Lysosomal acidification mechanisms

Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology

Forgac, M. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2272 · Cited by 1,626 · see citing works

X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity

Dutzler, R., Campbell, E., Cadene, M., Chait, B., & MacKinnon, R. (2002) · Nature · doi:10.1038/415287a · Cited by 1,567 · see citing works

AN INTRODUCTION TO TRP CHANNELS

Ramsey, I. S., Delling, M., & Clapham, D. E. (2005) · Annual Review of Physiology · doi:10.1146/annurev.physiol.68.040204.100431 · Cited by 1,549 · see citing works

Pannexin‐1 mediates large pore formation and interleukin‐1β release by the ATP‐gated P2X7 receptor

Pelegrı́n, P., & Surprenant, A. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601378 · Cited by 1,428 · see citing works

Loss of the ClC-7 Chloride Channel Leads to Osteopetrosis in Mice and Man

Kornak, U., Kasper, D., Bösl, M. R., Kaiser, E., Schweizer, M., Schulz, A., Friedrich, W., Delling, G., & Jentsch, T. J. (2001) · Cell · doi:10.1016/s0092-8674(01)00206-9 · Cited by 995 · see citing works

Gating the Selectivity Filter in ClC Chloride Channels

Dutzler, R., Campbell, E., & MacKinnon, R. (2003) · Science · doi:10.1126/science.1082708 · Cited by 783 · see citing works

Mammalian cell-cycle regulation: several Cdks, numerous cyclins and diverse compensatory mechanisms

Satyanarayana, A., & Kaldis, P. (2009) · Oncogene · doi:10.1038/onc.2009.170 · Cited by 772 · see citing works

NAADP mobilizes calcium from acidic organelles through two-pore channels

Calcraft, P. J., Ruas, M., Pan, Z., Cheng, X., Arredouani, A., Hao, X., Tang, J., Rietdorf, K., Teboul, L., Chuang, K.-T., et al. (2009) · Nature · doi:10.1038/nature08030 · Cited by 760 · see citing works

The ABC protein turned chloride channel whose failure causes cystic fibrosis

Gadsby, D. C., Vergani, P., & Csanády, L. (2006) · Nature · doi:10.1038/nature04712 · Cited by 706 · see citing works

Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness

Karet, F. E., Finberg, K. E., Nelson, R. D., Nayır, A., Mocan, H. N., Sanjad, S. A., Rodríguez‐Soriano, J., Santos, F., Cremers, C. W. R. J., Pietro, A. D., et al. (1999) · Nature Genetics · doi:10.1038/5022 · Cited by 687 · see citing works

Secondary active transport mediated by a prokaryotic homologue of ClC Cl- channels

Accardi, A., & Miller, C. (2004) · Nature · doi:10.1038/nature02314 · Cited by 612 · see citing works

The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel

Dong, X., Cheng, X., Mills, E., Delling, M., Wang, F., Kurz, T., & Xu, H. (2008) · Nature · doi:10.1038/nature07311 · Cited by 572 · see citing works

ClC-5 Cl--channel disruption impairs endocytosis in a mouse model for Dent's disease

Piwon, N., Gunther, W. C., Schwake, M., Bösl, M. R., & Jentsch, T. J. (2000) · Nature · doi:10.1038/35042597 · Cited by 548 · see citing works

v-ATPase V0 subunit d2–deficient mice exhibit impaired osteoclast fusion and increased bone formation

Lee, S.-H., Rho, J., Jeong, D., Sul, J., Kim, T. S., Kim, N., Kang, J.-S., Miyamoto, T. K., Suda, T., Lee, S., et al. (2006) · Nature Medicine · doi:10.1038/nm1514 · Cited by 547 · see citing works

Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes

Jentsch, T. J., Steinmeyer, K., & Schwarz, G. (1990) · Nature · doi:10.1038/348510a0 · Cited by 520 · see citing works

CFTR regulates phagosome acidification in macrophages and alters bactericidal activity

Di, A., Brown, M. E., Deriy, L. V., Li, C., Szeto, F. L., Chen, Y., Huang, P. C., Tong, J., Naren, A. P., Bindokas, V. P., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1456 · Cited by 494 · see citing works

Defective acidification of intracellular organelles in cystic fibrosis

Barasch, J. M., Kiss, B., Prince, A. S., Saiman, L. M., Gruenert, D. C., & Al‐Awqati, Q. (1991) · Nature · doi:10.1038/352070a0 · Cited by 491 · see citing works

Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins

Scheel, O., Zdebik, A., Lourdel, S., & Jentsch, T. (2005) · Nature · doi:10.1038/nature03860 · Cited by 483 · see citing works

Disassembly and Reassembly of the Yeast Vacuolar H+-ATPase in Vivo

Kane, P. M. (1995) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46944-4 · Cited by 462 · see citing works

Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5

Picollo, A., & Pusch, M. (2005) · Nature · doi:10.1038/nature03720 · Cited by 454 · see citing works

ClC-5, the chloride channel mutated in Dent’s disease, colocalizes with the proton pump in endocytotically active kidney cells

Gunther, W. C., Lüchow, A., Cluzeaud, F., Vandewalle, A., & Jentsch, T. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.14.8075 · Cited by 431 · see citing works

Open-state substructure of single chloride channels from Torpedo electroplax

Miller, C. (1982) · Philosophical transactions of the Royal Society of London. Series B, Biological sciences · doi:10.1098/rstb.1982.0140 · Cited by 415 · see citing works

P2X7 Receptor Differentially Couples to Distinct Release Pathways for IL-1β in Mouse Macrophage

Pelegrı́n, P., Barroso-Gutierrez, C., & Surprenant, A. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.11.7147 · Cited by 413 · see citing works

CLC Chloride Channels and Transporters: From Genes to Protein Structure, Pathology and Physiology

Jentsch, T. J. (2008) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701829110 · Cited by 405 · see citing works

The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes

Graves, A. R., Curran, P. K., Smith, C. L., & Mindell, J. A. (2008) · Nature · doi:10.1038/nature06907 · Cited by 399 · see citing works

Identification and characterization of a proton pump on lysosomes by fluorescein-isothiocyanate-dextran fluorescence.

Ohkuma, S., Moriyama, Y., & Takano, T. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.9.2758 · Cited by 394 · see citing works

Regulation and Isoform Function of the V-ATPases

Toei, M., Saum, R., & Forgac, M. D. (2010) · Biochemistry · doi:10.1021/bi100397s · Cited by 393 · see citing works

Albers-Schonberg disease (autosomal dominant osteopetrosis, type II) results from mutations in the ClCN7 chloride channel gene

Cleiren, E. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.25.2861 · Cited by 376 · see citing works

Loss of the chloride channel ClC‐7 leads to lysosomal storage disease and neurodegeneration

Kasper, D., Planells‐Cases, R., Fuhrmann, J. C., Scheel, O., Zeitz, O., Rüether, K., Schmitt, A. M., Poët, M., Steinfeld, R., Schweizer, M., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600576 · Cited by 372 · see citing works

ClC-7 requires Ostm1 as a β-subunit to support bone resorption and lysosomal function

Lange, P. F., Wartosch, L., Jentsch, T. J., & Fuhrmann, J. C. (2006) · Nature · doi:10.1038/nature04535 · Cited by 342 · see citing works

STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p.

Manolson, M. F., Wu, B., Proteau, D., Taillon, B. E., Roberts, B. T., Hoyt, M. A., & Jones, E. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36755-8 · Cited by 319 · see citing works

Lectures on the Comparative Pathology of Inflammation.

Asherson, G. L. (1970) · Europe PMC (PubMed Central) · Cited by 284 · see citing works

A cation counterflux supports lysosomal acidification

Steinberg, B. E., Huynh, K. K., Brodovitch, A., Jabs, S., Stauber, T., Jentsch, T. J., & Grinstein, S. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200911083 · Cited by 280 · see citing works

Topography and subunit stoichiometry of the coated vesicle proton pump.

Arai, H., Terres, G., Pink, S., & Forgac, M. D. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68376-0 · Cited by 276 · see citing works

Activation of Microglia Acidifies Lysosomes and Leads to Degradation of Alzheimer Amyloid Fibrils

Majumdar, A., Cruz, D., Asamoah, N., Buxbaum, A., Sohar, I., Lobel, P., & Maxfield, F. R. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-10-0975 · Cited by 271 · see citing works

Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle

Feng, L., Campbell, E., Hsiung, Y.-C., & MacKinnon, R. (2010) · Science · doi:10.1126/science.1195230 · Cited by 270 · see citing works

The VPH1 gene encodes a 95-kDa integral membrane polypeptide required for in vivo assembly and activity of the yeast vacuolar H(+)-ATPase.

Manolson, M. F., Proteau, D., Preston, R. A., Stenbit, A. E., Roberts, B. T., Hoyt, M. A., Preuss, D., Mulholland, J., Botstein, D., & Jones, E. W. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49711-1 · Cited by 264 · see citing works

Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly

Seol, J. H., Shevchenko, A., Shevchenko, A., & Deshaies, R. J. (2001) · Nature Cell Biology · doi:10.1038/35070067 · Cited by 263 · see citing works

Digestive Activity of Lysosomes

Coffey, J. W., & Duve, C. D. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93301-6 · Cited by 262 · see citing works

Homodimeric architecture of a CIC-type chloride ion channel

Middleton, R. E., Pheasant, D. J., & Miller, C. (1996) · Nature · doi:10.1038/383337a0 · Cited by 252 · see citing works

Digestive Activity of Lysosomes

Fowler, S., & Duve, C. D. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94453-4 · Cited by 252 · see citing works

Lysosomal Pathology and Osteopetrosis upon Loss of H + -Driven Lysosomal Cl – Accumulation

Weinert, S., Jabs, S., Supanchart, C., Schweizer, M., Gimber, N., Richter, M., Rademann, J., Stauber, T., Kornak, U., & Jentsch, T. J. (2010) · Science · doi:10.1126/science.1188072 · Cited by 238 · see citing works

TRP-ML1 Regulates Lysosomal pH and Acidic Lysosomal Lipid Hydrolytic Activity

Soyombo, A. A., Tjon‐Kon‐Sang, S., Rbaibi, Y., Bashllari, E., Bisceglia, J., Muallem, S., & Kiselyov, K. I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508211200 · Cited by 235 · see citing works

Chloride Channel ClCN7 Mutations Are Responsible for Severe Recessive, Dominant, and Intermediate Osteopetrosis

Frattini, A., Pangrazio, A., Susani, L., Sobacchi, C., Mirolo, M., Abinun, M., Andolina, M., Flanagan, A. M., Horwitz, E. M., Mıhçı, E., et al. (2003) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.2003.18.10.1740 · Cited by 224 · see citing works

Lysosomal storage disease upon disruption of the neuronal chloride transport protein ClC-6

Poët, M., Kornak, U., Schweizer, M., Zdebik, A. A., Scheel, O., Hölter, S. M., Wurst, W., Schmitt, A., Fuhrmann, J. C., Planells‐Cases, R., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606137103 · Cited by 201 · see citing works

A voltage-gated anion channel from the electric organ of Torpedo californica.

White, M. M., & Miller, C. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86687-5 · Cited by 195 · see citing works

The RAVE Complex Is Essential for Stable Assembly of the Yeast V-ATPase

Smardon, A. M., Tarsio, M., & Kane, P. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200682200 · Cited by 183 · see citing works

ClC‐6 and ClC‐7 are two novel broadly expressed members of the CLC chloride channel family

Brandt, S., & Jentsch, T. J. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)01298-2 · Cited by 183 · see citing works

Structure and Regulation of Insect Plasma Membrane H+ V-ATPase

Wieczorek, H., Grüber, G., Harvey, W. R., Huss, M., Merzendorfer, H., & Zeiske, W. (2000) · Journal of Experimental Biology · doi:10.1242/jeb.203.1.127 · Cited by 178 · see citing works

ABC transporters: a riddle wrapped in a mystery inside an enigma

Jones, P. M., O’Mara, M. L., & George, A. M. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.06.004 · Cited by 178 · see citing works

The neurogenetics of mucolipidosis type IV

Altarescu, G., Sun, M., Moore, D. F., Smith, J. A., Wiggs, E. A., Solomon, B. I., Patronas, N. J., Frei, K. P., Gupta, S., Kaneski, C. R., et al. (2002) · Neurology · doi:10.1212/wnl.59.3.306 · Cited by 177 · see citing works

Subunit Rotation of Vacuolar-type Proton Pumping ATPase

Hirata, T., Iwamoto-Kihara, A., Sun‐Wada, G., Okajima, T., Wada, Y., & Futai, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302756200 · Cited by 168 · see citing works

Physical Interaction between Aldolase and Vacuolar H+-ATPase Is Essential for the Assembly and Activity of the Proton Pump

Lu, M., Ammar, D. A., Ives, H. E., Albrecht, F., & Gluck, S. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702598200 · Cited by 167 · see citing works

The lysosomal proton pump is electrogenic.

Harikumar, P., & Reeves, J. P. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44471-1 · Cited by 162 · see citing works

Mucolipin‐1 Is a Lysosomal Membrane Protein Required for Intracellular Lactosylceramide Traffic

Pryor, P. R., Reimann, F. M., Gribble, F. M., & Luzio, J. P. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00475.x · Cited by 156 · see citing works

Yeast V-ATPase Complexes Containing Different Isoforms of the 100-kDa a-subunit Differ in Coupling Efficiency and in VivoDissociation

Kawasaki-Nishi, S., Nishi, T., & Forgac, M. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010790200 · Cited by 155 · see citing works

Ionic Currents Mediated by a Prokaryotic Homologue of CLC Cl− Channels

Accardi, A., Kolmakova-Partensky, L., Williams, C., & Miller, C. (2004) · The Journal of General Physiology · doi:10.1085/jgp.200308935 · Cited by 145 · see citing works

Disease-causing mutations in the cystic fibrosis transmembrane conductance regulator determine the functional responses of alveolar macrophages

Deriy, L. V., Gomez, E. A., Zhang, G., Beacham, D. W., Hopson, J. A., Gallan, A. J., Shevchenko, P. D., Bindokas, V. P., & Nelson, D. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.057372 · Cited by 135 · see citing works

Chloride channelopathies

Planells‐Cases, R., & Jentsch, T. J. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.02.002 · Cited by 130 · see citing works

The Mechanochemistry of V-ATPase Proton Pumps

Grabe, M., Wang, H., & OSTER, G. F. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76823-8 · Cited by 126 · see citing works

Characterization of Osteoclasts from Patients Harboring a G215R Mutation in ClC-7 Causing Autosomal Dominant Osteopetrosis Type II

Henriksen, K., Gram, J., Schaller, S., Dahl, B. H., Dziegiel, M. H., Bollerslev, J., & Karsdal, M. A. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63712-1 · Cited by 124 · see citing works

The cystic fibrosis transmembrane regulator is present and functional in endosomes. Role as a determinant of endosomal pH.

Lukács, G. L., Chang, X. B., Kartner, N., Rotstein, O. D., Riordan, J. R., & Grinstein, S. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42078-9 · Cited by 120 · see citing works

Cystic Fibrosis Transmembrane Conductance Regulator-independent Phagosomal Acidification in Macrophages

Haggie, P. M., & Verkman, A. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705296200 · Cited by 119 · see citing works

Use of glycyl- l -phenylalanine 2-naphthylamide, a lysosome-disrupting cathepsin C substrate, to distinguish between lysosomes and prelysosomal endocytic vacuoles

Berg, T., STRØMHAUG, P. E., Løvdal, T., Seglen, P. O., & Berg, T. (1994) · Biochemical Journal · doi:10.1042/bj3000229 · Cited by 114 · see citing works

The Chloride Channel ClC-4 Contributes to Endosomal Acidification and Trafficking

Mohammad-Panah, R., Harrison, R. E., Dhani, S. U., Ackerley, C. A., Huan, L., Wang, Y., & Bear, C. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304357200 · Cited by 113 · see citing works

Comparative studies on the electrical properties of the H+ translocating ATPase and pyrophosphatase of the vacuolar‐lysosomal compartment.

Hedrich, R., Kurkdjian, A., Guern, J., & Flügge, U. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08430.x · Cited by 111 · see citing works

Elevated lysosomal pH in Mucolipidosis type IV cells

Bach, G., Chen, C.-S., & Pagano, R. E. (1999) · Clinica Chimica Acta · doi:10.1016/s0009-8981(98)00183-1 · Cited by 106 · see citing works

Degradation of Alzheimer's amyloid fibrils by microglia requires delivery of ClC-7 to lysosomes

Majumdar, A., Capetillo‐Zarate, E., Cruz, D. L., Gouras, G. K., & Maxfield, F. R. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-09-0745 · Cited by 106 · see citing works

Lysosomal pH and analysis of the counter ion pathways that support acidification

DiCiccio, J. E., & Steinberg, B. E. (2011) · The Journal of General Physiology · doi:10.1085/jgp.201110596 · Cited by 99 · see citing works

Lysosomal degradation of endocytosed proteins depends on the chloride transport protein ClC‐7

Wartosch, L., Fuhrmann, J. C., Schweizer, M., Stauber, T., & Jentsch, T. J. (2009) · The FASEB Journal · doi:10.1096/fj.09-130880 · Cited by 97 · see citing works

Evidence against Defective -Golgi Acidification in Cystic Fibrosis

Seksek, O., Biwersi, J., & Verkman, A. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.26.15542 · Cited by 95 · see citing works

TRP‐ML1 functions as a lysosomal NAADP‐sensitive Ca2+ release channel in coronary arterial myocytes

Zhang, F., Jin, S., Yi, F., & Li, P. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00486.x · Cited by 95 · see citing works

Degradation of fibrillar forms of Alzheimer's amyloid β-peptide by macrophages

Majumdar, A., Chung, H., Dolios, G., Wang, R., Asamoah, N., Lobel, P., & Maxfield, F. R. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.12.001 · Cited by 92 · see citing works

Evidence for an ATP-driven “proton pump” in rat liver lysosomes by basic dyes uptake

Dell’Antone, P. (1979) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(79)90398-x · Cited by 90 · see citing works

Rotation of the Proteolipid Ring in the V-ATPase

Yokoyama, K., Nakano, M., Imamura, H., Yoshida, M., & Tamakoshi, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303104200 · Cited by 90 · see citing works

Chloride channel 7 (CLCN7) gene mutations in intermediate autosomal recessive osteopetrosis

Campos‐Xavier, B., Saraiva, J., Ribeiro, L. M., Münnich, A., & Cormier‐Daire, V. (2003) · Human Genetics · doi:10.1007/s00439-002-0861-9 · Cited by 88 · see citing works

H+ ATPase of chromaffin granules. Kinetics, regulation, and stoichiometry.

Johnson, R. G., Beers, M. F., & Scarpa, A. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33879-1 · Cited by 83 · see citing works

RAVE Is Essential for the Efficient Assembly of the C Subunit with the Vacuolar H+-ATPase

Smardon, A. M., & Kane, P. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703627200 · Cited by 80 · see citing works

Acidification of rat liver lysosomes: quantitation and comparison with endosomes

Dyke, R. W. V. (1993) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1993.265.4.c901 · Cited by 77 · see citing works

Microtubules Are Involved in Glucose-dependent Dissociation of the Yeast Vacuolar [H+]-ATPase in Vivo

Xu, T., & Forgac, M. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100637200 · Cited by 76 · see citing works

Location of the binding site for chloride ion activation of cathepsin C

Cigić, B., & Pain, R. H. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00697.x · Cited by 73 · see citing works

Vacuolar H+-ATPase d2 Subunit

Smith, A. N., Jouret, F. C., Bord, S., Borthwick, K. J., Al‐Lamki, R. S., Wagner, C. A., Ireland, D. C., Cormier‐Daire, V., Frattini, A., VILLA, A. M., et al. (2005) · Journal of the American Society of Nephrology · doi:10.1681/asn.2004090761 · Cited by 72 · see citing works

Unimpaired Lysosomal Acidification in Respiratory Epithelial Cells in Cystic Fibrosis

Haggie, P. M., & Verkman, A. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809161200 · Cited by 69 · see citing works

Electrophysiological Analysis of the Yeast V-Type Proton Pump: Variable Coupling Ratio and Proton Shunt

Kettner, C., Bertl, A., Obermeyer, G., Slayman, C. L., & Bihler, H. J. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74789-4 · Cited by 61 · see citing works

Defective organellar acidification as a cause of cystic fibrosis lung disease: reexamination of a recurring hypothesis

Haggie, P. M., & Verkman, A. S. (2009) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00018.2009 · Cited by 59 · see citing works

Functional CFTR in endosomal compartment of CFTR-expressing fibroblasts and T84 cells

Biwersi, J., & Verkman, A. S. (1994) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1994.266.1.c149 · Cited by 59 · see citing works

Electrogenic Nature of Lysosomal Proton Pump as Revealed with a Cyanine Dye1

Ohkuma, S., Moriyama, Y., & Takano, T. (1983) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a134547 · Cited by 46 · see citing works

The Vacuolar H+-ATPase of Lemon Fruits Is Regulated by Variable H+/ATP Coupling and Slip

Müller, M. L., Jensen, M., & Taiz, L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.10706 · Cited by 46 · see citing works

Utilization of Genetically Altered Animals in the Pharmaceutical Industry

Rudmann, D. G., & Durham, S. K. (1999) · Toxicologic Pathology · doi:10.1177/019262339902700121 · Cited by 44 · see citing works

The lysosome or lysosome-related organelle may serve as a Ca2+ store in the boutons of hippocampal pyramidal cells

McGuinness, L., Bardo, S. J., & Emptage, N. J. (2006) · Neuropharmacology · doi:10.1016/j.neuropharm.2006.07.029 · Cited by 41 · see citing works

Polymorphisms in theCLCN7Gene Modulate Bone Density in Postmenopausal Women and in Patients with Autosomal Dominant Osteopetrosis Type II

Kornak, U., Ostertag, A., Branger, S., Bénichou, O., & de Vernejoul, M. C. (2006) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2005-2017 · Cited by 39 · see citing works

The lysosomal H+ pump: 8-azido-ATP inhibition and the role of chloride in H+ transport

Cuppoletti, J., Aures-Fischer, D., & Sachs, G. M. (1987) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(87)90409-3 · Cited by 25 · see citing works

Reversal of the Red Beet Tonoplast H+-ATPase by a Pyrophosphate-Generated Proton Electrochemical Gradient

Schmidt, A., & Briskin, D. P. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1530 · Cited by 13 · see citing works

Targeted Drug Delivery with Polymers and Magnetic Nanoparticles: Covalent and Noncovalent Approaches, Release Control, and Clinical Studies

Ulbrich, K., Holá, K., Šubr, V., Bakandritsos, A., Tuček, J., & Zbořil, R. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00589 · Cited by 1,741 · see citing works

Signals from the lysosome: a control centre for cellular clearance and energy metabolism

Settembre, C., Fraldi, A., Medina, D. L., & Ballabio, A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3565 · Cited by 1,689 · see citing works

Molecular definitions of autophagy and related processes

Galluzzi, L., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cecconi, F., Choi, A. M., Chu, C. T., Codogno, P., Colombo, M. I., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796697 · Cited by 1,646 · see citing works

Lysosomes as dynamic regulators of cell and organismal homeostasis

Ballabio, A., & Bonifacino, J. S. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0185-4 · Cited by 1,469 · see citing works

Lysosomal Physiology

Xu, H., & Ren, D. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021014-071649 · Cited by 1,028 · see citing works

Discerning the Chemistry in Individual Organelles with Small‐Molecule Fluorescent Probes

Xu, W., Zeng, Z., Jiang, J., Chang, Y., & Yuan, L. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201510721 · Cited by 806 · see citing works

Lysosomal membrane permeabilization and cell death

Wang, F., Gómez‐Sintes, R., & Boya, P. (2018) · Traffic · doi:10.1111/tra.12613 · Cited by 781 · see citing works

The lysosome: from waste bag to potential therapeutic target

Appelqvist, H., Wäster, P., Kågedal, K., & Öllinger, K. (2013) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjt022 · Cited by 772 · see citing works

Lysosomes as a therapeutic target

Bonam, S. R., Wang, F., & Muller, S. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0036-1 · Cited by 764 · see citing works

Immunogenic Cell Death Activates the Tumor Immune Microenvironment to Boost the Immunotherapy Efficiency

Li, Z., Lai, X., Fu, S., Ren, L. F., Cai, H., Zhang, H., Gu, Z., Ma, X., & Luo, K. (2022) · Advanced Science · doi:10.1002/advs.202201734 · Cited by 688 · see citing works

Lysosomal metabolomics reveals V-ATPase- and mTOR-dependent regulation of amino acid efflux from lysosomes

Abu-Remaileh, M., Wyant, G. A., Kim, C., Laqtom, N. N., Abbasi, M., Chan, S. H., Freinkman, E., & Sabatini, D. M. (2017) · Science · doi:10.1126/science.aan6298 · Cited by 665 · see citing works

The Lysosome as a Regulatory Hub

Perera, R. M., & Zoncu, R. (2016) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111315-125125 · Cited by 664 · see citing works

β-Coronaviruses Use Lysosomes for Egress Instead of the Biosynthetic Secretory Pathway

Ghosh, S., Dellibovi-Ragheb, T. A., Kerviel, A., Pak, E., Qiu, Q., Fisher, M., Takvorian, P. M., Bleck, C. K. E., Hsu, V. W., Fehr, A. R., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.039 · Cited by 615 · see citing works

pH in nature, humans and skin

Proksch, E. (2018) · The Journal of Dermatology · doi:10.1111/1346-8138.14489 · Cited by 596 · see citing works

Advances in Oral Drug Delivery for Regional Targeting in the Gastrointestinal Tract - Influence of Physiological, Pathophysiological and Pharmaceutical Factors

Hua, S. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00524 · Cited by 565 · see citing works

Disorders of lysosomal acidification—The emerging role of v-ATPase in aging and neurodegenerative disease

Colacurcio, D. J., & Nixon, R. A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.004 · Cited by 548 · see citing works

siRNA Delivery Strategies: A Comprehensive Review of Recent Developments

Tatiparti, K., Sau, S., Kashaw, S. K., & Iyer, A. K. (2017) · Nanomaterials · doi:10.3390/nano7040077 · Cited by 429 · see citing works

Recent progress in development of siRNA delivery vehicles for cancer therapy

Kim, H. J., Kim, A., Miyata, K., & Kataoka, K. (2016) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2016.06.011 · Cited by 424 · see citing works

The cell biology of the retinal pigment epithelium

Lakkaraju, A., Umapathy, A., Tan, L. X., Daniele, L., Philp, N. J., Boesze-Battaglia, K., & Williams, D. S. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100846 · Cited by 422 · see citing works

Targeting the Endocytic Pathway and Autophagy Process as a Novel Therapeutic Strategy in COVID-19

Yang, N., & Shen, H. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.45498 · Cited by 408 · see citing works

Activation of lysosomal function in the course of autophagy via mTORC1 suppression and autophagosome-lysosome fusion

Zhou, J., Tan, S.-H., Nicolas, V., Bauvy, C., Yang, N., Zhang, J., Xue, Y., Codogno, P., & Shen, H. (2013) · Cell Research · doi:10.1038/cr.2013.11 · Cited by 391 · see citing works

Presenilin 1 Maintains Lysosomal Ca2+ Homeostasis via TRPML1 by Regulating vATPase-Mediated Lysosome Acidification

Lee, J.-H., McBrayer, M. K., Wolfe, D. M., Haslett, L. J., Kumar, A., Sato, Y., Lie, P. P. Y., Mohan, P., Coffey, E. E., Kompella, U., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.050 · Cited by 358 · see citing works

Autophagy failure in A lzheimer's disease and the role of defective lysosomal acidification

Wolfe, D. M., Lee, J., Kumar, A. R., Lee, S., Orenstein, S. J., & Nixon, R. A. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12169 · Cited by 348 · see citing works

Hydroxychloroquine in systemic lupus erythematosus (SLE)

Ponticelli, C. E., & Moroni, G. L. (2016) · Expert Opinion on Drug Safety · doi:10.1080/14740338.2017.1269168 · Cited by 345 · see citing works

Intracellular delivery of nanomaterials: How to catch endosomal escape in the act

Martens, T., Remaut, K., Demeester, J., Smedt, S. C. D., & Braeckmans, K. (2014) · Nano Today · doi:10.1016/j.nantod.2014.04.011 · Cited by 341 · see citing works

At the end of the autophagic road: an emerging understanding of lysosomal functions in autophagy

Shen, H., & Mizushima, N. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.12.001 · Cited by 334 · see citing works

Targeted protein degradation: advances in drug discovery and clinical practice

Zhong, G., Chang, X., Xie, W., & Zhou, X. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02004-x · Cited by 326 · see citing works

A Comprehensive Review of Autophagy and Its Various Roles in Infectious, Non-Infectious, and Lifestyle Diseases: Current Knowledge and Prospects for Disease Prevention, Novel Drug Design, and Therapy

Khandia, R., Dadar, M., Munjal, A. K., Dhama, K., Karthik, K., Tiwari, R., Yatoo, M. I., Iqbal, H. M. N., Singh, K. P., Joshi, S. K., et al. (2019) · Cells · doi:10.3390/cells8070674 · Cited by 323 · see citing works

<p>A Nanodrug Consisting Of Doxorubicin And Exosome Derived From Mesenchymal Stem Cells For Osteosarcoma Treatment In Vitro</p>

Wei, H., Chen, J., Wang, S., Fu, F., Zhu, X., Wu, C., Liu, Z., Zhong, G., & Lin, J. (2019) · International Journal of Nanomedicine · doi:10.2147/ijn.s218988 · Cited by 317 · see citing works

Lysosomal Biology and Function: Modern View of Cellular Debris Bin

Trivedi, P., Bartlett, J., & Pulinilkunnil, T. (2020) · Cells · doi:10.3390/cells9051131 · Cited by 240 · see citing works

Cancer-associated lysosomal changes: friends or foes?

Kallunki, T., Olsen, O. D., & Jäättelä, M. (2012) · Oncogene · doi:10.1038/onc.2012.292 · Cited by 301 · see citing works

Lysosomes as coordinators of cellular catabolism, metabolic signalling and organ physiology

Settembre, C., & Perera, R. M. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00676-x · Cited by 296 · see citing works

Organelle-Targeted Photosensitizers for Precision Photodynamic Therapy

Wang, R., Li, X., & Yoon, J. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c02019 · Cited by 294 · see citing works

The elements of life and medicines

Chellan, P., & Sadler, P. J. (2015) · Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences · doi:10.1098/rsta.2014.0182 · Cited by 281 · see citing works

Manganese‐Based Layered Double Hydroxide Nanoparticles as a T1‐MRI Contrast Agent with Ultrasensitive pH Response and High Relaxivity

Li, B., Gu, Z., Kurniawan, N. D., Chen, W., & Xu, Z. P. (2017) · Advanced Materials · doi:10.1002/adma.201700373 · Cited by 260 · see citing works

Parkinson’s disease-risk protein TMEM175 is a proton-activated proton channel in lysosomes

Hu, M., Li, P., Wang, C., Feng, X., Geng, Q., Chen, W., Marthi, M., Zhang, W., Gao, C., Reid, W., et al. (2022) · Cell · doi:10.1016/j.cell.2022.05.021 · Cited by 254 · see citing works

Functional nanoparticles exploit the bile acid pathway to overcome multiple barriers of the intestinal epithelium for oral insulin delivery

Fan, W., Xia, D., Zhu, Q., Li, X., He, S., Zhu, C., Guo, S., Hovgaard, L., Yang, M., & Gan, Y. (2017) · Biomaterials · doi:10.1016/j.biomaterials.2017.10.022 · Cited by 247 · see citing works

Autophagy in age-related macular degeneration

Kaarniranta, K., Błasiak, J., Liton, P. B., Boulton, M. E., Klionsky, D. J., & Sinha, D. (2022) · Autophagy · doi:10.1080/15548627.2022.2069437 · Cited by 247 · see citing works

In situ self-assembly for cancer therapy and imaging

Kim, J., Lee, S., Kim, Y., Choi, M., Lee, I., Kim, E., Yoon, C. G., Pu, K., Kang, H., & Kim, J. S. (2023) · Nature Reviews Materials · doi:10.1038/s41578-023-00589-3 · Cited by 242 · see citing works

Structure and Roles of V-type ATPases

Vasanthakumar, T., & Rubinstein, J. L. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.12.007 · Cited by 240 · see citing works

Lysosome dysfunction as a cause of neurodegenerative diseases: Lessons from frontotemporal dementia and amyotrophic lateral sclerosis

Root, J. T., Merino, P., Nuckols, A., Johnson, M. A., & Kukar, T. L. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105360 · Cited by 230 · see citing works

Quercetin induces p53‐independent cancer cell death through lysosome activation by the transcription factor EB and Reactive Oxygen Species‐dependent ferroptosis

Wang, Z., Ma, J., Li, X., Wu, Y., Shi, H., Chen, Y., Lu, G. X., Shen, H., Lu, G., & Zhou, J. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15350 · Cited by 238 · see citing works

Maintaining Iron Homeostasis Is the Key Role of Lysosomal Acidity for Cell Proliferation

Weber, R. A., Yen, F. S., Nicholson, S. P. V., Alwaseem, H., Bayraktar, E. C., Alam, M., Timson, R. C., La, K., Abu-Remaileh, M., Molina, H., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.01.003 · Cited by 236 · see citing works

The challenges of oral drug delivery via nanocarriers

Reinholz, J., Landfester, K., & Mailänder, V. (2018) · Drug Delivery · doi:10.1080/10717544.2018.1501119 · Cited by 234 · see citing works

Impaired lysosomal acidification triggers iron deficiency and inflammation in vivo

Yambire, K. F., Rostosky, C. M., Watanabe, T., Pacheu‐Grau, D., Torres-Odio, S., Sanchez-Guerrero, A., Senderovich, O., Meyron‐Holtz, E. G., Milošević, I., Frahm, J., et al. (2019) · eLife · doi:10.7554/elife.51031 · Cited by 229 · see citing works

The emerging roles of vacuolar-type ATPase-dependent Lysosomal acidification in neurodegenerative diseases

Song, Q., Meng, B., Xu, H., & Mao, Z. (2020) · Translational Neurodegeneration · doi:10.1186/s40035-020-00196-0 · Cited by 231 · see citing works

TMEM175 Is an Organelle K+ Channel Regulating Lysosomal Function

Cang, C., Aranda, K., Seo, Y.-J., Gasnier, B., & Ren, D. (2015) · Cell · doi:10.1016/j.cell.2015.08.002 · Cited by 232 · see citing works

Inhibition of Glycogen Synthase Kinase-3 Ameliorates β-Amyloid Pathology and Restores Lysosomal Acidification and Mammalian Target of Rapamycin Activity in the Alzheimer Disease Mouse Model

Avrahami, L., Farfara, D., Shaham-Kol, M., Vassar, R. J., Frenkel, D., & Eldar-Finkelman, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.409250 · Cited by 232 · see citing works

A pH-independent DNA nanodevice for quantifying chloride transport in organelles of living cells

Saha, S., Prakash, V., Halder, S., Chakraborty, K., & Krishnan, Y. (2015) · Nature Nanotechnology · doi:10.1038/nnano.2015.130 · Cited by 226 · see citing works

Life in the lumen: The multivesicular endosome

Gruenberg, J. E. (2019) · Traffic · doi:10.1111/tra.12715 · Cited by 212 · see citing works

Lysosomal cell death mechanisms in aging

Gómez-Sintes, R., Ledesma, M. D., & Boya, P. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.02.009 · Cited by 216 · see citing works

Chloride in Vesicular Trafficking and Function

Stauber, T., & Jentsch, T. J. (2012) · Annual Review of Physiology · doi:10.1146/annurev-physiol-030212-183702 · Cited by 216 · see citing works

Autophagy as a modulator of cell death machinery

Noguchi, M., Hirata, N., Tanaka, T., Suizu, F., Nakajima, H., & Chiorini, J. A. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2724-5 · Cited by 215 · see citing works

Mutations in KCNH1 and ATP6V1B2 cause Zimmermann-Laband syndrome

Kortüm, F., Caputo, V., Bauer, C. K., Stella, L., Ciolfi, A., Alawi, M., Bocchinfuso, G., Flex, E., Paolacci, S., Dentici, M. L., et al. (2015) · Nature Genetics · doi:10.1038/ng.3282 · Cited by 211 · see citing works

Regulation and function of V-ATPases in physiology and disease

Collins, M. P., & Forgac, M. D. (2020) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2020.183341 · Cited by 210 · see citing works

Cellular Proteostasis in Neurodegeneration

Kurtishi, A., Rosen, B., Patil, K. S., Alves, G. W., & Møller, S. G. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1334-z · Cited by 203 · see citing works

A metal-free nanozyme-activated prodrug strategy for targeted tumor catalytic therapy

Liang, Q. Y., Xi, J., Gao, X. J., Zhang, R., Yang, Y., Gao, X., Yan, X., Gao, L., & Fan, K. (2020) · Nano Today · doi:10.1016/j.nantod.2020.100935 · Cited by 206 · see citing works

Lysosomal membrane permeabilization in cell death: new evidence and implications for health and disease

Serrano‐Puebla, A., & Boya, P. (2016) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12966 · Cited by 204 · see citing works

The endoplasmic reticulum, not the pH gradient, drives calcium refilling of lysosomes

Garrity, A. G., Wang, W., Collier, C. M., Levey, S. A., Gao, Q., & Xu, H. (2016) · eLife · doi:10.7554/elife.15887 · Cited by 203 · see citing works

Lysosomal size matters

de Araújo, M. E. G., Liebscher, G., Hess, M. W., & Huber, L. A. (2019) · Traffic · doi:10.1111/tra.12714 · Cited by 204 · see citing works

Organelle-targeted therapies: a comprehensive review on system design for enabling precision oncology

Yang, J., Griffin, A. S., Qiang, Z., & Ren, J. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01243-0 · Cited by 211 · see citing works

Bacterial Vesicle Secretion and the Evolutionary Origin of the Eukaryotic Endomembrane System

Gould, S. B., Garg, S. G., & Martin, W. F. (2016) · Trends in Microbiology · doi:10.1016/j.tim.2016.03.005 · Cited by 193 · see citing works

A model of lysosomal pH regulation

Ishida, Y., Nayak, S., Mindell, J. A., & Grabe, M. (2013) · The Journal of General Physiology · doi:10.1085/jgp.201210930 · Cited by 193 · see citing works

Smart Electrospun Nanofibers for Controlled Drug Release: Recent Advances and New Perspectives

Weng, L., & Xie, J. (2015) · Current Pharmaceutical Design · doi:10.2174/1381612821666150302151959 · Cited by 193 · see citing works

“Dual-Key-and-Lock” Ruthenium Complex Probe for Lysosomal Formaldehyde in Cancer Cells and Tumors

Liu, C., Zhang, R., Zhang, W., Liu, J., Wang, Y., Du, Z., Song, B., Xu, Z. P., & Yuan, J. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b13898 · Cited by 192 · see citing works

Lysosomal Iron, Iron Chelation, and Cell Death

Terman, A., & Kurz, T. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4885 · Cited by 191 · see citing works

A Multifunctional Nanomicelle for Real‐Time Targeted Imaging and Precise Near‐Infrared Cancer Therapy

Tian, J., Ding, L., Ju, H., Yang, Y., Li, X., Shen, Z., Zhu, Z., Yu, J., & Yang, C. J. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201405490 · Cited by 191 · see citing works

Engineering the drug carrier biointerface to overcome biological barriers to drug delivery

Finbloom, J. A., Sousa, F., Stevens, M. M., & Desai, T. A. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.06.007 · Cited by 192 · see citing works

Autophagy blockade and lysosomal membrane permeabilization contribute to lead-induced nephrotoxicity in primary rat proximal tubular cells

Song, X.-B., Liu, G., Liu, F., Yan, Z., Wang, Z., Liu, Z., & Wang, L. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.262 · Cited by 187 · see citing works

Principles and functions of metabolic compartmentalization

Bar-Peled, L., & Kory, N. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00645-2 · Cited by 157 · see citing works

Identification of Pseudomonas aeruginosa Phenazines that Kill Caenorhabditis elegans

Cezairliyan, B. O., Vinayavekhin, N., Lee, D. G., Yuen, G. J., Saghatelian, A., & Ausubel, F. M. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003101 · Cited by 177 · see citing works

Molecular and cellular pathways contributing to brain aging

Zia, A., Pourbagher‐Shahri, A. M., Farkhondeh, T., & Samarghandian, S. (2021) · Behavioral and Brain Functions · doi:10.1186/s12993-021-00179-9 · Cited by 186 · see citing works

Progranulin regulates lysosomal function and biogenesis through acidification of lysosomes

Tanaka, Y., Suzuki, G., Matsuwaki, T., Hosokawa, M., Serrano, G. E., Beach, T. G., Yamanouchi, K., Hasegawa, M., & Nishihara, M. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx011 · Cited by 172 · see citing works

The influence of lysosomal stability of silver nanomaterials on their toxicity to human cells

Setyawati, M. I., Yuan, X. F., Xie, J., & Leong, D. T. (2014) · Biomaterials · doi:10.1016/j.biomaterials.2014.05.007 · Cited by 179 · see citing works

Artesunate Induces Cell Death in Human Cancer Cells via Enhancing Lysosomal Function and Lysosomal Degradation of Ferritin

Yang, N., Tan, S.-H., Ng, S., Shi, Y. P., Zhou, J., Tan, K. S. W., Wong, W. S. F., & Shen, H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.564567 · Cited by 175 · see citing works

Lysosomal Dysfunction and α‐Synuclein Aggregation in Parkinson's Disease: Diagnostic Links

Moors, T. E., Paciotti, S., Chiasserini, D., Calabresi, P., Parnetti, L., Beccari, T., & van de Berg, W. D. J. (2016) · Movement Disorders · doi:10.1002/mds.26562 · Cited by 175 · see citing works

Lysosomal Ion Channels as Decoders of Cellular Signals

Li, P., Gu, M., & Xu, H. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.10.006 · Cited by 174 · see citing works

Cathepsin B in neurodegeneration of Alzheimer's disease, traumatic brain injury, and related brain disorders

HOOK, V. Y. H., Yoon, M. C., Mosier, C., Ito, G., Podvin, S., Head, B. P., Rissman, R. A., O’Donoghue, A. J., & Hook, G. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140428 · Cited by 170 · see citing works

Brain Disorders Due to Lysosomal Dysfunction

Fraldi, A., Klein, A. D., Medina, D. L., & Settembre, C. (2016) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-070815-014031 · Cited by 169 · see citing works

Nanoplatforms for Targeted Stimuli-Responsive Drug Delivery: A Review of Platform Materials and Stimuli-Responsive Release and Targeting Mechanisms

Sun, Y., & Davis, E. W. (2021) · Nanomaterials · doi:10.3390/nano11030746 · Cited by 180 · see citing works

Enhanced efficiency of mitochondria-targeted peptide SS-31 for acute kidney injury by pH-responsive and AKI-kidney targeted nanopolyplexes

Liu, D., Jin, F., Shu, G., Xu, X., Qi, J., Kang, X., Yu, H., Lu, K., Jiang, S., Han, F., et al. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.04.034 · Cited by 169 · see citing works

Ratiometric Fluorescent Probe for Lysosomal pH Measurement and Imaging in Living Cells Using Single-Wavelength Excitation

Liu, X., Su, Y., Tian, H., Yang, L., Zhang, H., Song, X., & Foley, J. W. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b00754 · Cited by 170 · see citing works

Lysosomal Dysfunction in Down Syndrome Is APP-Dependent and Mediated by APP-βCTF (C99)

Jiang, Y., Sato, Y., Im, E., Berg, M., Bordi, M., Darji, S., Kumar, A., Mohan, P. S., Bandyopadhyay, U., Diaz, A., et al. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.0578-19.2019 · Cited by 166 · see citing works

Pharmacological modulators of autophagy activate a parallel noncanonical pathway driving unconventional LC3 lipidation

Jacquin, É., Leclerc‐Mercier, S., Judon, C., Blanchard, E., Fraitag, S., & Florey, O. (2017) · Autophagy · doi:10.1080/15548627.2017.1287653 · Cited by 164 · see citing works

Loss of TMEM106B Ameliorates Lysosomal and Frontotemporal Dementia-Related Phenotypes in Progranulin-Deficient Mice

Klein, Z. A., Takahashi, H., Ma, M., Stagi, M., Zhou, M. S., Lam, T. T., & Strittmatter, S. M. (2017) · Neuron · doi:10.1016/j.neuron.2017.06.026 · Cited by 161 · see citing works

Mitochondrial Dysfunction and Neurodegeneration in Lysosomal Storage Disorders

Plotegher, N., & Duchen, M. R. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.12.003 · Cited by 161 · see citing works

The Lysosome Signaling Platform: Adapting With the Times

Inpanathan, S., & Botelho, R. J. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00113 · Cited by 157 · see citing works

The voltage-gated sodium channel TPC1 confers endolysosomal excitability

Cang, C., Bekele, B., & Ren, D. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1522 · Cited by 164 · see citing works

Surface Functionalization of Polymeric Nanoparticles with Umbilical Cord-Derived Mesenchymal Stem Cell Membrane for Tumor-Targeted Therapy

Yang, N., Ding, Y., Zhang, Y., Wang, B., Zhao, X., Cheng, K., Huang, Y., Taleb, M., Zhao, J. T., Dong, W., et al. (2018) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.8b05363 · Cited by 163 · see citing works

The Histidine Transporter SLC15A4 Coordinates mTOR-Dependent Inflammatory Responses and Pathogenic Antibody Production

Kobayashi, T., Shimabukuro-Demoto, S., Yoshida-Sugitani, R., Furuyama-Tanaka, K., Karyu, H., Sugiura, Y., Shimizu, Y., Hosaka, T., Goto, M., Kato, N., et al. (2014) · Immunity · doi:10.1016/j.immuni.2014.08.011 · Cited by 160 · see citing works

Zn2+ dyshomeostasis caused by loss of ATP13A2/PARK9 leads to lysosomal dysfunction and alpha-synuclein accumulation

Tsunemi, T., & Krainc, D. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt572 · Cited by 159 · see citing works

The H+-ATPase (V-ATPase): from proton pump to signaling complex in health and disease

Eaton, A. F., Merkulova, M., & Brown, D. (2020) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00442.2020 · Cited by 157 · see citing works

Misrouting of v-ATPase subunit V0a1 dysregulates lysosomal acidification in a neurodegenerative lysosomal storage disease model

Bagh, M. B., Peng, S., Chandra, G., Zhang, Z., SINGH, S. P., Pattabiraman, N., Liu, A., & Mukherjee, A. B. (2017) · Nature Communications · doi:10.1038/ncomms14612 · Cited by 155 · see citing works

Delivery of MicroRNAs by Chitosan Nanoparticles to Functionally Alter Macrophage Cholesterol Efflux in Vitro and in Vivo

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