Cited by 421Alkaline Phosphatase Research StudiesBone and Dental Protein StudiesBiochemical and Molecular Research

The DOI matches its Crossref record; 91 of the 91 references it cites were found in a registry or an index.

Mammalian Alkaline Phosphatases: From Biology to Applications in Medicine and Biotechnology

Millán, José Luis·2006·Wiley eBooks

Open this paper in CoChat — free account

Abstract

PART I: GENE AND PROTEIN STRUCTURE 1 Gene Structure 2 Developmental Expression 3 Gene Regulation 4 Protein Structure and Functional Domains 5 Enzymatic Properties 6 Epitope Maps PART II: IN VIVO FUNCTIONS 7 The In Vivo Role of TNAP 8 Knockout Mouse Models PART III: AP EXPRESSION IN HEALTH AND DISEASE 9 APs as Physiological and Disease Markers 10 Neoplastic Expression of PLAP, GCAP, IAP (Regan, Nagao, Kasahara) and TNAP Isozymes PART IV: USES OF APS IN INDUSTRY AND BIOTECHNOLOGY 11 Applications of Recombinant APs 12 Use of APs in Prodrug Converting Strategies 13 APs as Therapeutic Agents 14 APs in the Food Industry 15 Veterinary Uses of AP Determinations 16 Methodologies

Integrity signals

Registry

Crossref · 10.1002/3527608060

Cites

91 of 91 references verified0 citation errors · 0 not checkable

Statistics

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

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

The nature of the chemical bond—1992
Pauling, L. C. (1992) · Journal of Chemical Education · doi:10.1021/ed069p519 · Cited by 13,235
Microdetermination of Phosphorus
Chen, P. S., Toribara, T. Y., & Warner, H. R. (1956) · Analytical Chemistry · doi:10.1021/ac60119a033 · Cited by 7,200
Catalysis in chemistry and enzymology
Jencks, W. P. (1969) · Medical Entomology and Zoology · Cited by 3,217
Histochemistry of Hepatic Phosphatases at a Physiologic pH: With Special Reference to the Demonstration of Bile Canaliculi
Wachstein, M., & Meisel, E. (1957) · American Journal of Clinical Pathology · doi:10.1093/ajcp/27.1.13 · Cited by 1,810
Estimation of Plasma Phosphatase by Determination of Hydrolysed Phenol with Amino-antipyrine
Kind, P. R., & King, E. J. (1954) · Journal of Clinical Pathology · doi:10.1136/jcp.7.4.322 · Cited by 1,658
Coupling of enzymes to proteins with glutaraldehyde
Avraméas, S. (1969) · Immunochemistry · doi:10.1016/0019-2791(69)90177-3 · Cited by 1,441
A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. Coli I. Purification and characterization of alkaline phosphatase
Garen, A., & Levinthal, C. (1960) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(60)91282-8 · Cited by 1,401
A new micromethod for the colorimetric determination of inorganic phosphate
Itaya, K., & Ui, M. (1966) · Clinica Chimica Acta · doi:10.1016/0009-8981(66)90114-8 · Cited by 829
Microtechnical Demonstration of Phosphatase in Tissue Sections.
Gömöri, G. (1939) · Experimental Biology and Medicine · doi:10.3181/00379727-42-10786 · Cited by 742
The Catalytic and Regulatory Properties of Enzymes
Koshland, D. E., & Neet, K. (1968) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.37.070168.002043 · Cited by 610

Flagged first, then by citations

Show all 91 references

Sorted by citations

Nucleotide- and nucleoside-converting ectoenzymes: Important modulators of purinergic signalling cascade
Yegutkin, G. G. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.01.024 · Cited by 1,155
Cellular function and molecular structure of ecto-nucleotidases
Zimmermann, H., Zebisch, M., & Sträter, N. (2012) · Purinergic Signalling · doi:10.1007/s11302-012-9309-4 · Cited by 985
Intestinal Alkaline Phosphatase Detoxifies Lipopolysaccharide and Prevents Inflammation in Zebrafish in Response to the Gut Microbiota
Bates, J. M., Akerlund, J., Mittge, E., & Guillemin, K. J. (2007) · Cell Host & Microbe · doi:10.1016/j.chom.2007.10.010 · Cited by 752
The Mechanism of Mineralization and the Role of Alkaline Phosphatase in Health and Disease
Orimo, H. (2010) · Journal of Nippon Medical School · doi:10.1272/jnms.77.4 · Cited by 719
Alkaline Phosphatases
Millán, J. L. (2006) · Purinergic Signalling · doi:10.1007/s11302-005-5435-6 · Cited by 610
Self-citation
Enzyme-Replacement Therapy in Life-Threatening Hypophosphatasia
Whyte, M. P., Greenberg, C. R., Salman, N., Bober, M. B., McAlister, W. H., Wenkert, D., Sickle, B. J. V., Simmons, J. H., Edgar, T. S., Bauer, M. L., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1106173 · Cited by 564
Self-citation
The Utilization of Inorganic and Organic Phosphorous Compounds as Nutrients by Eukaryotic Microalgae: A Multidisciplinary Perspective: Part I
Cembella, A. D., Antia, N. J., & Harrison, P. J. H. (1982) · CRC Critical Reviews in Microbiology · doi:10.3109/10408418209113567 · Cited by 538
Hypophosphatasia — aetiology, nosology, pathogenesis, diagnosis and treatment
Whyte, M. P. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.14 · Cited by 510
Alkaline Phosphatase and Hypophosphatasia
Millán, J. L., & Whyte, M. P. (2015) · Calcified Tissue International · doi:10.1007/s00223-015-0079-1 · Cited by 398
Self-citation
The Role of Phosphatases in the Initiation of Skeletal Mineralization
Millán, J. L. (2012) · Calcified Tissue International · doi:10.1007/s00223-012-9672-8 · Cited by 378
Self-citation
Physiological role of alkaline phosphatase explored in hypophosphatasia
Whyte, M. P. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05387.x · Cited by 362
Integrating Enzymatic Self-Assembly and Mitochondria Targeting for Selectively Killing Cancer Cells without Acquired Drug Resistance
Wang, H., Feng, Z., Wang, Y., Zhou, R., Yang, Z., & Xu, B. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b09783 · Cited by 318
Alkaline phosphatase: a novel treatment target for cardiovascular disease in CKD
Haarhaus, M. L., Brandenburg, V. M., Kalantar‐Zadeh, K., Stenvinkel, P., & Magnusson, P. (2017) · Nature Reviews Nephrology · doi:10.1038/nrneph.2017.60 · Cited by 316
Upregulation of alkaline phosphatase and pyrophosphate hydrolysis: Potential mechanism for uremic vascular calcification
Lomashvili, K. A., Garg, P. K., Narisawa, S., Millán, J. L., & O'Neill, W. C. (2008) · Kidney International · doi:10.1038/ki.2008.26 · Cited by 311
Self-citation
Enzymes involved in metabolism of extracellular nucleotides and nucleosides: Functional implications and measurement of activities
Yegutkin, G. G. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2014.953627 · Cited by 299
Hypophosphatasia
Mornet, É. (2007) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-2-40 · Cited by 276
Derivation of Primordial Germ Cells from Human Embryonic and Induced Pluripotent Stem Cells Is Significantly Improved by Coculture with Human Fetal Gonadal Cells
Park, T. S., Galić, Z., Conway, A. E., Lindgren, A., Handel, B. V., Magnusson, M., Richter, L., Teitell, M. A., Mikkola, H. K. A., Lowry, W. E., et al. (2009) · Stem Cells · doi:10.1002/stem.13 · Cited by 266
Enzyme Replacement Therapy for Murine Hypophosphatasia
Millán, J. L., Narisawa, S., Lemire, I., Loisel, T. P., Boileau, G., Léonard, P., Gramatikova, S. I., Terkeltaub, R. A., Pleshko, N. L., McKee, M. D., et al. (2007) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.071213 · Cited by 262
Self-citation
Enzyme-Instructed Self-Assembly of Small d -Peptides as a Multiple-Step Process for Selectively Killing Cancer Cells
Zhou, J., Du, X., Yamagata, N., & Xu, B. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b13541 · Cited by 244
Hypophosphatasia: An overview For 2017
Whyte, M. P. (2017) · Bone · doi:10.1016/j.bone.2017.02.011 · Cited by 252
Loss of skeletal mineralization by the simultaneous ablation of PHOSPHO1 and alkaline phosphatase function: A unified model of the mechanisms of initiation of skeletal calcification
Yadav, M. C., Simão, A. M., Narisawa, S., Huesa, C., McKee, M. D., Farquharson, C., & Millán, J. L. (2010) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.195 · Cited by 237
Self-citation
Real-time Ratiometric Fluorescent Assay for Alkaline Phosphatase Activity with Stimulus Responsive Infinite Coordination Polymer Nanoparticles
Deng, J., Yu, P., Wang, Y., & Mao, L. (2015) · Analytical Chemistry · doi:10.1021/ac504773n · Cited by 237
Enzymatic Noncovalent Synthesis
He, H., Tan, W., Guo, J., Yi, M., Shy, A. N., & Xu, B. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00306 · Cited by 225
Rationale for Design of Biologically Reversible Drug Derivatives: Prodrugs
Sinkula, A. A., & Yalkowsky, S. H. (1975) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.2600640203 · Cited by 222
Nanocomposite chitosan film containing graphene oxide/hydroxyapatite/gold for bone tissue engineering
Prakash, J., Prema, D., Venkataprasanna, K. S., Balagangadharan, K., Selvamurugan, N., & Venkatasubbu, G. D. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.03.095 · Cited by 218
Carbon Quantum Dots-Based Recyclable Real-Time Fluorescence Assay for Alkaline Phosphatase with Adenosine Triphosphate as Substrate
Qian, Z., Chai, L., Tang, C., Huang, Y., Chen, J., & Feng, H. X. (2015) · Analytical Chemistry · doi:10.1021/ac504519b · Cited by 207
Novel Inhibitors of Alkaline Phosphatase Suppress Vascular Smooth Muscle Cell Calcification
Narisawa, S., Harmey, D., Yadav, M. C., O'Neill, W. C., Hoylaerts, M., & Millán, J. L. (2007) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.070714 · Cited by 206
Self-citation
Multisystemic Functions of Alkaline Phosphatases
Buchet, R., Millán, J. L., & Magne, D. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-562-0_3 · Cited by 200
Self-citation
Inhibition of dsDNA-Templated Copper Nanoparticles by Pyrophosphate as a Label-Free Fluorescent Strategy for Alkaline Phosphatase Assay
Zhang, L., Zhao, J., Duan, M., Zhang, H., Jiang, J., & Yu, R. (2013) · Analytical Chemistry · doi:10.1021/ac4001942 · Cited by 194
Calmodulin-stimulated dephosphorylation of p-nitrophenyl phosphate and free phosphotyrosine by calcineurin.
Pallen, C. J., & Wang, J. H.-C. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32091-x · Cited by 194
Versatile and Amplified Biosensing through Enzymatic Cascade Reaction by Coupling Alkaline Phosphatase in Situ Generation of Photoresponsive Nanozyme
Jin, L.-Y., Dong, Y., Wu, X., Cao, G.-X., & Wang, G. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b02728 · Cited by 177
Asfotase alfa therapy for children with hypophosphatasia
Whyte, M. P., Madson, K. L., Phillips, D., Reeves, A. L., McAlister, W. H., Yakimoski, A., Mack, K. E., Hamilton, K., Kagan, K., Fujita, K. P., et al. (2016) · JCI Insight · doi:10.1172/jci.insight.85971 · Cited by 175
Intestinal alkaline phosphatase. Physical properties and quaternary structure
Fosset, M., Chappelet, D., & Lazdunski, M. (1974) · Biochemistry · doi:10.1021/bi00706a001 · Cited by 174
Enzyme-Instructed Self-Assembly for Spatiotemporal Profiling of the Activities of Alkaline Phosphatases on Live Cells
Zhou, J., Du, X., Berciu, C., He, H., Shi, J., Nicastro, D., & Xu, B. (2016) · Chem · doi:10.1016/j.chempr.2016.07.003 · Cited by 174
ATP and Adenosine Metabolism in Cancer: Exploitation for Therapeutic Gain
Yegutkin, G. G., & Boison, D. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000528 · Cited by 179
Structure of alkaline phosphatases
Kim, E. E., & Wyckoff, H. W. (1990) · Clinica Chimica Acta · doi:10.1016/0009-8981(90)90035-q · Cited by 171
A gold nanoparticles-based colorimetric assay for alkaline phosphatase detection with tunable dynamic range
Li, C. M., Zhen, S. J., Wang, J., Li, Y. F., & Huang, C. Z. (2012) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2012.12.015 · Cited by 161
Glucosamine hydrochloride functionalized tetraphenylethylene: A novel fluorescent probe for alkaline phosphatase based on the aggregation-induced emission
Chen, Q., Bian, N., Cao, C., Qiu, X., Qi, A., & Han, B. (2010) · Chemical Communications · doi:10.1039/c002894k · Cited by 162
Enzyme-Instructed Peptide Assemblies Selectively Inhibit Bone Tumors
Feng, Z., Han, X., Wang, H., Tang, T., & Xu, B. (2019) · Chem · doi:10.1016/j.chempr.2019.06.020 · Cited by 160
Functional interactions of lipids and proteins in rat intestinal microvillus membranes
Brasitus, T. A., Schachter, D., & Mamouneas, T. G. (1979) · Biochemistry · doi:10.1021/bi00586a013 · Cited by 159
Osteopontin regulates dentin and alveolar bone development and mineralization
Foster, B. L., Ao, M., Salmon, C. R., Chavez, M. B., Kolli, T. N., Tran, A. B., Chu, E. Y., Kantovitz, K. R., Yadav, M. C., Narisawa, S., et al. (2017) · Bone · doi:10.1016/j.bone.2017.12.004 · Cited by 155
Self-citation
Kinetic analysis of substrate utilization by native and TNAP-, NPP1-, or PHOSPHO1-deficient matrix vesicles
Ciancaglini, P., Yadav, M. C., Simão, A. M., Narisawa, S., Pizauro, J. M., Farquharson, C., Hoylaerts, M., & Millán, J. L. (2009) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.091023 · Cited by 154
Self-citation
Alkaline Phosphatase, an Unconventional Immune Protein
Rader, B. A. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00897 · Cited by 152
Fluorometric measurement of alkaline phosphatase activity in algae
Healey, F. P., & Hendzel, L. L. (1979) · Freshwater Biology · doi:10.1111/j.1365-2427.1979.tb01527.x · Cited by 150
Electrochemically generated green-fluorescent N-doped carbon quantum dots for facile monitoring alkaline phosphatase activity based on the Fe3+-mediating ON-OFF-ON-OFF fluorescence principle
Niu, F., Ying, Y., Hua, X., Niu, Y., Xu, Y., & Long, Y. (2017) · Carbon · doi:10.1016/j.carbon.2017.10.097 · Cited by 145
Inorganic polymeric phosphate/polyphosphate as an inducer of alkaline phosphatase and a modulator of intracellular Ca2+ level in osteoblasts (SaOS-2 cells) in vitro
Müller, W. E. G., Wang, X., Diehl‐Seifert, B., Kropf, K., Schloßmacher, U., Lieberwirth, I., Glaßer, G., Wiens, M., & Schröder, H. C. (2011) · Acta Biomaterialia · doi:10.1016/j.actbio.2011.03.007 · Cited by 144
Hypophosphatasia: Nonlethal disease despite skeletal presentation in utero (17 new cases and literature review)
Wenkert, D., McAlister, W. H., Coburn, S. P., Zerega, J., Ryan, L. M., Ericson, K. L., Hersh, J. H., Mumm, S. R., & Whyte, M. P. (2011) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.454 · Cited by 144
Impact of Ectoenzymes on P2 and P1 Receptor Signaling
Kukulski, F., Lévesque, S. A., & Sévigny, J. (2011) · Advances in pharmacology · doi:10.1016/b978-0-12-385526-8.00009-6 · Cited by 143
The Rachitic Tooth
Foster, B. L., Nociti, F. H., & Somerman, M. J. (2014) · Endocrine Reviews · doi:10.1210/er.2013-1009 · Cited by 155
Probing Biocatalytic Transformations with Luminescent DNA/Silver Nanoclusters
Liu, X., Wang, F., Niazov‐Elkan, A., Guo, W., & Willner, I. (2012) · Nano Letters · doi:10.1021/nl304283c · Cited by 137
5'-Nucleotidase from rat heart
Naito, Y., & Lowenstein, J. M. (1981) · Biochemistry · doi:10.1021/bi00521a014 · Cited by 135
A conjugated polyelectrolyte-based fluorescence sensor for pyrophosphate
Zhao, X., Liu, Y. J., & Schanze, K. S. (2007) · Chemical Communications · doi:10.1039/b706629e · Cited by 134
Enzyme Replacement Therapy Prevents Dental Defects in a Model of Hypophosphatasia
McKee, M. D., Nakano, Y., Masica, D. L., Gray, J. J., Lemire, I., Heft, R., Whyte, M. P., Crine, P., & Millán, J. L. (2011) · Journal of Dental Research · doi:10.1177/0022034510393517 · Cited by 128
Self-citation
Intestinal alkaline phosphatase. Catalytic properties and half of the sites reactivity
Chappelet, D., Fosset, M., Iwatsubo, M., Gache, C., & Lazdunski, M. (1974) · Biochemistry · doi:10.1021/bi00706a002 · Cited by 125
Bone Alkaline Phosphatase and Tartrate-Resistant Acid Phosphatase: Potential Co-regulators of Bone Mineralization
Linder, C. H., Ek‐Rylander, B., Krumpel, M., Norgård, M., Narisawa, S., Millán, J. L., Andersson, G. N., & Magnusson, P. (2017) · Calcified Tissue International · doi:10.1007/s00223-017-0259-2 · Cited by 124
Self-citation
A fluorometric assay for alkaline phosphatase activity based on β-cyclodextrin-modified carbon quantum dots through host-guest recognition
Tang, C., Qian, Z., Huang, Y., Xu, J., Ao, H., Zhao, M., Zhou, J., Chen, J., & Feng, H. X. (2016) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2016.04.047 · Cited by 121
Bone alkaline phosphatase: An important biomarker in chronic kidney disease – mineral and bone disorder
Nizet, A., Cavalier, E., Stenvinkel, P., Haarhaus, M. L., & Magnusson, P. (2019) · Clinica Chimica Acta · doi:10.1016/j.cca.2019.11.012 · Cited by 119
Effects of calf intestinal alkaline phosphatase, phosphatase inhibitors, and phosphorylated compounds on the rate of activation of glucocorticoid-receptor complexes
Barnett, C. A., Schmidt, T. J., & Litwack, G. (1980) · Biochemistry · doi:10.1021/bi00564a046 · Cited by 115
Nucleic Acid-Regulated Perylene Probe-Induced Gold Nanoparticle Aggregation: A New Strategy for Colorimetric Sensing of Alkaline Phosphatase Activity and Inhibitor Screening
Jiao, H., Chen, J., Li, W., Wang, F., Zhou, H., Li, Y., & Yu, C. (2014) · ACS Applied Materials & Interfaces · doi:10.1021/am405020b · Cited by 114
Cysteine-directed fluorescent gold nanoclusters for the sensing of pyrophosphate and alkaline phosphatase
Chen, Y., Li, W., Wang, Y., Yang, X., Chen, J., Jiang, Y., Yu, C., & Lin, Q. (2014) · Journal of Materials Chemistry C · doi:10.1039/c4tc00173g · Cited by 113
A New Intrinsic Thermal Parameter for Enzymes Reveals True Temperature Optima
Peterson, M. E., Eisenthal, R., Danson, M. J., Spence, A., & Daniel, R. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309143200 · Cited by 112
Tooth root dentin mineralization defects in a mouse model of hypophosphatasia
Foster, B., Nagatomo, K. J., Tso, H., Tran, A. T., Nociti, F. H., Narisawa, S., Yadav, M., McKee, M. D., Millán, J. L., & Somerman, M. (2012) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.1767 · Cited by 108
Self-citation
The role of tissue-nonspecific alkaline phosphatase in the phosphate-induced activation of alkaline phosphatase and mineralization in SaOS-2 human osteoblast-like cells
Orimo, H., & Shimada, T. (2008) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-008-9788-3 · Cited by 107
Discovery and Validation of a Series of Aryl Sulfonamides as Selective Inhibitors of Tissue-Nonspecific Alkaline Phosphatase (TNAP)
Dahl, R. S., Sergienko, E. A., Su, Y., Mostofi, Y. S., Yang, L., Simão, A. M., Narisawa, S., Brown, B. T., Mangravita-Novo, A., Vicchiarelli, M., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900383s · Cited by 107
Self-citation
Tissue-nonspecific alkaline phosphatase deficiency causes abnormal craniofacial bone development in the Alpl−/− mouse model of infantile hypophosphatasia
Jin, L., Nam, H. K., Campbell, C. R., Gasque, K. C. D. S., Millán, J. L., & Hatch, N. E. (2014) · Bone · doi:10.1016/j.bone.2014.06.040 · Cited by 99
Self-citation
Alpl prevents bone ageing sensitivity by specifically regulating senescence and differentiation in mesenchymal stem cells
Liu, W., Zhang, L., Xuan, K., Hu, C., Liu, S., Liao, L., Li, B., Jin, F., Shi, S., & Jin, Y. J. (2018) · Bone Research · doi:10.1038/s41413-018-0029-4 · Cited by 100
Regulated phosphorylation and dephosphorylation of GAL4, a transcriptional activator.Preprint
Mylin, L. M., Bhat, J. P., & Hopper, J. E. (1989) · Genes & Development · doi:10.1101/gad.3.8.1157 · Cited by 92
Transgenic Overexpression of Tissue‐Nonspecific Alkaline Phosphatase (TNAP) in Vascular Endothelium Results in Generalized Arterial Calcification
Savinov, A. Y., Salehi, M., Yadav, M. C., Radichev, I., Millán, J. L., & Savinova, O. V. (2015) · Journal of the American Heart Association · doi:10.1161/jaha.115.002499 · Cited by 95
Self-citation
Rapid and Reliable Detection of Alkaline Phosphatase by a Hot Spots Amplification Strategy Based on Well-Controlled Assembly on Single Nanoparticle
Zeng, Y., Ren, J., Wang, S., Mai, J.-M., Qu, B., Zhang, Y., Shen, A., & Hu, J. (2017) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.7b09336 · Cited by 94
History of ectonucleotidases and their role in purinergic signaling
Zimmermann, H. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114322 · Cited by 93
Clinical and Radiographic Findings in Adults With Persistent Hypophosphatasemia
McKiernan, F. E., Berg, R. L., & Fuehrer, J. T. (2014) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.2178 · Cited by 92
Regulating the Rate of Molecular Self‐Assembly for Targeting Cancer Cells
Zhou, J., Du, X., & Xu, B. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201600753 · Cited by 91
Enzymatically Formed Peptide Assemblies Sequestrate Proteins and Relocate Inhibitors to Selectively Kill Cancer Cells
He, H., Liu, S., Wu, D., & Xu, B. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202006290 · Cited by 90
Enzyme replacement prevents enamel defects in hypophosphatasia mice
Yadav, M. C., de Oliveira, R. C., Foster, B. L., Fong, H. K., Cory, E., Narisawa, S., Sah, R. L., Somerman, M. J., Whyte, M. P., & Millán, J. L. (2012) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.1619 · Cited by 90
Self-citation
Soluble Ecto-5′-nucleotidase (5′-NT), Alkaline Phosphatase, and Adenosine Deaminase (ADA1) Activities in Neonatal Blood Favor Elevated Extracellular Adenosine
Pettengill, M. A., Robson, S. C., Tresenriter, M., Millán, J. L., Usheva, A., Bingham, T. C., Belderbos, M. E., Bergelson, I., Burl, S., Kampmann, B., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.484212 · Cited by 89
Self-citation
Tissue-Nonspecific Alkaline Phosphatase Acts Redundantly with PAP and NT5E to Generate Adenosine in the Dorsal Spinal Cord
Street, S. E., Kramer, N. J., Walsh, P. L., Taylor‐Blake, B., Yadav, M. C., King, I. F. G., Vihko, P., Wightman, R. M., Millán, J. L., & Zylka, M. J. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.0133-13.2013 · Cited by 87
Self-citation
Phosphate transport across renal cortical brush border membrane vesicles from rats stabilized on a normal, high or low phosphate diet
Kempson, S. A., & Dousa, T. P. (1979) · Life Sciences · doi:10.1016/0024-3205(79)90337-0 · Cited by 87
Switchable fluorescence of gold nanoclusters for probing the activity of alkaline phosphatase and its application in immunoassay.
Hu, X., Wu, X.-M., Fang, X.-X., Li, Z.-J., & Wang, G.-L. (2016) · Biosensors & bioelectronics · doi:10.1016/j.bios.2015.10.046 · Cited by 78
Design and synthesis of pyrazole derivatives as potent and selective inhibitors of tissue-nonspecific alkaline phosphatase (TNAP)
Sidique, S., Ardecky, R., Su, Y., Narisawa, S., Brown, B. T., Millán, J. L., Sergienko, E. A., & Cosford, N. D. P. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.10.107 · Cited by 87
Self-citation
Calcium and calmodulin-dependent phosphorylation of a 62 kd protein induces microtubule depolymerization in sea urchin mitotic apparatuses
Dinsmore, J., & Sloboda, R. D. (1988) · Cell · doi:10.1016/0092-8674(88)90094-3 · Cited by 86
Targeting Metabolism of Extracellular Nucleotides via Inhibition of Ectonucleotidases CD73 and CD39
Jeffrey, J. L., Lawson, K. V., & Powers, J. P. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01044 · Cited by 85
A Review of Phosphate Mineral Nucleation in Biology and Geobiology
Omelon, S., Ariganello, M., Bonucci, E., Grynpas, M., & Nanci, A. (2013) · Calcified Tissue International · doi:10.1007/s00223-013-9784-9 · Cited by 85
The Physiological and Pathological Role of Tissue Nonspecific Alkaline Phosphatase beyond Mineralization
Sekaran, S., Vimalraj, S., & Thangavelu, L. P. (2021) · Biomolecules · doi:10.3390/biom11111564 · Cited by 90
Near-infrared fluorescence probe for the determination of alkaline phosphatase
Liu, S., Pang, S., Na, W., & Su, X. (2013) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2013.12.023 · Cited by 81
Enzymic hydrolysis of phosphonate esters. Reaction mechanism of intestinal 5'-nucleotide phosphodiesterase
Kelly, S. J., & Butler, L. G. (1977) · Biochemistry · doi:10.1021/bi00625a011 · Cited by 79
ATP and acetylcholine, equal brethren.
Zimmermann, H. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2007.09.004 · Cited by 83
PURIFICATION AND PROPERTIES OF BRAIN ALKALINE PHOSPHATASE
Dorai, D. T., & Bachhawat, B. K. (1977) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1977.tb10699.x · Cited by 79
Overview of Optical and Electrochemical Alkaline Phosphatase (ALP) Biosensors: Recent Approaches in Cells Culture Techniques
Balbaied, T., & Moore, E. (2019) · Biosensors · doi:10.3390/bios9030102 · Cited by 76
Hypophosphatasia: clinical manifestation and burden of disease in adult patients
Conti, F. (2017) · Clinical cases in mineral and bone metabolism · doi:10.11138/ccmbm/2017.14.1.230 · Cited by 75
Pulsed Low Intensity Ultrasound Enhances Mineralisation in Preosteoblast Cells
Unsworth, J., Kaneez, S., Harris, S., Ridgway, J. N., Fenwick, S., Chenery, D. H., & Harrison, A. J. (2007) · Ultrasound in Medicine & Biology · doi:10.1016/j.ultrasmedbio.2006.12.003 · Cited by 74
Phosphate: Known and potential roles during development and regeneration of teeth and supporting structures
Foster, B. L., Tompkins, K. A., Rutherford, R. B., Zhang, H., Chu, E. Y., Fong, H. K., & Somerman, M. J. (2008) · Birth Defects Research Part C Embryo Today Reviews · doi:10.1002/bdrc.20136 · Cited by 78
Chronic Recurrent Multifocal Osteomyelitis Mimicked in Childhood Hypophosphatasia
Whyte, M. P., Wenkert, D., McAlister, W. H., Zulf Mughal, M., Freemont, A. J., Whitehouse, R. W., Baildam, E. M., Coburn, S. P., Ryan, L. M., & Mumm, S. R. (2009) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.090308 · Cited by 74
Artificial Intracellular Filaments
Feng, Z., Wang, H., Wang, F., Oh, Y., Berciu, C., Cui, Q., Egelman, E. H., & Xu, B. (2020) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2020.100085 · Cited by 74
Interactions between CD36 and global intestinal alkaline phosphatase in mouse small intestine and effects of high-fat diet
Lynes, M. D., Narisawa, S., Millán, J. L., & Widmaier, E. P. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00235.2011 · Cited by 73
Self-citation
Extracellular matrix mineralization in periodontal tissues: Noncollagenous matrix proteins, enzymes, and relationship to hypophosphatasia and X‐linked hypophosphatemia
McKee, M. D., Hoac, B., Addison, W. N., Barros, N. M. T., Millán, J. L., & Chaussain, C. (2013) · Periodontology 2000 · doi:10.1111/prd.12029 · Cited by 73
Self-citation
Hypophosphatasia
Whyte, M. P. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-373884-4.00080-x · Cited by 71
Catalytic Signature of a Heat-Stable, Chimeric Human Alkaline Phosphatase with Therapeutic Potential
Kiffer-Moreira, T., Sheen, C. R., Gasque, K. C. D. S., Bolean, M., Ciancaglini, P., van Elsas, A., Hoylaerts, M., & Millán, J. L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089374 · Cited by 71
Self-citation
Biological stenciling of mineralization in the skeleton: Local enzymatic removal of inhibitors in the extracellular matrix
Reznikov, N., Hoac, B., Buss, D. J., Addison, W. N., Barros, N. M. T., & McKee, M. D. (2020) · Bone · doi:10.1016/j.bone.2020.115447 · Cited by 69
Enzyme-Instructed Intracellular Peptide Assemblies
Liu, Z., Guo, J., Qiao, Y., & Xu, B. (2023) · Accounts of Chemical Research · doi:10.1021/acs.accounts.3c00542 · Cited by 70
Hypophosphatasia: A Unique Disorder of Bone Mineralization
Villa-Suárez, J. M., García‐Fontana, C., Andújar-Vera, F., González-Salvatierra, S., de Haro-Muñoz, T., Contreras-Bolívar, V., García-Fontana, B., & Muñoz‐Torres, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094303 · Cited by 69

Authors: Millán, J. L.
Venue: Wiley eBooks
Publisher: Wiley
Published: 2006-01-09
DOI: 10.1002/3527608060
OpenAlex: W625374770
Cited by: 421
References: 91
Citations by year: 2026: 4 · 2025: 5 · 2024: 4 · 2023: 4 · 2022: 8 · 2021: 17 · 2020: 31 · 2019: 31 · 2018: 20 · 2017: 24 · 2016: 23 · 2015: 30 · 2014: 24 · 2013: 23 · 2012: 14
FWCI: 32.05
Type: book
Language: en
Open access: closed
Licence: doi.wiley.com/10.1002/tdm_license_1.1 (tdm)
Locations: Wiley eBooks (publishedVersion)
Topics: Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Alkaline Phosphatase Research Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Bone and Dental Protein Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Keywords: tissue-nonspecific alkaline phosphatase, placental alkaline phosphatase, GCAP, IAP, isozymes, gene structure, developmental gene expression, gene expression regulation, protein structure, enzyme properties, epitope mapping, knockout mouse models, disease markers, prodrug activation, therapeutic enzymes, food industry applications, veterinary diagnostics

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

Mammalian Alkaline Phosphatases: From Biology to Applications in Medicine and Biotechnology

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks