The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Plasma clearance of glycoproteins with terminal mannose and N-acetylglucosamine by liver non-parenchymal cells. Studies with β-glucuronidase, N-acetyl-β-d-glucosaminidase, ribonuclease B and agalacto-orosomucoid
Open accessAbstract
Glycoproteins having mannose and/or N-acetylglucosamine in the terminal non-reducing position [Stockert, Morell & Scheinberg (1976) Biochem. Biophys. Res. Commun. 68, 988–993], and various lysosomal enzymes [Stahl, Schlesinger, Rodman & Doebber (1976) Nature (London) 264, 86–8] are rapidly cleared from plasma by the liver after intravenous administration. A liver cell-separation technique was used to determine the cellular localization of 125I-labelled beta-glucuronidase, ribonuclease B, agalacto-orosomucoid and asialo-orosomucoid. On a specific readioactivity basis, all ligands except 125I-labelled asialo-orosomucoid were enriched in the non-parenchymal cell fraction. Isolated cells, fixed and stained for beta-glucuronidase or N-acetyl-beta-D-glucosaminidase activity after intravenous injection of the enzymes, showed enrichment in the non-parenchymal cell fraction (probably Kupffer cells). After uptake by the non-parenchymal cells, liver lysosomal beta-glucuronidase and N-acetyl-beta-D-glucosaminidase showed degradation half-times of 2.2 and 0.4 days respectively.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Citations
Cites
Bolton, A. E., & Hunter, W. M. (1973) · Biochemical Journal · doi:10.1042/bj1330529 · Cited by 3,240
de Duve, C., & Wattiaux, R. (1966) · Annual Review of Physiology · doi:10.1146/annurev.ph.28.030166.002251 · Cited by 3,033
Antigen-antibody crossed electrophoresis
Laurell, C. ‐. (1965) · Analytical Biochemistry · doi:10.1016/0003-2697(65)90278-2 · Cited by 1,420
Ashwell, G., & Morell, A. G. (1974) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122860.ch3 · Cited by 1,212
Blouin, A., Bolender, R. P., & Weibel, E. R. (1977) · The Journal of Cell Biology · doi:10.1083/jcb.72.2.441 · Cited by 879
Stahl, P. D., Rodman, J. S., Miller, M. J., & Schlesinger, P. H. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.3.1399 · Cited by 590
Self-citationHuman cathepsin B1. Purification and some properties of the enzyme
Barrett, A. J. (1973) · Biochemical Journal · doi:10.1042/bj1310809 · Cited by 324
Mass isolation and culture of rat kupffer cells.
Munthe‐Kaas, A. C., Berg, T., Seglen, P. O., & Seljelid, R. (1975) · The Journal of Experimental Medicine · doi:10.1084/jem.141.1.1 · Cited by 212
Receptors for Immunoglobulin and Complement on Human Alveolar Macrophages
Reynolds, H. Y., Atkinson, J. P., Newball, H. H., & Frank, M. M. (1975) · The Journal of Immunology · doi:10.4049/jimmunol.114.6.1813 · Cited by 201
The Isolation of Ribonuclease B, a Glycoprotein, from Bovine Pancreatic Juice
Plummer, T. H., Hirs, C. H. W., & Tench, A. L. (1963) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81195-4 · Cited by 167
Flagged first, then by citations
Cited by
Sorted by citations
Items 101–200 of 209
Plasma markers of COVID-19 severity: a pilot study
Beimdiek, J., Janciauskiene, S. M., Wrenger, S., Volland, S., Roży, A., Fuge, J., Olejnicka, B. T., Pink, I., Illig, T., Popov, A., et al. (2022) · Respiratory Research · doi:10.1186/s12931-022-02272-7 · Cited by 30
Calvo, P., Barba, J., & Cabezas, J. A. (1982) · Clinica Chimica Acta · doi:10.1016/0009-8981(82)90400-4 · Cited by 29
Stavenhagen, K., Laan, L. C., Gao, C., Mehta, A. Y., Heimburg‐Molinaro, J., Glickman, J. N., van Die, I., & Cummings, R. D. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03863-1 · Cited by 28
Endocytosis of hyaluronidase-1 by the liver
Gasingirwa, M.-C., Thirion, J., Mertens-Strijthagen, J., Coninck, S. W., Flamion, B., Wattiaux, R., & Jadot, M. (2010) · Biochemical Journal · doi:10.1042/bj20100711 · Cited by 28
Harada, M., Shakado, S., Sakisaka, S., Tamaki, S., Ohishi, M., Sasatomi, K., Koga, H., Sata, M., & Tanikawa, K. (1997) · Liver International · doi:10.1111/j.1600-0676.1997.tb01025.x · Cited by 28
Purification and characterization of the d-mannose receptor from J774 mouse macrophage cells
Blum, J. S., Stahl, P. D., Díaz, R., & Fiani, M. L. (1991) · Carbohydrate Research · doi:10.1016/s0008-6215(00)90605-0 · Cited by 27
Self-citationNiesen, T. E., Alpers, D., Stahl, P. D., & Rosenblum, J. L. (1984) · Journal of Leukocyte Biology · doi:10.1002/jlb.36.3.307 · Cited by 26
Self-citationde Jong, A. S., Bouma, J. M. W., & Gruber, M. (1981) · Biochemical Journal · doi:10.1042/bj1980045 · Cited by 26
Chen, K., Wu, S.-Y., Leu, Y.-L., Prijovich, Z. M., Chen, B., Wang, H., Cheng, T., & Roffler, S. R. (2011) · Bioconjugate Chemistry · doi:10.1021/bc1005784 · Cited by 24
Dunn, W. A., & Englard, S. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43292-9 · Cited by 25
Clonal growth in vitro by mouse Kupffer cells
Chen, D.-M., Lin, H.-S., Stahl, P. D., & Stanley, E. R. (1979) · Experimental Cell Research · doi:10.1016/0014-4827(79)90449-x · Cited by 25
Self-citationGroß, V., Heinrich, P. C., Berg, D. V., Steube, K. G., Andus, T., Tran‐Thi, T., Decker, K., & Gerok, W. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb14048.x · Cited by 24
Carbohydrate-binding proteins of human serum: isolation of two mannose/fucose-specific lectins
Taylor, M. E., & Summerfield, J. A. (1987) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(87)90125-7 · Cited by 24
Glycosylation patterns in cells: an evolutionary marker?
Hughes, R. C., & Butters, T. D. (1981) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(81)90083-9 · Cited by 24
Dannevig, B. H., Struksnæs, G., Skogh, T., Kindberg, G. M., & Berg, T. (1990) · Fish Physiology and Biochemistry · doi:10.1007/bf00004462 · Cited by 23
Oligosaccharides on cathepsin D from porcine spleen
Nakao, Y., Kozutsumi, Y., Kawasaki, T., Yamashina, I., van HALBEEK, H., & Vliegenthart, J. F. G. (1984) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(84)90128-0 · Cited by 22
DAMM, J. B. L., Voshol, H., Hård, K., Kamerling, J. P., van Dedem, G. W. K., & Vliegenthart, J. F. G. (1988) · Glycoconjugate Journal · doi:10.1007/bf01049083 · Cited by 22
How good is the evidence to suggest that phagocytosis of ROS by RPE is receptor mediated?
McLaughlin, B. J., Cooper, N. G. F., & Shepherd, V. L. (1994) · Progress in Retinal and Eye Research · doi:10.1016/1350-9462(94)90008-6 · Cited by 22
Li, Q., & Guo, Z. (2017) · Organic Letters · doi:10.1021/acs.orglett.7b03275 · Cited by 21
Brady, R. O. (1982) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(82)90072-9 · Cited by 21
Kooistra, T., Duursma, A. M., Bouma, J. M. W., & Gruber, M. (1980) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(80)90020-3 · Cited by 21
Nanovaccines in cancer immunotherapy: Focusing on dendritic cell targeting
Achmad, H., Ibrahim, Y. S., Al‐Taee, M. M., Gabr, G. A., Riaz, M. W., Alshahrani, S. H., Ramírez‐Coronel, A. A., Jalil, A. T., Budi, H. S., Sawitri, W., et al. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109434 · Cited by 20
The Oligosaccharides of Plasma Glycoproteins: Synthesis, Structure, and Function
Baenziger, J. (1984) · Elsevier eBooks · doi:10.1016/b978-0-12-568404-0.50012-0 · Cited by 20
Receptors for Lysosomal Enzymes and Glycoproteins
Shepherd, V. L., Schlesinger, P. H., & Stahl, P. D. (1983) · Current topics in membranes and transport · doi:10.1016/s0070-2161(08)60535-3 · Cited by 20
Self-citationVidal‐Sicart, S., Vera, D. R., & Olmos, R. A. V. (2018) · Revista Española de Medicina Nuclear e Imagen Molecular (English Edition) · doi:10.1016/j.remnie.2018.10.009 · Cited by 19
Post-translational modification of proteins
Lodish, H. F. (1981) · Enzyme and Microbial Technology · doi:10.1016/0141-0229(81)90084-3 · Cited by 19
The effects of moderate drinking and abstinence on serum and urinary β-hexosaminidase levels
Kärkkäinen, P. A., Jokelainen, K., Roine, R. O., Suokas, A., & Salaspuro, M. P. (1990) · Drug and Alcohol Dependence · doi:10.1016/0376-8716(90)90137-4 · Cited by 19
Accarias, S., Genthon, C., Rengel, D., Boullier, S., Foucras, G., & Tabouret, G. (2016) · Innate Immunity · doi:10.1177/1753425916651330 · Cited by 18
Fucose plays a role in the clearance and uptake of glucocerebrosidase by rat liver cells
Furbish, F. S., Krett, N. L., Barranger, J. A., & Brady, R. O. (1980) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(80)80103-3 · Cited by 18
The Identification of Macrophage-enriched Glycoproteins Using Glycoproteomics
Zarif, J. C., Yang, W., Hernandez, J. R., Zhang, H., & Pienta, K. J. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.064444 · Cited by 17
Martins, P. R., Gameiro, M. C., Castoldi, L., Romagnoli, G. G., Lopes, F. C., Pinto, A. V. F. D. S., Loyola, W., & Kaneno, R. (2008) · Memórias do Instituto Oswaldo Cruz · doi:10.1590/s0074-02762008005000011 · Cited by 17
Beutler, E. (1981) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(81)90035-9 · Cited by 17
Identification of a defence mechanism in vivo against the leakage of enterokinase into the blood
GRANT, D. A. W., Magee, A. I., Meeks, D., Regan, C., Bainbridge, D. R. J., & Hermon-Taylor, J. (1979) · Biochemical Journal · doi:10.1042/bj1840619 · Cited by 17
Isolation and characterization of endogenous ligands for liver mannan-binding protein
Mori, K., Kawasaki, T., & Yamashina, I. (1988) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(88)90331-1 · Cited by 17
Receptors for native gonadotropins in amphibian liver
Kubokawa, K., & Ishii, S. (1987) · General and Comparative Endocrinology · doi:10.1016/0016-6480(87)90037-2 · Cited by 17
Straus, W., & Keller, J. M. (1986) · Histochemistry and Cell Biology · doi:10.1007/bf00493477 · Cited by 17
Carbohydrate Structure, Biological Recognition, and Immune Function
Reading, C. L. (1984) · Springer eBooks · doi:10.1007/978-1-4684-7464-0_5 · Cited by 17
Prevention of carbohydrate-mediated clearance of ricin-containing immunotoxins by the liver
Blakey, D. C., & Thorpe, P. E. (1988) · Cancer treatment and research · doi:10.1007/978-1-4613-1083-9_25 · Cited by 17
Some recent applications of carbohydrates and their derivatives in the pharmaceutical industry
van Boeckel, C. A. A. (1986) · Recueil des Travaux Chimiques des Pays-Bas · doi:10.1002/recl.19861050202 · Cited by 16
Muchmore, A. V., Decker, J. M., & Blaese, R. M. (1981) · Immunobiology · doi:10.1016/s0171-2985(81)80069-1 · Cited by 16
Mouse liver lysosomes contain enzymatically active processed forms of Hyal-1
Boonen, M., Emeline, P., Gilis, F., Flamion, B., & Jadot, M. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.03.070 · Cited by 15
Zaghmi, A., Drouin‐Ouellet, J., Brambilla, D., & Gauthier, M. A. (2020) · Biomaterials · doi:10.1016/j.biomaterials.2020.120461 · Cited by 17
Simmons, B. M., Stahl, P. D., & Russell, J. H. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)90608-5 · Cited by 15
Self-citationDing, J., Andersson, R. E., Hultberg, B. L., Soltesz, V. L., & Bengmark, S. (1993) · Scandinavian Journal of Gastroenterology · doi:10.3109/00365529309096045 · Cited by 15
Wilson, G. (1979) · The Journal of General Physiology · doi:10.1085/jgp.74.4.495 · Cited by 15
Endocytosis of native and glycosylated bovine serum albumin by duct cells of the rat parotid gland
Lotti, L. V., & Hand, A. R. (1989) · Cell and Tissue Research · doi:10.1007/bf00224116 · Cited by 14
The effect of surface sugars on liposomes in immunopotentiation
Latif, N. A., & Bachhawat, B. K. (1984) · Immunology Letters · doi:10.1016/0165-2478(84)90053-1 · Cited by 14
Lectin-affinity isolation of microvillous membranes from the pigmented epithelium of rat retina
Cooper, N. G. F., Tarnowski, B. I., & McLaughlin, B. J. (1987) · Current Eye Research · doi:10.3109/02713688709034868 · Cited by 14
Analysis of Diffrentiation and Transformation of Cells by Lectins
Raedler, A., Schreiber, S., & Batsakis, J. G. (1988) · CRC Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408368809106861 · Cited by 14
Modification of glycosylation of renin in sodium-depleted and captopril-treated rats
Kim, S., Hosoi, M., Hiruma, M., Ikemoto, F., & Yamamoto, K. (1989) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1989.256.6.e798 · Cited by 14
Uptake and processing of glycoproteins by rat hepatic mannose receptor
Taylor, M. E., Leaning, M. S., & Summerfield, J. A. (1987) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1987.252.5.e690 · Cited by 13
Straus, W. (1983) · Histochemistry and Cell Biology · doi:10.1007/bf00496617 · Cited by 12
Brady, R. O., & Furbish, F. S. (1982) · Springer eBooks · doi:10.1007/978-1-4684-4085-0_84 · Cited by 12
Serum β-hexosaminidase isoenzymes are precursor forms
Isaksson, A., & Hultberg, B. L. (1995) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.3109/00365519509104983 · Cited by 12
Bocci, V. A. (1982) · Survey of Immunologic Research · doi:10.1007/bf02918338 · Cited by 11
AHMAD, I., Sarkar, A., & Bachhawat, B. K. (1991) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.10.171 · Cited by 10
Carter, S. D., Brennan, F. M., Grace, S. A., & Elson, C. J. (1984) · PubMed Central · Cited by 10
Cell types in rat liver cultures: their identification and isolation
Grisham, J. W. (1983) · Springer eBooks · doi:10.1007/978-1-4613-3879-6_2 · Cited by 10
Fritzvold, R., Dannevig, B. H., & Berg, T. (1989) · Fish Physiology and Biochemistry · doi:10.1007/bf01875606 · Cited by 9
Sebok, K., Meloche, S., & Sairam, M. R. (1990) · Life Sciences · doi:10.1016/0024-3205(90)90094-8 · Cited by 9
Pattern of Serum Beta-Hexosaminidase in Liver Cirrhosis
Hultberg, B. L., Isaksson, A., Joelsson, B. E., ALWMARK, A., Gullstrand, P., & Bengmark, S. (1983) · Scandinavian Journal of Gastroenterology · doi:10.3109/00365528309182109 · Cited by 9
Ludolph, D., Groß, V., Katz, N. R., Giffhorn‐Katz, S., Kreisel, W., Heinrich, P. C., & Gerok, W. (1989) · Biochemical Pharmacology · doi:10.1016/0006-2952(89)90092-0 · Cited by 8
A biochemical dissection of the functional polarity of the plasma membrane of the hepatocyte
Evans, W. H. (1980) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(80)90003-9 · Cited by 8
Serial section analysis of clathrin-coated pits in rat liver sinusoidal endothelial cells
Goldenthal, K. L., Pastan, I. H., & Willingham, M. C. (1985) · Experimental Cell Research · doi:10.1016/0014-4827(85)90091-6 · Cited by 8
Restagno, D., Saraswat, M., Aziz, P. V., Smith, K., Roberts, A. J., Hintze, J., & Marth, J. D. (2025) · Nature Communications · doi:10.1038/s41467-025-61346-4 · Cited by 7
Carbohydrate mediated drug delivery: Synthesis and characterization of new lipid-conjugates
Ahmad, M. U., Ali, S. M., Ahmad, A., Sheikh, S., Chen, P. L., & Ahmad, I. (2014) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2014.10.003 · Cited by 7
Deugnier, Y., Treut, A. L., Glaise, D., Brissot, P., & Gall, J. L. (1980) · Clinica Chimica Acta · doi:10.1016/0009-8981(80)90345-9 · Cited by 7
Steube, K. G., Groß, V., Häussinger, D., Tran‐Thi, T., Decker, K., Gerok, W., & Heinrich, P. C. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80135-8 · Cited by 7
Donskow‐Łysoniewska, K., Krawczak, K., Machcińska, M., Głaczyńska, M., & Doligalska, M. (2019) · Immunobiology · doi:10.1016/j.imbio.2019.08.004 · Cited by 6
Koizumi, A., Hasegawa, L. S., Thomas, I. K., & Toshiko, I. (1986) · Biochemical Pharmacology · doi:10.1016/0006-2952(86)90184-x · Cited by 6
Internalization of Collagen: An Important Matrix Turnover Pathway in Cancer
Kuczek, D. E., Hübbe, M. L., & Madsen, D. H. (2017) · Biology of extracellular matrix · doi:10.1007/978-3-319-60907-2_2 · Cited by 5
Blomhoff, H. K., Blomhoff, R., & Christensen, T. (1984) · International Journal of Biochemistry · doi:10.1016/0020-711x(84)90041-7 · Cited by 5
Labeled proteins, their preparation and applications
Káš, J., & Rauch, P. (1983) · Topics in current chemistry · doi:10.1007/3-540-12396-2_8 · Cited by 5
Graabæk, P. M. (1986) · Journal of Ultrastructure and Molecular Structure Research · doi:10.1016/0889-1605(86)90064-9 · Cited by 5
Lysosomes and Mononuclear Phagocytes
Stahl, P. D. (1983) · Springer eBooks · doi:10.1007/978-94-009-5975-0_6 · Cited by 5
Self-citationThe Mannose Recognition Pathway-Implications for Lysosome Physiology
Stahl, P. D., Wileman, T. E., & Shepherd, V. L. (1984) · Elsevier eBooks · doi:10.1016/b978-0-12-079280-1.50018-8 · Cited by 5
Self-citationTumor-associated macrophages: orchestrators of the tumor microenvironment
Echols, J. B., Meehan, A. W., Marotto, K., Ordonez, V., & Hildreth, B. E. (2026) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00834.2025 · Cited by 4
Faguet, G. B., & Agee, J. F. (1997) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428199709039039 · Cited by 4
Serum β‐Hexosaminidase in Diabetes Mellitus with Reference to the Type of Treatment
Agardh, C., Hultberg, B. L., & Thorén, S. A. (1982) · Acta Medica Scandinavica · doi:10.1111/j.0954-6820.1982.tb03166.x · Cited by 4
(2008) · Springer eBooks · doi:10.1007/978-1-4020-6754-9_5403 · Cited by 4
Chen, W., Barback, C. V., Wang, S., Hoh, C. K., Chang, E. Y., Hall, D. J., Head, B. P., & Vera, D. R. (2020) · Nuclear Medicine and Biology · doi:10.1016/j.nucmedbio.2020.02.013 · Cited by 3
Hultberg, B. L., Isaksson, A., Agardh, E., & AGARDH, C. ‐. (1991) · Clinica Chimica Acta · doi:10.1016/0009-8981(91)90071-j · Cited by 3
Lake‐Bakaar, D. M. (1980) · Acta Pharmacologica et Toxicologica · doi:10.1111/j.1600-0773.1980.tb02465.x · Cited by 3
Origin and Dynamics of Lysosomes
FIGURA, K. V., Klein, U., & Hasilík, A. (1980) · Springer eBooks · doi:10.1007/978-3-642-81557-7_15 · Cited by 3
Membrane Recycling (Shuttle?) in Endocytosis
Tulkens, P. M., Schneider, Y., Trouet, A., Karnovsky, M. L., & Baggiolini, M. (1980) · Springer eBooks · doi:10.1007/978-94-009-8793-7_24 · Cited by 3
Faguet, G. B., & Agee, J. F. (1997) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428199709039041 · Cited by 3
Role of N-glycosylation for the plasma clearance of rat liver secretory glycoproteins
GROSS, V., Steube, K. G., Tran‐Thi, T., Gerok, W., & Heinrich, P. C. (1989) · Biochemical Society Transactions · doi:10.1042/bst0170021 · Cited by 3
Glycan‐Mediated Targeting Methods
Vong, K., Tanaka, K., & Fukase, K. (2019) · doi:10.1002/9783527344406.ch17 · Cited by 3
Beutler, E., & Dale, G. L. (1979) · Elsevier eBooks · doi:10.1016/b978-0-12-066250-0.50031-4 · Cited by 3
Carbohydrate-Recognition Proteins of Macrophages and Related Cells
Taylor, M. E. (1993) · Blood cell biochemistry · doi:10.1007/978-1-4757-9534-9_14 · Cited by 2
Vidal‐Sicart, S., Vera, D. R., & Olmos, R. A. V. (2018) · Revista Española de Medicina Nuclear e Imagen Molecular · doi:10.1016/j.remn.2018.09.001 · Cited by 2
In Vivo and in Vitro Evidence for a Lysosomal Enzyme Uptake System in Macrophages
Stahl, P. D., Townsend, R. R., Tietze, C., Schlesinger, P. H., Silverstein, S. C., & van der Meer, J. W. M. (1980) · Springer eBooks · doi:10.1007/978-94-009-8793-7_33 · Cited by 2
Self-citationMurray, M. C., BHAVANANDAN, V. P., & Davidson, E. A. (1988) · Glycoconjugate Journal · doi:10.1007/bf01049920 · Cited by 2
Hallinan, F. M. (1981) · Medical Hypotheses · doi:10.1016/0306-9877(81)90089-x · Cited by 2
DISTRIBUTION OF ACID HYDROLASES IN THE NEPHRON OF NORMAL AND DIABETIC RATS
Hir, M. L., Dubach, U. C., & Guder, W. (1980) · Elsevier eBooks · doi:10.1016/b978-0-08-025517-0.50015-1 · Cited by 2
Bandaranayake, U. K., Sato, H., & Miho, S. (2024) · Analytical Sciences · doi:10.1007/s44211-024-00649-w · Cited by 1
Recent Advances in Defining Mannose Receptor Structure and Function
Pontow, S. E., & Stahl, P. D. (1995) · Springer eBooks · doi:10.1007/978-3-642-79547-3_21 · Cited by 1
Self-citationThe fate of intravenously administered biotin-labelled hyaluronidase in the rat
LACE, D., Gacesa, P., & Olavesen, A. H. (1991) · Biochemical Pharmacology · doi:10.1016/0006-2952(91)90114-k · Cited by 1
Versavel, C., de Vonne, T. L., & Mouray, H. (1986) · PubMed Central · Cited by 1
The role of the lectin VIP36 in the early secretory pathway
Reiterer, V. (2010) · edoc (University of Basel) · doi:10.5451/unibas-005405317
Metadata
- Authors
- Schlesinger, P. H., Doebber, T. W., Mandell, B. F., White, R., DeSchryver, C., Rodman, J. S., Miller, M. J., & Stahl, P.
- Affiliations
- University of Namur (BE)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1978-10-15
- Volume
- 176
- Issue
- 1
- Pages
- 103-109
- ISSN
- 0264-6021 (ISSN-L)
- PMC
- PMC1186209
- OpenAlex
- W1717442359
- Cited by
- 209
- References
- 33
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 2 · 2023: 2 · 2022: 3 · 2021: 1 · 2020: 3 · 2019: 4 · 2018: 5 · 2017: 5 · 2016: 3 · 2015: 1 · 2014: 2 · 2012: 1
- FWCI
- 9.03
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Health Sciences › Medicine › Hepatology › Liver physiology and pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- plasma clearance, Kupffer cells, mannose, N-acetylglucosamine, glycoproteins, beta-glucuronidase, N-acetyl-beta-D-glucosaminidase, ribonuclease B, lysosomal enzymes, enzyme degradation, liver
- MeSH terms
- Acetylglucosamine, Acetylglucosaminidase, Animals, Female, Glucuronidase, Glycoproteins, Ligands, Liver, Lysosomes, Mannose, Orosomucoid, Ribonucleases, Rats
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