Antithrombin III inhibits mesangial cell proliferation." Journal of the American Society of Nephrology 7, no. 10 (1996): 2249–53. http://dx.doi.org/10.1681/asn.v7102249.
Full textMycroft-West, Courtney J., Lynsay C. Cooper, Anthony J. Devlin та ін. "A Glycosaminoglycan Extract from Portunus pelagicus Inhibits BACE1, the β Secretase Implicated in Alzheimer’s Disease". Marine Drugs 17, № 5 (2019): 293. http://dx.doi.org/10.3390/md17050293.
Full textBuddecke, E. "Non-anticoagulant functions of heparin and heparan sulfate." Hämostaseologie 16, no. 01 (1996): 6–14. http://dx.doi.org/10.1055/s-0038-1656632.
Full textFareed, Jawed, Rakesh Wahi, Indermohan Thethi, et al. "Molecular Mimicry in the Adulteration of Heparins. Chemical Basis for the Development of Oversulfated Chondroitin Sulfate and Related Contaminants." Blood 118, no. 21 (2011): 4322. http://dx.doi.org/10.1182/blood.v118.21.4322.4322.
Full textChao, Yapeng, Shaoxiang Xiong, Xiulan Cheng, and Shijun Qian. "Mass Spectrometric Evidence of Heparin Disaccharides for the Catalytic Characterization of a Novel Endolytic Heparinase." Acta Biochimica et Biophysica Sinica 36, no. 12 (2004): 840–44. http://dx.doi.org/10.1093/abbs/36.12.840.
Full textYanaka, Kiyoyuki, Stephen R. Spellman, James B. McCarthy, Theodore R. Oegema, Walter C. Low, and Paul J. Camarata. "Reduction of brain injury using heparin to inhibit leukocyte accumulation in a rat model of transient focal cerebral ischemia. I. Protective mechanism." Journal of Neurosurgery 85, no. 6 (1996): 1102–7. http://dx.doi.org/10.3171/jns.1996.85.6.1102.
Full textBadillo-Samapayo, Jessica, and Jesús Aguilar-Castro. "Trombocitopenia como efecto secundario por la administración de heparinas en los pacientes de COVID-19. Una revisión sistemática." Casos y Revisiones de Salud 4, no. 1 (2022): 72–88. http://dx.doi.org/10.22201/fesz.26831422e.2022.4.1.7.
Full textJaques, L. B. "Heparin." Hämostaseologie 05, no. 04 (1985): 154–59. http://dx.doi.org/10.1055/s-0038-1655119.
Full textKouta, Ahmed, Walter Jeske, Debra Hoppensteadt, Omer Iqbal, Yiming Yao, and Jawed Fareed. "Comparative Pharmacological Profiles of Various Bovine, Ovine, and Porcine Heparins." Clinical and Applied Thrombosis/Hemostasis 25 (January 1, 2019): 107602961988940. http://dx.doi.org/10.1177/1076029619889406.
Full textShi, Deling, Changkai Bu, Peng He, et al. "Structural Characteristics of Heparin Binding to SARS-CoV-2 Spike Protein RBD of Omicron Sub-Lineages BA.2.12.1, BA.4 and BA.5." Viruses 14, no. 12 (2022): 2696. http://dx.doi.org/10.3390/v14122696.
Full textScully, M. F., V. Ellis, N. Shah, and V. Kakkar. "Effect of a heparan sulphate with high affinity for antithrombin III upon inactivation of thrombin and coagulation factor Xa." Biochemical Journal 262, no. 2 (1989): 651–58. http://dx.doi.org/10.1042/bj2620651.
Full textBaig, Nausheen, Ahmed Kouta, Walter Jeske, et al. "Validation of the Bioequivalence of USP Potency Adjusted Porcine, Ovine, and Bovine Heparins." Blood 136, Supplement 1 (2020): 6. http://dx.doi.org/10.1182/blood-2020-142861.
Full textSu, Dunhao, Yong Li, Edwin A. Yates, Mark A. Skidmore, Marcelo A. Lima, and David G. Fernig. "Analysis of protein-heparin interactions using a portable SPR instrument." PeerJ Analytical Chemistry 4 (April 8, 2022): e15. http://dx.doi.org/10.7717/peerj-achem.15.
Full textLindsay, Susan L., Rebecca Sherrard Smith, Edwin A. Yates, et al. "Validation of Recombinant Heparan Sulphate Reagents for CNS Repair." Biology 12, no. 3 (2023): 407. http://dx.doi.org/10.3390/biology12030407.
Full textOlson, Guy, Walter Jeske, Omer Iqbal, et al. "Potency Adjusted Blended Heparin of Bovine, Ovine, and Porcine Heparin Exhibit Comparable Biologic Effects to Referenced Single-Sourced Porcine Heparin." Clinical and Applied Thrombosis/Hemostasis 29 (January 2023): 107602962311632. http://dx.doi.org/10.1177/10760296231163251.
Full textVairo, Bruno, Leonardo Cinelli, Gustavo Santos, et al. "Heparins from porcine and bovine intestinal mucosa: Are they similar drugs?" Thrombosis and Haemostasis 103, no. 05 (2010): 1005–15. http://dx.doi.org/10.1160/th09-11-0761.
Full textGreinacher, A., I. Michels, and C. Mueller-Eckhardt. "Heparin-Associated Thrombocytopenia: The Antibody Is Not Heparin Specific." Thrombosis and Haemostasis 67, no. 05 (1992): 545–49. http://dx.doi.org/10.1055/s-0038-1648491.
Full textPatton, W. A., C. A. Granzow, L. A. Getts, et al. "Identification of a heparin-binding protein using monoclonal antibodies that block heparin binding to porcine aortic endothelial cells." Biochemical Journal 311, no. 2 (1995): 461–69. http://dx.doi.org/10.1042/bj3110461.
Full textHoppensteadt, Debra, Jeanine M. Walenga, Jawed Fareed, and Rodger L. Bick. "Heparin, low–molecular-weight heparins, and heparin pentasaccharide." Hematology/Oncology Clinics of North America 17, no. 1 (2003): 313–41. http://dx.doi.org/10.1016/s0889-8588(02)00091-6.
Full textWeiss, Ryan J., Philipp N. Spahn, Alejandro Gómez Toledo, et al. "ZNF263 is a transcriptional regulator of heparin and heparan sulfate biosynthesis." Proceedings of the National Academy of Sciences 117, no. 17 (2020): 9311–17. http://dx.doi.org/10.1073/pnas.1920880117.
Full textVisentin, Gian Paolo. "Heparin-Induced Thrombocytopenia: Molecular Pathogenesis." Thrombosis and Haemostasis 82, no. 08 (1999): 448–56. http://dx.doi.org/10.1055/s-0037-1615865.
Full textSung, Michelle, Jeanine Walenga, Walter Jeske, Omer Iqbal, and Mamdouh Bakhos. "Comparing a New Bovine Source Heparin to the Clinically Used Porcine Heparin for Platelet Function Effects and Heparin-Induced Thrombocytopenia Potential." Blood 132, Supplement 1 (2018): 2540. http://dx.doi.org/10.1182/blood-2018-99-118781.
Full textWalsh, R. L., T. J. Dillon, R. Scicchitano, and G. McLennan. "Heparin and heparan sulphate are inhibitors of human leucocyte elastase." Clinical Science 81, no. 3 (1991): 341–46. http://dx.doi.org/10.1042/cs0810341.
Full textKhiella, Marco, Walter Jeske, Jeanine Walenga, et al. "Bovine Heparin Compared to Porcine Heparin to Demonstrate Bioequivalence." Blood 132, Supplement 1 (2018): 1253. http://dx.doi.org/10.1182/blood-2018-99-118809.
Full textLjungberg, B., and H. Johnsson. "In Vivo Effects of a Low Molecular Weight Heparin Fragment on Platelet Aggregation and Platelet Dependent Hemostasis in Dogs." Thrombosis and Haemostasis 60, no. 02 (1988): 232–35. http://dx.doi.org/10.1055/s-0038-1647036.
Full textWalenga, Jeanine, Walter Jeske, Sabrina Bertini, et al. "Bovine Heparin Demonstrates the Same Interaction with HIT Antibodies As Porcine Heparin." Blood 134, Supplement_1 (2019): 2351. http://dx.doi.org/10.1182/blood-2019-127304.
Full textCarlsson, Pernilla, Jenny Presto, Dorothe Spillmann, Ulf Lindahl, and Lena Kjellén. "Heparin/Heparan Sulfate Biosynthesis." Journal of Biological Chemistry 283, no. 29 (2008): 20008–14. http://dx.doi.org/10.1074/jbc.m801652200.
Full textSandoval, Daniel R., Alejandro Gomez Toledo, Chelsea D. Painter, et al. "Proteomics-based screening of the endothelial heparan sulfate interactome reveals that C-type lectin 14a (CLEC14A) is a heparin-binding protein." Journal of Biological Chemistry 295, no. 9 (2020): 2804–21. http://dx.doi.org/10.1074/jbc.ra119.011639.
Full textVILAR, Rolando E., Dineshchandra GHAEL, Min LI, et al. "Nitric oxide degradation of heparin and heparan sulphate." Biochemical Journal 324, no. 2 (1997): 473–79. http://dx.doi.org/10.1042/bj3240473.
Full textAhmed, Tahir, Jaime Ungo, Min Zhou, and Carlos Campo. "Inhibition of allergic late airway responses by inhaled heparin-derived oligosaccharides." Journal of Applied Physiology 88, no. 5 (2000): 1721–29. http://dx.doi.org/10.1152/jappl.2000.88.5.1721.
Full textLeong, John M., Douglas Robbins, Louis Rosenfeld, Biswajit Lahiri, and Nikhat Parveen. "Structural Requirements for Glycosaminoglycan Recognition by the Lyme Disease Spirochete, Borrelia burgdorferi." Infection and Immunity 66, no. 12 (1998): 6045–48. http://dx.doi.org/10.1128/iai.66.12.6045-6048.1998.
Full textSekiguchi, Asuka, Miwako Narita, Toshio Yano, et al. "Enhancing Effects of Heparin/Low Molecular Weight Heparin/Heparan Sulfate on Antigen Presentation and Antigen-Specific Cytotoxic T Lymphocyte (CTL) Induction by Monocyte-Derived Dendritic Cells." Blood 104, no. 11 (2004): 3816. http://dx.doi.org/10.1182/blood.v104.11.3816.3816.
Full textKung, Chun, Jagadeesh Gabbeta, Valeri Krougliak, Emmanuel Quiazon, and Mark Triscott. "Liquid Heparin Assay: A Straightforward Approach for Monitoring the Clinical Use of Heparins." Blood 108, no. 11 (2006): 890. http://dx.doi.org/10.1182/blood.v108.11.890.890.
Full textSkaanning, Line K., Angelo Santoro, Thomas Skamris та ін. "The Non-Fibrillating N-Terminal of α-Synuclein Binds and Co-Fibrillates with Heparin". Biomolecules 10, № 8 (2020): 1192. http://dx.doi.org/10.3390/biom10081192.
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