J. Miyazaki and Y. Toumon, “Experimental evaluation of temperature increase and associated detection sensitivity in shot noise-limited photothermal microscopy,” Opt. Commun. 430, 170–175 (2019).
[Crossref]
Y. C. Wong, D. Ysselstein, and D. Krainc, “Mitochondria-lysosome contacts regulate mitochondrial fission via RAB7 GTP hydrolysis,” Nature 554(7692), 382–386 (2018).
[Crossref]
M. Audano, A. Schneider, and N. Mitro, “Mitochondria, lysosomes, and dysfunction: their meaning in neurodegeneration,” J. Neurochem. 147(3), 291–309 (2018).
[Crossref]
J. Miyazaki, “Improvement of signal-to-noise ratio in photothermal microscopy by optimizing detection aperture,” Opt. Commun. 390, 99–104 (2017).
[Crossref]
K. Todkar, H. S. Ilamathi, and M. Germain, “Mitochondria and Lysosomes: Discovering Bonds,” Front. Cell Dev. Biol. 5, 106 (2017).
[Crossref]
Y. Fujiwara, K. Wada, and T. Kabuta, “Lysosomal degradation of intracellular nucleic acids-multiple autophagic pathways,” J. Biochem. 161, 145–154 (2016).
[Crossref]
J. Pu, C. M. Guardia, T. Keren-Kaplan, and J. S. Bonifacino, “Mechanisms and functions of lysosome positioning,” J. Cell Sci. 129(23), 4329–4339 (2016).
[Crossref]
J. He, N. Wang, H. Tsurui, M. Kato, M. Iida, and T. Kobayashi, “Noninvasive, label-free, three-dimensional imaging of melanoma with confocal photothermal microscopy: Differentiate malignant melanoma from benign tumor tissue,” Sci. Rep. 6(1), 30209 (2016).
[Crossref]
J. Miyazaki, T. Iida, S. Tanaka, A. Hayashi-Takagi, H. Kasai, S. Okabe, and T. Kobayashi, “Fast 3D visualization of endogenous brain signals with high-sensitivity laser scanning photothermal microscopy,” Biomed. Opt. Express 7(5), 1702–1710 (2016).
[Crossref]
J. Miyazaki, H. Tsurui, K. Kawasumi, and T. Kobayashi, “Sensitivity enhancement of photothermal microscopy with radially segmented balanced detection,” Opt. Lett. 40(4), 479–482 (2015).
[Crossref]
J. Miyazaki, H. Tsurui, K. Kawasumi, and T. Kobayashi, “Simultaneous dual-wavelength imaging of nonfluorescent tissues with 3D subdiffraction photothermal microscopy,” Opt. Express 23(3), 3647–3656 (2015).
[Crossref]
J. Miyazaki, H. Tsurui, and T. Kobayashi, “Reduction of distortion in photothermal microscopy and its application to the high-resolution three-dimensional imaging of nonfluorescent tissues,” Biomed. Opt. Express 6(9), 3217–3224 (2015).
[Crossref]
T. Saito and J. Sadoshima, “Molecular mechanisms of mitochondrial autophagy/mitophagy in the heart,” Circ. Res. 116(8), 1477–1490 (2015).
[Crossref]
Y. Elbaz-Alon, E. Rosenfeld-Gur, V. Shinder, A. H. Futerman, T. Geiger, and M. Schuldiner, “A Dynamic Interface between Vacuoles and Mitochondria in Yeast,” Dev. Cell 30(1), 95–102 (2014).
[Crossref]
C. Honscher, M. Mari, K. Auffarth, M. Bohnert, J. Griffith, W. Geerts, M. van der Laan, M. Cabrera, F. Reggiori, and C. Ungermann, “Cellular Metabolism Regulates Contact Sites between Vacuoles and Mitochondria,” Dev. Cell 30(1), 86–94 (2014).
[Crossref]
P. Vermeulen, L. Cognet, and B. Lounis, “Photothermal microscopy: optical detection of small absorbers in scattering environments,” J. Microsc. 254(3), 115–121 (2014).
[Crossref]
D. A. Nedosekin, E. I. Galanzha, S. Ayyadevara, R. J. Shmookler Reis, and V. P. Zharov, “Photothermal confocal spectromicroscopy of multiple cellular chromophores and fluorophores,” Biophys. J. 102(3), 672–681 (2012).
[Crossref]
M. Okada, N. I. Smith, A. F. Palonpon, H. Endo, S. Kawata, M. Sodeoka, and K. Fujita, “Label-free Raman observation of cytochrome c dynamics during apoptosis,” Proc. Natl. Acad. Sci. U. S. A. 109(1), 28–32 (2012).
[Crossref]
F. M. Platt, B. Boland, and A. C. van der Spoel, “The cell biology of disease: lysosomal storage disorders: the cellular impact of lysosomal dysfunction,” J. Cell Biol. 199(5), 723–734 (2012).
[Crossref]
S. Lu, W. Min, S. Chong, G. R. Holtom, and X. S. Xie, “Label-free imaging of heme proteins with two-photon excited photothermal lens microscopy,” Appl. Phys. Lett. 96(11), 113701 (2010).
[Crossref]
A. V. Brusnichkin, D. A. Nedosekin, E. I. Galanzha, Y. A. Vladimirov, E. F. Shevtsova, M. A. Proskurnin, and V. P. Zharov, “Ultrasensitive label-free photothermal imaging, spectral identification, and quantification of cytochrome c in mitochondria, live cells, and solutions,” J. Biophotonics 3(12), 791–806 (2010).
[Crossref]
A. Gaiduk, M. Yorulmaz, P. V. Ruijgrok, and M. Orrit, “Room-temperature detection of a single molecule's absorption by photothermal contrast,” Science 330(6002), 353–356 (2010).
[Crossref]
E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal. Chem. 74(7), 1560–1564 (2002).
[Crossref]
H. Andersson, T. Baechi, M. Hoechl, and C. Richter, “Autofluorescence of living cells,” J. Microsc. 191(1), 1–7 (2002).
[Crossref]
W. H. Gao, Y. M. Pu, K. Q. Luo, and D. C. Chang, “Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells,” J. Cell Sci. 114, 2855–2862 (2001).
I. Jordens, M. Fernandez-Borja, M. Marsman, S. Dusseljee, L. Janssen, J. Calafat, H. Janssen, R. Wubbolts, and J. Neefjes, “The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors,” Curr. Biol. 11(21), 1680–1685 (2001).
[Crossref]
K. Uchiyama, A. Hibara, H. Kimura, T. Sawada, and T. Kitamori, “Thermal lens microscope,” Jpn. J. Appl. Phys. 39(Part 1, No. 9A), 5316–5322 (2000).
[Crossref]
E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal. Chem. 74(7), 1560–1564 (2002).
[Crossref]
H. Andersson, T. Baechi, M. Hoechl, and C. Richter, “Autofluorescence of living cells,” J. Microsc. 191(1), 1–7 (2002).
[Crossref]
M. Audano, A. Schneider, and N. Mitro, “Mitochondria, lysosomes, and dysfunction: their meaning in neurodegeneration,” J. Neurochem. 147(3), 291–309 (2018).
[Crossref]
C. Honscher, M. Mari, K. Auffarth, M. Bohnert, J. Griffith, W. Geerts, M. van der Laan, M. Cabrera, F. Reggiori, and C. Ungermann, “Cellular Metabolism Regulates Contact Sites between Vacuoles and Mitochondria,” Dev. Cell 30(1), 86–94 (2014).
[Crossref]
D. A. Nedosekin, E. I. Galanzha, S. Ayyadevara, R. J. Shmookler Reis, and V. P. Zharov, “Photothermal confocal spectromicroscopy of multiple cellular chromophores and fluorophores,” Biophys. J. 102(3), 672–681 (2012).
[Crossref]
H. Andersson, T. Baechi, M. Hoechl, and C. Richter, “Autofluorescence of living cells,” J. Microsc. 191(1), 1–7 (2002).
[Crossref]
C. Honscher, M. Mari, K. Auffarth, M. Bohnert, J. Griffith, W. Geerts, M. van der Laan, M. Cabrera, F. Reggiori, and C. Ungermann, “Cellular Metabolism Regulates Contact Sites between Vacuoles and Mitochondria,” Dev. Cell 30(1), 86–94 (2014).
[Crossref]
F. M. Platt, B. Boland, and A. C. van der Spoel, “The cell biology of disease: lysosomal storage disorders: the cellular impact of lysosomal dysfunction,” J. Cell Biol. 199(5), 723–734 (2012).
[Crossref]
J. Pu, C. M. Guardia, T. Keren-Kaplan, and J. S. Bonifacino, “Mechanisms and functions of lysosome positioning,” J. Cell Sci. 129(23), 4329–4339 (2016).
[Crossref]
A. V. Brusnichkin, D. A. Nedosekin, E. I. Galanzha, Y. A. Vladimirov, E. F. Shevtsova, M. A. Proskurnin, and V. P. Zharov, “Ultrasensitive label-free photothermal imaging, spectral identification, and quantification of cytochrome c in mitochondria, live cells, and solutions,” J. Biophotonics 3(12), 791–806 (2010).
[Crossref]
C. Honscher, M. Mari, K. Auffarth, M. Bohnert, J. Griffith, W. Geerts, M. van der Laan, M. Cabrera, F. Reggiori, and C. Ungermann, “Cellular Metabolism Regulates Contact Sites between Vacuoles and Mitochondria,” Dev. Cell 30(1), 86–94 (2014).
[Crossref]
I. Jordens, M. Fernandez-Borja, M. Marsman, S. Dusseljee, L. Janssen, J. Calafat, H. Janssen, R. Wubbolts, and J. Neefjes, “The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors,” Curr. Biol. 11(21), 1680–1685 (2001).
[Crossref]
W. H. Gao, Y. M. Pu, K. Q. Luo, and D. C. Chang, “Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells,” J. Cell Sci. 114, 2855–2862 (2001).
S. Lu, W. Min, S. Chong, G. R. Holtom, and X. S. Xie, “Label-free imaging of heme proteins with two-photon excited photothermal lens microscopy,” Appl. Phys. Lett. 96(11), 113701 (2010).
[Crossref]
P. Vermeulen, L. Cognet, and B. Lounis, “Photothermal microscopy: optical detection of small absorbers in scattering environments,” J. Microsc. 254(3), 115–121 (2014).
[Crossref]
D. Lasne, G. A. Blab, F. De Giorgi, F. Ichas, B. Lounis, and L. Cognet, “Label-free optical imaging of mitochondria in live cells,” Opt. Express 15(21), 14184–14193 (2007).
[Crossref]
I. Jordens, M. Fernandez-Borja, M. Marsman, S. Dusseljee, L. Janssen, J. Calafat, H. Janssen, R. Wubbolts, and J. Neefjes, “The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors,” Curr. Biol. 11(21), 1680–1685 (2001).
[Crossref]
Y. Elbaz-Alon, E. Rosenfeld-Gur, V. Shinder, A. H. Futerman, T. Geiger, and M. Schuldiner, “A Dynamic Interface between Vacuoles and Mitochondria in Yeast,” Dev. Cell 30(1), 95–102 (2014).
[Crossref]
M. Okada, N. I. Smith, A. F. Palonpon, H. Endo, S. Kawata, M. Sodeoka, and K. Fujita, “Label-free Raman observation of cytochrome c dynamics during apoptosis,” Proc. Natl. Acad. Sci. U. S. A. 109(1), 28–32 (2012).
[Crossref]
I. Jordens, M. Fernandez-Borja, M. Marsman, S. Dusseljee, L. Janssen, J. Calafat, H. Janssen, R. Wubbolts, and J. Neefjes, “The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors,” Curr. Biol. 11(21), 1680–1685 (2001).
[Crossref]
M. Okada, N. I. Smith, A. F. Palonpon, H. Endo, S. Kawata, M. Sodeoka, and K. Fujita, “Label-free Raman observation of cytochrome c dynamics during apoptosis,” Proc. Natl. Acad. Sci. U. S. A. 109(1), 28–32 (2012).
[Crossref]
Y. Fujiwara, K. Wada, and T. Kabuta, “Lysosomal degradation of intracellular nucleic acids-multiple autophagic pathways,” J. Biochem. 161, 145–154 (2016).
[Crossref]
Y. Elbaz-Alon, E. Rosenfeld-Gur, V. Shinder, A. H. Futerman, T. Geiger, and M. Schuldiner, “A Dynamic Interface between Vacuoles and Mitochondria in Yeast,” Dev. Cell 30(1), 95–102 (2014).
[Crossref]
A. Gaiduk, M. Yorulmaz, P. V. Ruijgrok, and M. Orrit, “Room-temperature detection of a single molecule's absorption by photothermal contrast,” Science 330(6002), 353–356 (2010).
[Crossref]
D. A. Nedosekin, E. I. Galanzha, S. Ayyadevara, R. J. Shmookler Reis, and V. P. Zharov, “Photothermal confocal spectromicroscopy of multiple cellular chromophores and fluorophores,” Biophys. J. 102(3), 672–681 (2012).
[Crossref]
A. V. Brusnichkin, D. A. Nedosekin, E. I. Galanzha, Y. A. Vladimirov, E. F. Shevtsova, M. A. Proskurnin, and V. P. Zharov, “Ultrasensitive label-free photothermal imaging, spectral identification, and quantification of cytochrome c in mitochondria, live cells, and solutions,” J. Biophotonics 3(12), 791–806 (2010).
[Crossref]
W. H. Gao, Y. M. Pu, K. Q. Luo, and D. C. Chang, “Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells,” J. Cell Sci. 114, 2855–2862 (2001).
C. Honscher, M. Mari, K. Auffarth, M. Bohnert, J. Griffith, W. Geerts, M. van der Laan, M. Cabrera, F. Reggiori, and C. Ungermann, “Cellular Metabolism Regulates Contact Sites between Vacuoles and Mitochondria,” Dev. Cell 30(1), 86–94 (2014).
[Crossref]
Y. Elbaz-Alon, E. Rosenfeld-Gur, V. Shinder, A. H. Futerman, T. Geiger, and M. Schuldiner, “A Dynamic Interface between Vacuoles and Mitochondria in Yeast,” Dev. Cell 30(1), 95–102 (2014).
[Crossref]
K. Todkar, H. S. Ilamathi, and M. Germain, “Mitochondria and Lysosomes: Discovering Bonds,” Front. Cell Dev. Biol. 5, 106 (2017).
[Crossref]
C. Honscher, M. Mari, K. Auffarth, M. Bohnert, J. Griffith, W. Geerts, M. van der Laan, M. Cabrera, F. Reggiori, and C. Ungermann, “Cellular Metabolism Regulates Contact Sites between Vacuoles and Mitochondria,” Dev. Cell 30(1), 86–94 (2014).
[Crossref]
J. Pu, C. M. Guardia, T. Keren-Kaplan, and J. S. Bonifacino, “Mechanisms and functions of lysosome positioning,” J. Cell Sci. 129(23), 4329–4339 (2016).
[Crossref]
J. He, N. Wang, H. Tsurui, M. Kato, M. Iida, and T. Kobayashi, “Noninvasive, label-free, three-dimensional imaging of melanoma with confocal photothermal microscopy: Differentiate malignant melanoma from benign tumor tissue,” Sci. Rep. 6(1), 30209 (2016).
[Crossref]
K. Uchiyama, A. Hibara, H. Kimura, T. Sawada, and T. Kitamori, “Thermal lens microscope,” Jpn. J. Appl. Phys. 39(Part 1, No. 9A), 5316–5322 (2000).
[Crossref]
H. Andersson, T. Baechi, M. Hoechl, and C. Richter, “Autofluorescence of living cells,” J. Microsc. 191(1), 1–7 (2002).
[Crossref]
S. Lu, W. Min, S. Chong, G. R. Holtom, and X. S. Xie, “Label-free imaging of heme proteins with two-photon excited photothermal lens microscopy,” Appl. Phys. Lett. 96(11), 113701 (2010).
[Crossref]
C. Honscher, M. Mari, K. Auffarth, M. Bohnert, J. Griffith, W. Geerts, M. van der Laan, M. Cabrera, F. Reggiori, and C. Ungermann, “Cellular Metabolism Regulates Contact Sites between Vacuoles and Mitochondria,” Dev. Cell 30(1), 86–94 (2014).
[Crossref]
J. He, N. Wang, H. Tsurui, M. Kato, M. Iida, and T. Kobayashi, “Noninvasive, label-free, three-dimensional imaging of melanoma with confocal photothermal microscopy: Differentiate malignant melanoma from benign tumor tissue,” Sci. Rep. 6(1), 30209 (2016).
[Crossref]
K. Todkar, H. S. Ilamathi, and M. Germain, “Mitochondria and Lysosomes: Discovering Bonds,” Front. Cell Dev. Biol. 5, 106 (2017).
[Crossref]
I. Jordens, M. Fernandez-Borja, M. Marsman, S. Dusseljee, L. Janssen, J. Calafat, H. Janssen, R. Wubbolts, and J. Neefjes, “The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors,” Curr. Biol. 11(21), 1680–1685 (2001).
[Crossref]
I. Jordens, M. Fernandez-Borja, M. Marsman, S. Dusseljee, L. Janssen, J. Calafat, H. Janssen, R. Wubbolts, and J. Neefjes, “The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors,” Curr. Biol. 11(21), 1680–1685 (2001).
[Crossref]
I. Jordens, M. Fernandez-Borja, M. Marsman, S. Dusseljee, L. Janssen, J. Calafat, H. Janssen, R. Wubbolts, and J. Neefjes, “The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors,” Curr. Biol. 11(21), 1680–1685 (2001).
[Crossref]
Y. Fujiwara, K. Wada, and T. Kabuta, “Lysosomal degradation of intracellular nucleic acids-multiple autophagic pathways,” J. Biochem. 161, 145–154 (2016).
[Crossref]
J. He, N. Wang, H. Tsurui, M. Kato, M. Iida, and T. Kobayashi, “Noninvasive, label-free, three-dimensional imaging of melanoma with confocal photothermal microscopy: Differentiate malignant melanoma from benign tumor tissue,” Sci. Rep. 6(1), 30209 (2016).
[Crossref]
J. Miyazaki, H. Tsurui, K. Kawasumi, and T. Kobayashi, “Sensitivity enhancement of photothermal microscopy with radially segmented balanced detection,” Opt. Lett. 40(4), 479–482 (2015).
[Crossref]
J. Miyazaki, H. Tsurui, K. Kawasumi, and T. Kobayashi, “Simultaneous dual-wavelength imaging of nonfluorescent tissues with 3D subdiffraction photothermal microscopy,” Opt. Express 23(3), 3647–3656 (2015).
[Crossref]
M. Okada, N. I. Smith, A. F. Palonpon, H. Endo, S. Kawata, M. Sodeoka, and K. Fujita, “Label-free Raman observation of cytochrome c dynamics during apoptosis,” Proc. Natl. Acad. Sci. U. S. A. 109(1), 28–32 (2012).
[Crossref]
J. Pu, C. M. Guardia, T. Keren-Kaplan, and J. S. Bonifacino, “Mechanisms and functions of lysosome positioning,” J. Cell Sci. 129(23), 4329–4339 (2016).
[Crossref]
K. Uchiyama, A. Hibara, H. Kimura, T. Sawada, and T. Kitamori, “Thermal lens microscope,” Jpn. J. Appl. Phys. 39(Part 1, No. 9A), 5316–5322 (2000).
[Crossref]
E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal. Chem. 74(7), 1560–1564 (2002).
[Crossref]
K. Uchiyama, A. Hibara, H. Kimura, T. Sawada, and T. Kitamori, “Thermal lens microscope,” Jpn. J. Appl. Phys. 39(Part 1, No. 9A), 5316–5322 (2000).
[Crossref]
J. Miyazaki, T. Iida, S. Tanaka, A. Hayashi-Takagi, H. Kasai, S. Okabe, and T. Kobayashi, “Fast 3D visualization of endogenous brain signals with high-sensitivity laser scanning photothermal microscopy,” Biomed. Opt. Express 7(5), 1702–1710 (2016).
[Crossref]
J. He, N. Wang, H. Tsurui, M. Kato, M. Iida, and T. Kobayashi, “Noninvasive, label-free, three-dimensional imaging of melanoma with confocal photothermal microscopy: Differentiate malignant melanoma from benign tumor tissue,” Sci. Rep. 6(1), 30209 (2016).
[Crossref]
J. Miyazaki, H. Tsurui, and T. Kobayashi, “Reduction of distortion in photothermal microscopy and its application to the high-resolution three-dimensional imaging of nonfluorescent tissues,” Biomed. Opt. Express 6(9), 3217–3224 (2015).
[Crossref]
J. Miyazaki, H. Tsurui, K. Kawasumi, and T. Kobayashi, “Sensitivity enhancement of photothermal microscopy with radially segmented balanced detection,” Opt. Lett. 40(4), 479–482 (2015).
[Crossref]
J. Miyazaki, H. Tsurui, K. Kawasumi, and T. Kobayashi, “Simultaneous dual-wavelength imaging of nonfluorescent tissues with 3D subdiffraction photothermal microscopy,” Opt. Express 23(3), 3647–3656 (2015).
[Crossref]
Y. C. Wong, D. Ysselstein, and D. Krainc, “Mitochondria-lysosome contacts regulate mitochondrial fission via RAB7 GTP hydrolysis,” Nature 554(7692), 382–386 (2018).
[Crossref]
P. Vermeulen, L. Cognet, and B. Lounis, “Photothermal microscopy: optical detection of small absorbers in scattering environments,” J. Microsc. 254(3), 115–121 (2014).
[Crossref]
D. Lasne, G. A. Blab, F. De Giorgi, F. Ichas, B. Lounis, and L. Cognet, “Label-free optical imaging of mitochondria in live cells,” Opt. Express 15(21), 14184–14193 (2007).
[Crossref]
S. Lu, W. Min, S. Chong, G. R. Holtom, and X. S. Xie, “Label-free imaging of heme proteins with two-photon excited photothermal lens microscopy,” Appl. Phys. Lett. 96(11), 113701 (2010).
[Crossref]
W. H. Gao, Y. M. Pu, K. Q. Luo, and D. C. Chang, “Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells,” J. Cell Sci. 114, 2855–2862 (2001).
C. Honscher, M. Mari, K. Auffarth, M. Bohnert, J. Griffith, W. Geerts, M. van der Laan, M. Cabrera, F. Reggiori, and C. Ungermann, “Cellular Metabolism Regulates Contact Sites between Vacuoles and Mitochondria,” Dev. Cell 30(1), 86–94 (2014).
[Crossref]
I. Jordens, M. Fernandez-Borja, M. Marsman, S. Dusseljee, L. Janssen, J. Calafat, H. Janssen, R. Wubbolts, and J. Neefjes, “The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors,” Curr. Biol. 11(21), 1680–1685 (2001).
[Crossref]
S. Lu, W. Min, S. Chong, G. R. Holtom, and X. S. Xie, “Label-free imaging of heme proteins with two-photon excited photothermal lens microscopy,” Appl. Phys. Lett. 96(11), 113701 (2010).
[Crossref]
M. Audano, A. Schneider, and N. Mitro, “Mitochondria, lysosomes, and dysfunction: their meaning in neurodegeneration,” J. Neurochem. 147(3), 291–309 (2018).
[Crossref]
J. Miyazaki and Y. Toumon, “Experimental evaluation of temperature increase and associated detection sensitivity in shot noise-limited photothermal microscopy,” Opt. Commun. 430, 170–175 (2019).
[Crossref]
J. Miyazaki, “Improvement of signal-to-noise ratio in photothermal microscopy by optimizing detection aperture,” Opt. Commun. 390, 99–104 (2017).
[Crossref]
J. Miyazaki, T. Iida, S. Tanaka, A. Hayashi-Takagi, H. Kasai, S. Okabe, and T. Kobayashi, “Fast 3D visualization of endogenous brain signals with high-sensitivity laser scanning photothermal microscopy,” Biomed. Opt. Express 7(5), 1702–1710 (2016).
[Crossref]
J. Miyazaki, H. Tsurui, and T. Kobayashi, “Reduction of distortion in photothermal microscopy and its application to the high-resolution three-dimensional imaging of nonfluorescent tissues,” Biomed. Opt. Express 6(9), 3217–3224 (2015).
[Crossref]
J. Miyazaki, H. Tsurui, K. Kawasumi, and T. Kobayashi, “Sensitivity enhancement of photothermal microscopy with radially segmented balanced detection,” Opt. Lett. 40(4), 479–482 (2015).
[Crossref]
J. Miyazaki, H. Tsurui, K. Kawasumi, and T. Kobayashi, “Simultaneous dual-wavelength imaging of nonfluorescent tissues with 3D subdiffraction photothermal microscopy,” Opt. Express 23(3), 3647–3656 (2015).
[Crossref]
D. A. Nedosekin, E. I. Galanzha, S. Ayyadevara, R. J. Shmookler Reis, and V. P. Zharov, “Photothermal confocal spectromicroscopy of multiple cellular chromophores and fluorophores,” Biophys. J. 102(3), 672–681 (2012).
[Crossref]
A. V. Brusnichkin, D. A. Nedosekin, E. I. Galanzha, Y. A. Vladimirov, E. F. Shevtsova, M. A. Proskurnin, and V. P. Zharov, “Ultrasensitive label-free photothermal imaging, spectral identification, and quantification of cytochrome c in mitochondria, live cells, and solutions,” J. Biophotonics 3(12), 791–806 (2010).
[Crossref]
I. Jordens, M. Fernandez-Borja, M. Marsman, S. Dusseljee, L. Janssen, J. Calafat, H. Janssen, R. Wubbolts, and J. Neefjes, “The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors,” Curr. Biol. 11(21), 1680–1685 (2001).
[Crossref]
M. Okada, N. I. Smith, A. F. Palonpon, H. Endo, S. Kawata, M. Sodeoka, and K. Fujita, “Label-free Raman observation of cytochrome c dynamics during apoptosis,” Proc. Natl. Acad. Sci. U. S. A. 109(1), 28–32 (2012).
[Crossref]
A. Gaiduk, M. Yorulmaz, P. V. Ruijgrok, and M. Orrit, “Room-temperature detection of a single molecule's absorption by photothermal contrast,” Science 330(6002), 353–356 (2010).
[Crossref]
M. Okada, N. I. Smith, A. F. Palonpon, H. Endo, S. Kawata, M. Sodeoka, and K. Fujita, “Label-free Raman observation of cytochrome c dynamics during apoptosis,” Proc. Natl. Acad. Sci. U. S. A. 109(1), 28–32 (2012).
[Crossref]
F. M. Platt, B. Boland, and A. C. van der Spoel, “The cell biology of disease: lysosomal storage disorders: the cellular impact of lysosomal dysfunction,” J. Cell Biol. 199(5), 723–734 (2012).
[Crossref]
A. V. Brusnichkin, D. A. Nedosekin, E. I. Galanzha, Y. A. Vladimirov, E. F. Shevtsova, M. A. Proskurnin, and V. P. Zharov, “Ultrasensitive label-free photothermal imaging, spectral identification, and quantification of cytochrome c in mitochondria, live cells, and solutions,” J. Biophotonics 3(12), 791–806 (2010).
[Crossref]
J. Pu, C. M. Guardia, T. Keren-Kaplan, and J. S. Bonifacino, “Mechanisms and functions of lysosome positioning,” J. Cell Sci. 129(23), 4329–4339 (2016).
[Crossref]
W. H. Gao, Y. M. Pu, K. Q. Luo, and D. C. Chang, “Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells,” J. Cell Sci. 114, 2855–2862 (2001).
C. Honscher, M. Mari, K. Auffarth, M. Bohnert, J. Griffith, W. Geerts, M. van der Laan, M. Cabrera, F. Reggiori, and C. Ungermann, “Cellular Metabolism Regulates Contact Sites between Vacuoles and Mitochondria,” Dev. Cell 30(1), 86–94 (2014).
[Crossref]
H. Andersson, T. Baechi, M. Hoechl, and C. Richter, “Autofluorescence of living cells,” J. Microsc. 191(1), 1–7 (2002).
[Crossref]
Y. Elbaz-Alon, E. Rosenfeld-Gur, V. Shinder, A. H. Futerman, T. Geiger, and M. Schuldiner, “A Dynamic Interface between Vacuoles and Mitochondria in Yeast,” Dev. Cell 30(1), 95–102 (2014).
[Crossref]
A. Gaiduk, M. Yorulmaz, P. V. Ruijgrok, and M. Orrit, “Room-temperature detection of a single molecule's absorption by photothermal contrast,” Science 330(6002), 353–356 (2010).
[Crossref]
T. Saito and J. Sadoshima, “Molecular mechanisms of mitochondrial autophagy/mitophagy in the heart,” Circ. Res. 116(8), 1477–1490 (2015).
[Crossref]
T. Saito and J. Sadoshima, “Molecular mechanisms of mitochondrial autophagy/mitophagy in the heart,” Circ. Res. 116(8), 1477–1490 (2015).
[Crossref]
E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal. Chem. 74(7), 1560–1564 (2002).
[Crossref]
E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal. Chem. 74(7), 1560–1564 (2002).
[Crossref]
K. Uchiyama, A. Hibara, H. Kimura, T. Sawada, and T. Kitamori, “Thermal lens microscope,” Jpn. J. Appl. Phys. 39(Part 1, No. 9A), 5316–5322 (2000).
[Crossref]
M. Audano, A. Schneider, and N. Mitro, “Mitochondria, lysosomes, and dysfunction: their meaning in neurodegeneration,” J. Neurochem. 147(3), 291–309 (2018).
[Crossref]
Y. Elbaz-Alon, E. Rosenfeld-Gur, V. Shinder, A. H. Futerman, T. Geiger, and M. Schuldiner, “A Dynamic Interface between Vacuoles and Mitochondria in Yeast,” Dev. Cell 30(1), 95–102 (2014).
[Crossref]
A. V. Brusnichkin, D. A. Nedosekin, E. I. Galanzha, Y. A. Vladimirov, E. F. Shevtsova, M. A. Proskurnin, and V. P. Zharov, “Ultrasensitive label-free photothermal imaging, spectral identification, and quantification of cytochrome c in mitochondria, live cells, and solutions,” J. Biophotonics 3(12), 791–806 (2010).
[Crossref]
Y. Elbaz-Alon, E. Rosenfeld-Gur, V. Shinder, A. H. Futerman, T. Geiger, and M. Schuldiner, “A Dynamic Interface between Vacuoles and Mitochondria in Yeast,” Dev. Cell 30(1), 95–102 (2014).
[Crossref]
D. A. Nedosekin, E. I. Galanzha, S. Ayyadevara, R. J. Shmookler Reis, and V. P. Zharov, “Photothermal confocal spectromicroscopy of multiple cellular chromophores and fluorophores,” Biophys. J. 102(3), 672–681 (2012).
[Crossref]
M. Okada, N. I. Smith, A. F. Palonpon, H. Endo, S. Kawata, M. Sodeoka, and K. Fujita, “Label-free Raman observation of cytochrome c dynamics during apoptosis,” Proc. Natl. Acad. Sci. U. S. A. 109(1), 28–32 (2012).
[Crossref]
M. Okada, N. I. Smith, A. F. Palonpon, H. Endo, S. Kawata, M. Sodeoka, and K. Fujita, “Label-free Raman observation of cytochrome c dynamics during apoptosis,” Proc. Natl. Acad. Sci. U. S. A. 109(1), 28–32 (2012).
[Crossref]
E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal. Chem. 74(7), 1560–1564 (2002).
[Crossref]
K. Todkar, H. S. Ilamathi, and M. Germain, “Mitochondria and Lysosomes: Discovering Bonds,” Front. Cell Dev. Biol. 5, 106 (2017).
[Crossref]
E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal. Chem. 74(7), 1560–1564 (2002).
[Crossref]
J. Miyazaki and Y. Toumon, “Experimental evaluation of temperature increase and associated detection sensitivity in shot noise-limited photothermal microscopy,” Opt. Commun. 430, 170–175 (2019).
[Crossref]
J. He, N. Wang, H. Tsurui, M. Kato, M. Iida, and T. Kobayashi, “Noninvasive, label-free, three-dimensional imaging of melanoma with confocal photothermal microscopy: Differentiate malignant melanoma from benign tumor tissue,” Sci. Rep. 6(1), 30209 (2016).
[Crossref]
J. Miyazaki, H. Tsurui, and T. Kobayashi, “Reduction of distortion in photothermal microscopy and its application to the high-resolution three-dimensional imaging of nonfluorescent tissues,” Biomed. Opt. Express 6(9), 3217–3224 (2015).
[Crossref]
J. Miyazaki, H. Tsurui, K. Kawasumi, and T. Kobayashi, “Simultaneous dual-wavelength imaging of nonfluorescent tissues with 3D subdiffraction photothermal microscopy,” Opt. Express 23(3), 3647–3656 (2015).
[Crossref]
J. Miyazaki, H. Tsurui, K. Kawasumi, and T. Kobayashi, “Sensitivity enhancement of photothermal microscopy with radially segmented balanced detection,” Opt. Lett. 40(4), 479–482 (2015).
[Crossref]
K. Uchiyama, A. Hibara, H. Kimura, T. Sawada, and T. Kitamori, “Thermal lens microscope,” Jpn. J. Appl. Phys. 39(Part 1, No. 9A), 5316–5322 (2000).
[Crossref]
C. Honscher, M. Mari, K. Auffarth, M. Bohnert, J. Griffith, W. Geerts, M. van der Laan, M. Cabrera, F. Reggiori, and C. Ungermann, “Cellular Metabolism Regulates Contact Sites between Vacuoles and Mitochondria,” Dev. Cell 30(1), 86–94 (2014).
[Crossref]
C. Honscher, M. Mari, K. Auffarth, M. Bohnert, J. Griffith, W. Geerts, M. van der Laan, M. Cabrera, F. Reggiori, and C. Ungermann, “Cellular Metabolism Regulates Contact Sites between Vacuoles and Mitochondria,” Dev. Cell 30(1), 86–94 (2014).
[Crossref]
F. M. Platt, B. Boland, and A. C. van der Spoel, “The cell biology of disease: lysosomal storage disorders: the cellular impact of lysosomal dysfunction,” J. Cell Biol. 199(5), 723–734 (2012).
[Crossref]
P. Vermeulen, L. Cognet, and B. Lounis, “Photothermal microscopy: optical detection of small absorbers in scattering environments,” J. Microsc. 254(3), 115–121 (2014).
[Crossref]
A. V. Brusnichkin, D. A. Nedosekin, E. I. Galanzha, Y. A. Vladimirov, E. F. Shevtsova, M. A. Proskurnin, and V. P. Zharov, “Ultrasensitive label-free photothermal imaging, spectral identification, and quantification of cytochrome c in mitochondria, live cells, and solutions,” J. Biophotonics 3(12), 791–806 (2010).
[Crossref]
Y. Fujiwara, K. Wada, and T. Kabuta, “Lysosomal degradation of intracellular nucleic acids-multiple autophagic pathways,” J. Biochem. 161, 145–154 (2016).
[Crossref]
J. He, N. Wang, H. Tsurui, M. Kato, M. Iida, and T. Kobayashi, “Noninvasive, label-free, three-dimensional imaging of melanoma with confocal photothermal microscopy: Differentiate malignant melanoma from benign tumor tissue,” Sci. Rep. 6(1), 30209 (2016).
[Crossref]
Y. C. Wong, D. Ysselstein, and D. Krainc, “Mitochondria-lysosome contacts regulate mitochondrial fission via RAB7 GTP hydrolysis,” Nature 554(7692), 382–386 (2018).
[Crossref]
I. Jordens, M. Fernandez-Borja, M. Marsman, S. Dusseljee, L. Janssen, J. Calafat, H. Janssen, R. Wubbolts, and J. Neefjes, “The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors,” Curr. Biol. 11(21), 1680–1685 (2001).
[Crossref]
S. Lu, W. Min, S. Chong, G. R. Holtom, and X. S. Xie, “Label-free imaging of heme proteins with two-photon excited photothermal lens microscopy,” Appl. Phys. Lett. 96(11), 113701 (2010).
[Crossref]
A. Gaiduk, M. Yorulmaz, P. V. Ruijgrok, and M. Orrit, “Room-temperature detection of a single molecule's absorption by photothermal contrast,” Science 330(6002), 353–356 (2010).
[Crossref]
Y. C. Wong, D. Ysselstein, and D. Krainc, “Mitochondria-lysosome contacts regulate mitochondrial fission via RAB7 GTP hydrolysis,” Nature 554(7692), 382–386 (2018).
[Crossref]
D. A. Nedosekin, E. I. Galanzha, S. Ayyadevara, R. J. Shmookler Reis, and V. P. Zharov, “Photothermal confocal spectromicroscopy of multiple cellular chromophores and fluorophores,” Biophys. J. 102(3), 672–681 (2012).
[Crossref]
A. V. Brusnichkin, D. A. Nedosekin, E. I. Galanzha, Y. A. Vladimirov, E. F. Shevtsova, M. A. Proskurnin, and V. P. Zharov, “Ultrasensitive label-free photothermal imaging, spectral identification, and quantification of cytochrome c in mitochondria, live cells, and solutions,” J. Biophotonics 3(12), 791–806 (2010).
[Crossref]
E. Tamaki, K. Sato, M. Tokeshi, K. Sato, M. Aihara, and T. Kitamori, “Single-cell analysis by a scanning thermal lens microscope with a microchip: direct monitoring of cytochrome c distribution during apoptosis process,” Anal. Chem. 74(7), 1560–1564 (2002).
[Crossref]
S. Lu, W. Min, S. Chong, G. R. Holtom, and X. S. Xie, “Label-free imaging of heme proteins with two-photon excited photothermal lens microscopy,” Appl. Phys. Lett. 96(11), 113701 (2010).
[Crossref]
J. Miyazaki, H. Tsurui, and T. Kobayashi, “Reduction of distortion in photothermal microscopy and its application to the high-resolution three-dimensional imaging of nonfluorescent tissues,” Biomed. Opt. Express 6(9), 3217–3224 (2015).
[Crossref]
J. Miyazaki, T. Iida, S. Tanaka, A. Hayashi-Takagi, H. Kasai, S. Okabe, and T. Kobayashi, “Fast 3D visualization of endogenous brain signals with high-sensitivity laser scanning photothermal microscopy,” Biomed. Opt. Express 7(5), 1702–1710 (2016).
[Crossref]
D. A. Nedosekin, E. I. Galanzha, S. Ayyadevara, R. J. Shmookler Reis, and V. P. Zharov, “Photothermal confocal spectromicroscopy of multiple cellular chromophores and fluorophores,” Biophys. J. 102(3), 672–681 (2012).
[Crossref]
T. Saito and J. Sadoshima, “Molecular mechanisms of mitochondrial autophagy/mitophagy in the heart,” Circ. Res. 116(8), 1477–1490 (2015).
[Crossref]
I. Jordens, M. Fernandez-Borja, M. Marsman, S. Dusseljee, L. Janssen, J. Calafat, H. Janssen, R. Wubbolts, and J. Neefjes, “The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors,” Curr. Biol. 11(21), 1680–1685 (2001).
[Crossref]
Y. Elbaz-Alon, E. Rosenfeld-Gur, V. Shinder, A. H. Futerman, T. Geiger, and M. Schuldiner, “A Dynamic Interface between Vacuoles and Mitochondria in Yeast,” Dev. Cell 30(1), 95–102 (2014).
[Crossref]
C. Honscher, M. Mari, K. Auffarth, M. Bohnert, J. Griffith, W. Geerts, M. van der Laan, M. Cabrera, F. Reggiori, and C. Ungermann, “Cellular Metabolism Regulates Contact Sites between Vacuoles and Mitochondria,” Dev. Cell 30(1), 86–94 (2014).
[Crossref]
K. Todkar, H. S. Ilamathi, and M. Germain, “Mitochondria and Lysosomes: Discovering Bonds,” Front. Cell Dev. Biol. 5, 106 (2017).
[Crossref]
Y. Fujiwara, K. Wada, and T. Kabuta, “Lysosomal degradation of intracellular nucleic acids-multiple autophagic pathways,” J. Biochem. 161, 145–154 (2016).
[Crossref]
A. V. Brusnichkin, D. A. Nedosekin, E. I. Galanzha, Y. A. Vladimirov, E. F. Shevtsova, M. A. Proskurnin, and V. P. Zharov, “Ultrasensitive label-free photothermal imaging, spectral identification, and quantification of cytochrome c in mitochondria, live cells, and solutions,” J. Biophotonics 3(12), 791–806 (2010).
[Crossref]
F. M. Platt, B. Boland, and A. C. van der Spoel, “The cell biology of disease: lysosomal storage disorders: the cellular impact of lysosomal dysfunction,” J. Cell Biol. 199(5), 723–734 (2012).
[Crossref]
J. Pu, C. M. Guardia, T. Keren-Kaplan, and J. S. Bonifacino, “Mechanisms and functions of lysosome positioning,” J. Cell Sci. 129(23), 4329–4339 (2016).
[Crossref]
W. H. Gao, Y. M. Pu, K. Q. Luo, and D. C. Chang, “Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells,” J. Cell Sci. 114, 2855–2862 (2001).
P. Vermeulen, L. Cognet, and B. Lounis, “Photothermal microscopy: optical detection of small absorbers in scattering environments,” J. Microsc. 254(3), 115–121 (2014).
[Crossref]
H. Andersson, T. Baechi, M. Hoechl, and C. Richter, “Autofluorescence of living cells,” J. Microsc. 191(1), 1–7 (2002).
[Crossref]
M. Audano, A. Schneider, and N. Mitro, “Mitochondria, lysosomes, and dysfunction: their meaning in neurodegeneration,” J. Neurochem. 147(3), 291–309 (2018).
[Crossref]
K. Uchiyama, A. Hibara, H. Kimura, T. Sawada, and T. Kitamori, “Thermal lens microscope,” Jpn. J. Appl. Phys. 39(Part 1, No. 9A), 5316–5322 (2000).
[Crossref]
Y. C. Wong, D. Ysselstein, and D. Krainc, “Mitochondria-lysosome contacts regulate mitochondrial fission via RAB7 GTP hydrolysis,” Nature 554(7692), 382–386 (2018).
[Crossref]
J. Miyazaki and Y. Toumon, “Experimental evaluation of temperature increase and associated detection sensitivity in shot noise-limited photothermal microscopy,” Opt. Commun. 430, 170–175 (2019).
[Crossref]
J. Miyazaki, “Improvement of signal-to-noise ratio in photothermal microscopy by optimizing detection aperture,” Opt. Commun. 390, 99–104 (2017).
[Crossref]
J. Miyazaki, H. Tsurui, K. Kawasumi, and T. Kobayashi, “Simultaneous dual-wavelength imaging of nonfluorescent tissues with 3D subdiffraction photothermal microscopy,” Opt. Express 23(3), 3647–3656 (2015).
[Crossref]
D. Lasne, G. A. Blab, F. De Giorgi, F. Ichas, B. Lounis, and L. Cognet, “Label-free optical imaging of mitochondria in live cells,” Opt. Express 15(21), 14184–14193 (2007).
[Crossref]
M. Okada, N. I. Smith, A. F. Palonpon, H. Endo, S. Kawata, M. Sodeoka, and K. Fujita, “Label-free Raman observation of cytochrome c dynamics during apoptosis,” Proc. Natl. Acad. Sci. U. S. A. 109(1), 28–32 (2012).
[Crossref]
J. He, N. Wang, H. Tsurui, M. Kato, M. Iida, and T. Kobayashi, “Noninvasive, label-free, three-dimensional imaging of melanoma with confocal photothermal microscopy: Differentiate malignant melanoma from benign tumor tissue,” Sci. Rep. 6(1), 30209 (2016).
[Crossref]
A. Gaiduk, M. Yorulmaz, P. V. Ruijgrok, and M. Orrit, “Room-temperature detection of a single molecule's absorption by photothermal contrast,” Science 330(6002), 353–356 (2010).
[Crossref]