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Showing 61 to 71 of 71 entries
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Diversity in autoimmunity against retinal, neuronal, and axonal antigens in acquired neuro-retinopathy.

Journal of ophthalmic inflammation and infection

Adamus G, Brown L, Schiffman J, Iannaccone A.
PMID: 21744285
J Ophthalmic Inflamm Infect. 2011 Sep;1(3):111-21. doi: 10.1007/s12348-011-0028-8. Epub 2011 Jul 10.

PURPOSE: Autoimmune retinopathies and optic neuropathies are complex disorders of the retina and the optic nerve, in which patients develop autoantibodies (AAbs) against retinal and optic nerve proteins. Autoimmunity might significantly influence the outcome of retinal and optic nerve...

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Adamus G, Brown L, Schiffman J, et al. Diversity in autoimmunity against retinal, neuronal, and axonal antigens in acquired neuro-retinopathy. J Ophthalmic Inflamm Infect. 2011;1(3):111-21doi: 10.1007/s12348-011-0028-8.
Adamus, G., Brown, L., Schiffman, J., & Iannaccone, A. (2011). Diversity in autoimmunity against retinal, neuronal, and axonal antigens in acquired neuro-retinopathy. Journal of ophthalmic inflammation and infection, 1(3), 111-21. https://doi.org/10.1007/s12348-011-0028-8
Adamus, Grazyna, et al. "Diversity in autoimmunity against retinal, neuronal, and axonal antigens in acquired neuro-retinopathy." Journal of ophthalmic inflammation and infection vol. 1,3 (2011): 111-21. doi: https://doi.org/10.1007/s12348-011-0028-8
Adamus G, Brown L, Schiffman J, Iannaccone A. Diversity in autoimmunity against retinal, neuronal, and axonal antigens in acquired neuro-retinopathy. J Ophthalmic Inflamm Infect. 2011 Sep;1(3):111-21. doi: 10.1007/s12348-011-0028-8. Epub 2011 Jul 10. PMID: 21744285; PMCID: PMC3168374.
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Mannosylated Linear and Cyclic Single Amino Acid Mutant Peptides Using a Small 10 Amino Acid Linker Constitute Promising Candidates Against Multiple Sclerosis.

Frontiers in immunology

Day S, Tselios T, Androutsou ME, Tapeinou A, Frilligou I, Stojanovska L, Matsoukas J, Apostolopoulos V.
PMID: 26082772
Front Immunol. 2015 Apr 07;6:136. doi: 10.3389/fimmu.2015.00136. eCollection 2015.

Multiple sclerosis (MS) is a serious autoimmune demyelinating disease leading to loss of neurological function. The design and synthesis of various altered peptide ligands of immunodominant epitopes of myelin proteins to alter the autoimmune response, is a promising therapeutic...

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Day S, Tselios T, Androutsou ME, et al. Mannosylated Linear and Cyclic Single Amino Acid Mutant Peptides Using a Small 10 Amino Acid Linker Constitute Promising Candidates Against Multiple Sclerosis. Front Immunol. 2015;6:136doi: 10.3389/fimmu.2015.00136.
Day, S., Tselios, T., Androutsou, M. E., Tapeinou, A., Frilligou, I., Stojanovska, L., Matsoukas, J., & Apostolopoulos, V. (2015). Mannosylated Linear and Cyclic Single Amino Acid Mutant Peptides Using a Small 10 Amino Acid Linker Constitute Promising Candidates Against Multiple Sclerosis. Frontiers in immunology, 6136. https://doi.org/10.3389/fimmu.2015.00136
Day, Stephanie, et al. "Mannosylated Linear and Cyclic Single Amino Acid Mutant Peptides Using a Small 10 Amino Acid Linker Constitute Promising Candidates Against Multiple Sclerosis." Frontiers in immunology vol. 6 (2015): 136. doi: https://doi.org/10.3389/fimmu.2015.00136
Day S, Tselios T, Androutsou ME, Tapeinou A, Frilligou I, Stojanovska L, Matsoukas J, Apostolopoulos V. Mannosylated Linear and Cyclic Single Amino Acid Mutant Peptides Using a Small 10 Amino Acid Linker Constitute Promising Candidates Against Multiple Sclerosis. Front Immunol. 2015 Apr 07;6:136. doi: 10.3389/fimmu.2015.00136. eCollection 2015. PMID: 26082772; PMCID: PMC4450228.
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Selective loss of myelin proteins during autolysis.

Neurochemical research

Fishman MA, Trotter JL, Agrawal HC.
PMID: 24272052
Neurochem Res. 1977 Jun;2(3):247-57. doi: 10.1007/BF00969355.

Rat brains allowed to autolyze in situ for 12 h selectively lost myelin proteins. Basic proteins are markedly decreased, but DM-20 (1) and proteolipid proteins also are lost from the myelin of developing and mature rat brain. At room...

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Fishman MA, Trotter JL, Agrawal HC. Selective loss of myelin proteins during autolysis. Neurochem Res. 1977;2(3):247-57doi: 10.1007/BF00969355.
Fishman, M. A., Trotter, J. L., & Agrawal, H. C. (1977). Selective loss of myelin proteins during autolysis. Neurochemical research, 2(3), 247-57. https://doi.org/10.1007/BF00969355
Fishman, M A, et al. "Selective loss of myelin proteins during autolysis." Neurochemical research vol. 2,3 (1977): 247-57. doi: https://doi.org/10.1007/BF00969355
Fishman MA, Trotter JL, Agrawal HC. Selective loss of myelin proteins during autolysis. Neurochem Res. 1977 Jun;2(3):247-57. doi: 10.1007/BF00969355. PMID: 24272052.
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Neurotrophin-4 induces myelin protein zero expression in cultured Schwann cells via the TrkB/PI3K/Akt/mTORC1 pathway.

Animal cells and systems

Guo W, Li Y, Sun C, Duan HQ, Liu S, Xu YQ, Feng SQ.
PMID: 30460055
Anim Cells Syst (Seoul). 2017 Feb 21;21(2):84-92. doi: 10.1080/19768354.2017.1289980. eCollection 2017.

Myelin formation during peripheral nervous system development, as well as myelin repair after injury and in disease, requires multiple intrinsic and extrinsic signals. Neurotrophin-4 (NT-4) is a member of the neurotrophin family, which regulates the development of neuronal networks...

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Guo W, Li Y, Sun C, et al. Neurotrophin-4 induces myelin protein zero expression in cultured Schwann cells via the TrkB/PI3K/Akt/mTORC1 pathway. Anim Cells Syst (Seoul). 2017;21(2):84-92doi: 10.1080/19768354.2017.1289980.
Guo, W., Li, Y., Sun, C., Duan, H. Q., Liu, S., Xu, Y. Q., & Feng, S. Q. (2017). Neurotrophin-4 induces myelin protein zero expression in cultured Schwann cells via the TrkB/PI3K/Akt/mTORC1 pathway. Animal cells and systems, 21(2), 84-92. https://doi.org/10.1080/19768354.2017.1289980
Guo, Wei, et al. "Neurotrophin-4 induces myelin protein zero expression in cultured Schwann cells via the TrkB/PI3K/Akt/mTORC1 pathway." Animal cells and systems vol. 21,2 (2017): 84-92. doi: https://doi.org/10.1080/19768354.2017.1289980
Guo W, Li Y, Sun C, Duan HQ, Liu S, Xu YQ, Feng SQ. Neurotrophin-4 induces myelin protein zero expression in cultured Schwann cells via the TrkB/PI3K/Akt/mTORC1 pathway. Anim Cells Syst (Seoul). 2017 Feb 21;21(2):84-92. doi: 10.1080/19768354.2017.1289980. eCollection 2017. PMID: 30460055; PMCID: PMC6138314.
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Endoplasmic Reticulum Protein Quality Control Failure in Myelin Disorders.

Frontiers in molecular neuroscience

Volpi VG, Touvier T, D'Antonio M.
PMID: 28101003
Front Mol Neurosci. 2017 Jan 04;9:162. doi: 10.3389/fnmol.2016.00162. eCollection 2016.

Reaching the correct three-dimensional structure is crucial for the proper function of a protein. The endoplasmic reticulum (ER) is the organelle where secreted and transmembrane proteins are synthesized and folded. To guarantee high fidelity of protein synthesis and maturation...

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Volpi VG, Touvier T, D'Antonio M. Endoplasmic Reticulum Protein Quality Control Failure in Myelin Disorders. Front Mol Neurosci. 2017;9:162doi: 10.3389/fnmol.2016.00162.
Volpi, V. G., Touvier, T., & D'Antonio, M. (2016). Endoplasmic Reticulum Protein Quality Control Failure in Myelin Disorders. Frontiers in molecular neuroscience, 9162. https://doi.org/10.3389/fnmol.2016.00162
Volpi, Vera G, et al. "Endoplasmic Reticulum Protein Quality Control Failure in Myelin Disorders." Frontiers in molecular neuroscience vol. 9 (2016): 162. doi: https://doi.org/10.3389/fnmol.2016.00162
Volpi VG, Touvier T, D'Antonio M. Endoplasmic Reticulum Protein Quality Control Failure in Myelin Disorders. Front Mol Neurosci. 2017 Jan 04;9:162. doi: 10.3389/fnmol.2016.00162. eCollection 2016. PMID: 28101003; PMCID: PMC5209374.
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The Influence of Neuron-Extrinsic Factors and Aging on Injury Progression and Axonal Repair in the Central Nervous System.

Frontiers in cell and developmental biology

Sutherland TC, Geoffroy CG.
PMID: 32269994
Front Cell Dev Biol. 2020 Mar 25;8:190. doi: 10.3389/fcell.2020.00190. eCollection 2020.

In the aging western population, the average age of incidence for spinal cord injury (SCI) has increased, as has the length of survival of SCI patients. This places great importance on understanding SCI in middle-aged and aging patients. Axon...

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Sutherland TC, Geoffroy CG. The Influence of Neuron-Extrinsic Factors and Aging on Injury Progression and Axonal Repair in the Central Nervous System. Front Cell Dev Biol. 2020;8:190doi: 10.3389/fcell.2020.00190.
Sutherland, T. C., & Geoffroy, C. G. (2020). The Influence of Neuron-Extrinsic Factors and Aging on Injury Progression and Axonal Repair in the Central Nervous System. Frontiers in cell and developmental biology, 8190. https://doi.org/10.3389/fcell.2020.00190
Sutherland, Theresa C, and Geoffroy, Cédric G. "The Influence of Neuron-Extrinsic Factors and Aging on Injury Progression and Axonal Repair in the Central Nervous System." Frontiers in cell and developmental biology vol. 8 (2020): 190. doi: https://doi.org/10.3389/fcell.2020.00190
Sutherland TC, Geoffroy CG. The Influence of Neuron-Extrinsic Factors and Aging on Injury Progression and Axonal Repair in the Central Nervous System. Front Cell Dev Biol. 2020 Mar 25;8:190. doi: 10.3389/fcell.2020.00190. eCollection 2020. PMID: 32269994; PMCID: PMC7109259.
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Herpesviruses and the hidden links to Multiple Sclerosis neuropathology.

Journal of neuroimmunology

Jakhmola S, Upadhyay A, Jain K, Mishra A, Jha HC.
PMID: 34174587
J Neuroimmunol. 2021 Sep 15;358:577636. doi: 10.1016/j.jneuroim.2021.577636. Epub 2021 Jun 19.

Herpesviruses like Epstein-Barr virus, human herpesvirus (HHV)-6, HHV-1, VZV, and human endogenous retroviruses, have an age-old clinical association with multiple sclerosis (MS). MS is an autoimmune disease of the nervous system wherein the myelin sheath deteriorates. The most popular...

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Jakhmola S, Upadhyay A, Jain K, et al. Herpesviruses and the hidden links to Multiple Sclerosis neuropathology. J Neuroimmunol. 2021;358:577636doi: 10.1016/j.jneuroim.2021.577636.
Jakhmola, S., Upadhyay, A., Jain, K., Mishra, A., & Jha, H. C. (2021). Herpesviruses and the hidden links to Multiple Sclerosis neuropathology. Journal of neuroimmunology, 358577636. https://doi.org/10.1016/j.jneuroim.2021.577636
Jakhmola, Shweta, et al. "Herpesviruses and the hidden links to Multiple Sclerosis neuropathology." Journal of neuroimmunology vol. 358 (2021): 577636. doi: https://doi.org/10.1016/j.jneuroim.2021.577636
Jakhmola S, Upadhyay A, Jain K, Mishra A, Jha HC. Herpesviruses and the hidden links to Multiple Sclerosis neuropathology. J Neuroimmunol. 2021 Sep 15;358:577636. doi: 10.1016/j.jneuroim.2021.577636. Epub 2021 Jun 19. PMID: 34174587.
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Blocking Kallikrein 6 promotes developmental myelination.

Glia

Yoon H, Triplet EM, Simon WL, Choi CI, Kleppe LS, De Vita E, Miller AK, Scarisbrick IA.
PMID: 34626143
Glia. 2022 Mar;70(3):430-450. doi: 10.1002/glia.24100. Epub 2021 Oct 09.

Kallikrein related peptidase 6 (Klk6) is a secreted serine protease highly expressed in oligodendrocytes and implicated in demyelinating conditions. To gain insights into the significance of Klk6 to oligodendrocyte biology, we investigated the impact of global Klk6 gene knockout...

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Yoon H, Triplet EM, Simon WL, et al. Blocking Kallikrein 6 promotes developmental myelination. Glia. 2021;70(3):430-450doi: 10.1002/glia.24100.
Yoon, H., Triplet, E. M., Simon, W. L., Choi, C. I., Kleppe, L. S., De Vita, E., Miller, A. K., & Scarisbrick, I. A. (2022). Blocking Kallikrein 6 promotes developmental myelination. Glia, 70(3), 430-450. https://doi.org/10.1002/glia.24100
Yoon, Hyesook, et al. "Blocking Kallikrein 6 promotes developmental myelination." Glia vol. 70,3 (2022): 430-450. doi: https://doi.org/10.1002/glia.24100
Yoon H, Triplet EM, Simon WL, Choi CI, Kleppe LS, De Vita E, Miller AK, Scarisbrick IA. Blocking Kallikrein 6 promotes developmental myelination. Glia. 2022 Mar;70(3):430-450. doi: 10.1002/glia.24100. Epub 2021 Oct 09. PMID: 34626143.
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Blocking Kallikrein 6 promotes developmental myelination.

Glia

Yoon H, Triplet EM, Simon WL, Choi CI, Kleppe LS, De Vita E, Miller AK, Scarisbrick IA.
PMID: 34626143
Glia. 2022 Mar;70(3):430-450. doi: 10.1002/glia.24100. Epub 2021 Oct 09.

Kallikrein related peptidase 6 (Klk6) is a secreted serine protease highly expressed in oligodendrocytes and implicated in demyelinating conditions. To gain insights into the significance of Klk6 to oligodendrocyte biology, we investigated the impact of global Klk6 gene knockout...

Cite
Yoon H, Triplet EM, Simon WL, et al. Blocking Kallikrein 6 promotes developmental myelination. Glia. 2021;70(3):430-450doi: 10.1002/glia.24100.
Yoon, H., Triplet, E. M., Simon, W. L., Choi, C. I., Kleppe, L. S., De Vita, E., Miller, A. K., & Scarisbrick, I. A. (2022). Blocking Kallikrein 6 promotes developmental myelination. Glia, 70(3), 430-450. https://doi.org/10.1002/glia.24100
Yoon, Hyesook, et al. "Blocking Kallikrein 6 promotes developmental myelination." Glia vol. 70,3 (2022): 430-450. doi: https://doi.org/10.1002/glia.24100
Yoon H, Triplet EM, Simon WL, Choi CI, Kleppe LS, De Vita E, Miller AK, Scarisbrick IA. Blocking Kallikrein 6 promotes developmental myelination. Glia. 2022 Mar;70(3):430-450. doi: 10.1002/glia.24100. Epub 2021 Oct 09. PMID: 34626143.
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Clemastine improves electrophysiologic and histomorphometric changes through promoting myelin repair in a murine model of compression neuropathy.

Scientific reports

Lee JI, Park JW, Lee KJ, Lee DH.
PMID: 34686718
Sci Rep. 2021 Oct 22;11(1):20886. doi: 10.1038/s41598-021-00389-1.

Compression neuropathies are common and debilitating conditions that result in variable functional recovery after surgical decompression. Recent drug repurposing studies have verified that clemastine promotes functional recovery through enhancement of myelin repair in demyelinating disease. We investigated the utility...

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Lee JI, Park JW, Lee KJ, et al. Clemastine improves electrophysiologic and histomorphometric changes through promoting myelin repair in a murine model of compression neuropathy. Sci Rep. 2021;11(1):20886doi: 10.1038/s41598-021-00389-1.
Lee, J. I., Park, J. W., Lee, K. J., & Lee, D. H. (2021). Clemastine improves electrophysiologic and histomorphometric changes through promoting myelin repair in a murine model of compression neuropathy. Scientific reports, 11(1), 20886. https://doi.org/10.1038/s41598-021-00389-1
Lee, Jung Il, et al. "Clemastine improves electrophysiologic and histomorphometric changes through promoting myelin repair in a murine model of compression neuropathy." Scientific reports vol. 11,1 (2021): 20886. doi: https://doi.org/10.1038/s41598-021-00389-1
Lee JI, Park JW, Lee KJ, Lee DH. Clemastine improves electrophysiologic and histomorphometric changes through promoting myelin repair in a murine model of compression neuropathy. Sci Rep. 2021 Oct 22;11(1):20886. doi: 10.1038/s41598-021-00389-1. PMID: 34686718; PMCID: PMC8536687.
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Hypomyelinating leukodystrophies - unravelling myelin biology.

Nature reviews. Neurology

Wolf NI, Ffrench-Constant C, van der Knaap MS.
PMID: 33324001
Nat Rev Neurol. 2021 Feb;17(2):88-103. doi: 10.1038/s41582-020-00432-1. Epub 2020 Dec 15.

Hypomyelinating leukodystrophies constitute a subset of genetic white matter disorders characterized by a primary lack of myelin deposition. Most patients with severe hypomyelination present in infancy or early childhood and develop severe neurological deficits, but the clinical presentation can...

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Wolf NI, Ffrench-Constant C, van der Knaap MS. Hypomyelinating leukodystrophies - unravelling myelin biology. Nat Rev Neurol. 2020;17(2):88-103doi: 10.1038/s41582-020-00432-1.
Wolf, N. I., Ffrench-Constant, C., & van der Knaap, M. S. (2021). Hypomyelinating leukodystrophies - unravelling myelin biology. Nature reviews. Neurology, 17(2), 88-103. https://doi.org/10.1038/s41582-020-00432-1
Wolf, Nicole I, et al. "Hypomyelinating leukodystrophies - unravelling myelin biology." Nature reviews. Neurology vol. 17,2 (2021): 88-103. doi: https://doi.org/10.1038/s41582-020-00432-1
Wolf NI, Ffrench-Constant C, van der Knaap MS. Hypomyelinating leukodystrophies - unravelling myelin biology. Nat Rev Neurol. 2021 Feb;17(2):88-103. doi: 10.1038/s41582-020-00432-1. Epub 2020 Dec 15. PMID: 33324001.
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Showing 61 to 71 of 71 entries