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Showing 13 to 24 of 71 entries
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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; PMCID: PMC8732303.
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Dysregulation in Subcellular Localization of Myelin Basic Protein mRNA Does Not Result in Altered Myelination in Amyotrophic Lateral Sclerosis.

Frontiers in neuroscience

Barton SK, Gregory JM, Selvaraj BT, McDade K, Henstridge CM, Spires-Jones TL, James OG, Mehta AR, Story D, Burr K, Magnani D, Isaacs AM, Smith C, Chandran S.
PMID: 34539336
Front Neurosci. 2021 Sep 01;15:705306. doi: 10.3389/fnins.2021.705306. eCollection 2021.

Pathological hallmarks of amyotrophic lateral sclerosis (ALS), including protein misfolding, are well established in oligodendrocytes. More recently, an RNA trafficking deficit of key myelin proteins has been suggested in oligodendrocytes in ALS but the extent to which this affects...

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Barton SK, Gregory JM, Selvaraj BT, et al. Dysregulation in Subcellular Localization of Myelin Basic Protein mRNA Does Not Result in Altered Myelination in Amyotrophic Lateral Sclerosis. Front Neurosci. 2021;15:705306doi: 10.3389/fnins.2021.705306.
Barton, S. K., Gregory, J. M., Selvaraj, B. T., McDade, K., Henstridge, C. M., Spires-Jones, T. L., James, O. G., Mehta, A. R., Story, D., Burr, K., Magnani, D., Isaacs, A. M., Smith, C., & Chandran, S. (2021). Dysregulation in Subcellular Localization of Myelin Basic Protein mRNA Does Not Result in Altered Myelination in Amyotrophic Lateral Sclerosis. Frontiers in neuroscience, 15705306. https://doi.org/10.3389/fnins.2021.705306
Barton, Samantha K, et al. "Dysregulation in Subcellular Localization of Myelin Basic Protein mRNA Does Not Result in Altered Myelination in Amyotrophic Lateral Sclerosis." Frontiers in neuroscience vol. 15 (2021): 705306. doi: https://doi.org/10.3389/fnins.2021.705306
Barton SK, Gregory JM, Selvaraj BT, McDade K, Henstridge CM, Spires-Jones TL, James OG, Mehta AR, Story D, Burr K, Magnani D, Isaacs AM, Smith C, Chandran S. Dysregulation in Subcellular Localization of Myelin Basic Protein mRNA Does Not Result in Altered Myelination in Amyotrophic Lateral Sclerosis. Front Neurosci. 2021 Sep 01;15:705306. doi: 10.3389/fnins.2021.705306. eCollection 2021. PMID: 34539336; PMCID: PMC8440970.
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Recent Advances in Antigen-Specific Immunotherapies for the Treatment of Multiple Sclerosis.

Brain sciences

Kammona O, Kiparissides C.
PMID: 32486045
Brain Sci. 2020 May 29;10(6). doi: 10.3390/brainsci10060333.

Multiple sclerosis (MS) is an autoimmune disease of the central nervous system and is considered to be the leading non-traumatic cause of neurological disability in young adults. Current treatments for MS comprise long-term immunosuppressant drugs and disease-modifying therapies (DMTs)...

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Kammona O, Kiparissides C. Recent Advances in Antigen-Specific Immunotherapies for the Treatment of Multiple Sclerosis. Brain Sci. 2020;10(6)doi: 10.3390/brainsci10060333.
Kammona, O., & Kiparissides, C. (2020). Recent Advances in Antigen-Specific Immunotherapies for the Treatment of Multiple Sclerosis. Brain sciences, 10(6), . https://doi.org/10.3390/brainsci10060333
Kammona, Olga, and Kiparissides, Costas. "Recent Advances in Antigen-Specific Immunotherapies for the Treatment of Multiple Sclerosis." Brain sciences vol. 10,6 (2020). doi: https://doi.org/10.3390/brainsci10060333
Kammona O, Kiparissides C. Recent Advances in Antigen-Specific Immunotherapies for the Treatment of Multiple Sclerosis. Brain Sci. 2020 May 29;10(6). doi: 10.3390/brainsci10060333. PMID: 32486045; PMCID: PMC7348736.
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Distinct T cell signatures define subsets of patients with multiple sclerosis.

Neurology(R) neuroimmunology & neuroinflammation

Johnson MC, Pierson ER, Spieker AJ, Nielsen AS, Posso S, Kita M, Buckner JH, Goverman JM.
PMID: 27606354
Neurol Neuroimmunol Neuroinflamm. 2016 Aug 23;3(5):e278. doi: 10.1212/NXI.0000000000000278. eCollection 2016 Oct.

OBJECTIVE: We investigated T cell responses to myelin proteins in the blood of healthy controls and 2 groups of patients with relapsing-remitting multiple sclerosis (RRMS) who exhibited lesions either predominantly in the brain or predominantly in the spinal cord...

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Johnson MC, Pierson ER, Spieker AJ, et al. Distinct T cell signatures define subsets of patients with multiple sclerosis. Neurol Neuroimmunol Neuroinflamm. 2016;3(5):e278doi: 10.1212/NXI.0000000000000278.
Johnson, M. C., Pierson, E. R., Spieker, A. J., Nielsen, A. S., Posso, S., Kita, M., Buckner, J. H., & Goverman, J. M. (2016). Distinct T cell signatures define subsets of patients with multiple sclerosis. Neurology(R) neuroimmunology & neuroinflammation, 3(5), e278. https://doi.org/10.1212/NXI.0000000000000278
Johnson, Mark C, et al. "Distinct T cell signatures define subsets of patients with multiple sclerosis." Neurology(R) neuroimmunology & neuroinflammation vol. 3,5 (2016): e278. doi: https://doi.org/10.1212/NXI.0000000000000278
Johnson MC, Pierson ER, Spieker AJ, Nielsen AS, Posso S, Kita M, Buckner JH, Goverman JM. Distinct T cell signatures define subsets of patients with multiple sclerosis. Neurol Neuroimmunol Neuroinflamm. 2016 Aug 23;3(5):e278. doi: 10.1212/NXI.0000000000000278. eCollection 2016 Oct. PMID: 27606354; PMCID: PMC4996538.
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Localization of Myelin Proteins in the Developing Shark Spinal Cord.

The Biological bulletin

Gould RM, Spivack WD, Gilland E, Pant HC, Tseng D.
PMID: 29300646
Biol Bull. 1992 Oct;183(2):358-359. doi: 10.1086/BBLv183n2p358.

No abstract available.

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Gould RM, Spivack WD, Gilland E, et al. Localization of Myelin Proteins in the Developing Shark Spinal Cord. Biol Bull. 1992;183(2):358-359doi: 10.1086/BBLv183n2p358.
Gould, R. M., Spivack, W. D., Gilland, E., Pant, H. C., & Tseng, D. (1992). Localization of Myelin Proteins in the Developing Shark Spinal Cord. The Biological bulletin, 183(2), 358-359. https://doi.org/10.1086/BBLv183n2p358
Gould, R M, et al. "Localization of Myelin Proteins in the Developing Shark Spinal Cord." The Biological bulletin vol. 183,2 (1992): 358-359. doi: https://doi.org/10.1086/BBLv183n2p358
Gould RM, Spivack WD, Gilland E, Pant HC, Tseng D. Localization of Myelin Proteins in the Developing Shark Spinal Cord. Biol Bull. 1992 Oct;183(2):358-359. doi: 10.1086/BBLv183n2p358. PMID: 29300646.
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Role of Calpain in Spinal Cord Injury: Effects of Calpain and Free Radical Inhibitors.

Annals of the New York Academy of Sciences

Banik NL, Shields DC, Ray S, Davis B, Matzelle D, Wilford G, Hogan EL.
PMID: 29090802
Ann N Y Acad Sci. 1998 May;844(1):131-137. doi: 10.1111/j.1749-6632.1998.tb08228.x.

The demonstration of increased calpain activity, immunostaining, and expression at the gene (mRNA) and protein levels concomitant with ultrastructural degeneration and loss of axon and myelin proteins in lesioned cord have implicated a pivotal role for calpain in tissue...

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Banik NL, Shields DC, Ray S, et al. Role of Calpain in Spinal Cord Injury: Effects of Calpain and Free Radical Inhibitors. Ann N Y Acad Sci. 1998;844(1):131-137doi: 10.1111/j.1749-6632.1998.tb08228.x.
Banik, N. L., Shields, D. C., Ray, S., Davis, B., Matzelle, D., Wilford, G., & Hogan, E. L. (1998). Role of Calpain in Spinal Cord Injury: Effects of Calpain and Free Radical Inhibitors. Annals of the New York Academy of Sciences, 844(1), 131-137. https://doi.org/10.1111/j.1749-6632.1998.tb08228.x
Banik, N L, et al. "Role of Calpain in Spinal Cord Injury: Effects of Calpain and Free Radical Inhibitors." Annals of the New York Academy of Sciences vol. 844,1 (1998): 131-137. doi: https://doi.org/10.1111/j.1749-6632.1998.tb08228.x
Banik NL, Shields DC, Ray S, Davis B, Matzelle D, Wilford G, Hogan EL. Role of Calpain in Spinal Cord Injury: Effects of Calpain and Free Radical Inhibitors. Ann N Y Acad Sci. 1998 May;844(1):131-137. doi: 10.1111/j.1749-6632.1998.tb08228.x. PMID: 29090802.
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Appearance of Myelin proteins during vertebrate evolution.

Neurochemistry international

Waehneldt TV, Matthieu JM, Jeserich G.
PMID: 20493148
Neurochem Int. 1986;9(4):463-74. doi: 10.1016/0197-0186(86)90136-1.

Myelin, defined as an arrangement of spirally fused unit membranes, is an acquisition of vertebrates and first appeared during evolution in Gnathostomata. In all species studied PNS and CNS myelins contain the myelin-associated glycoprotein (MAG) and the myelin basic...

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Waehneldt TV, Matthieu JM, Jeserich G. Appearance of Myelin proteins during vertebrate evolution. Neurochem Int. 1986;9(4):463-74doi: 10.1016/0197-0186(86)90136-1.
Waehneldt, T. V., Matthieu, J. M., & Jeserich, G. (1986). Appearance of Myelin proteins during vertebrate evolution. Neurochemistry international, 9(4), 463-74. https://doi.org/10.1016/0197-0186(86)90136-1
Waehneldt, T V, et al. "Appearance of Myelin proteins during vertebrate evolution." Neurochemistry international vol. 9,4 (1986): 463-74. doi: https://doi.org/10.1016/0197-0186(86)90136-1
Waehneldt TV, Matthieu JM, Jeserich G. Appearance of Myelin proteins during vertebrate evolution. Neurochem Int. 1986;9(4):463-74. doi: 10.1016/0197-0186(86)90136-1. PMID: 20493148.
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NG2 cells response to axonal alteration in the spinal cord white matter in mice with genetic disruption of neurofilament light subunit expression.

Molecular neurodegeneration

Wu YJ, Tang YF, Xiao ZC, Bao ZM, He BP.
PMID: 18957081
Mol Neurodegener. 2008 Oct 28;3:18. doi: 10.1186/1750-1326-3-18.

BACKGROUND: Chondroitin sulphate proteoglycan (NG2) expressing cells, morphologically characterized by multi-branched processes and small cell bodies, are the 4th commonest cell population of non-neuronal cell type in the central nervous system (CNS). They can interact with nodes of Ranvier,...

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Wu YJ, Tang YF, Xiao ZC, et al. NG2 cells response to axonal alteration in the spinal cord white matter in mice with genetic disruption of neurofilament light subunit expression. Mol Neurodegener. 2008;3:18doi: 10.1186/1750-1326-3-18.
Wu, Y. J., Tang, Y. F., Xiao, Z. C., Bao, Z. M., & He, B. P. (2008). NG2 cells response to axonal alteration in the spinal cord white matter in mice with genetic disruption of neurofilament light subunit expression. Molecular neurodegeneration, 318. https://doi.org/10.1186/1750-1326-3-18
Wu, Ya Jun, et al. "NG2 cells response to axonal alteration in the spinal cord white matter in mice with genetic disruption of neurofilament light subunit expression." Molecular neurodegeneration vol. 3 (2008): 18. doi: https://doi.org/10.1186/1750-1326-3-18
Wu YJ, Tang YF, Xiao ZC, Bao ZM, He BP. NG2 cells response to axonal alteration in the spinal cord white matter in mice with genetic disruption of neurofilament light subunit expression. Mol Neurodegener. 2008 Oct 28;3:18. doi: 10.1186/1750-1326-3-18. PMID: 18957081; PMCID: PMC2584033.
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Nervous system myelin in the electric ray, Torpedo marmorata: Morphological characterization of the membrane and biochemical analysis of its protein components.

Neurochemistry international

Waehneldt TV, Kiene ML, Malotka J, Kiecke C, Neuhoff V.
PMID: 20488042
Neurochem Int. 1984;6(2):223-35. doi: 10.1016/0197-0186(84)90097-4.

In Torpedo, PNS as well as CNS myelines are characterized by clearly separated double intraperiod lines. CNS myelin of Torpedo contains two glycosylated hydrophobic proteins labelled T1 (25,800 Da1) and T2 (29,700 Da1), and two basic proteins BP1 and...

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Waehneldt TV, Kiene ML, Malotka J, et al. Nervous system myelin in the electric ray, Torpedo marmorata: Morphological characterization of the membrane and biochemical analysis of its protein components. Neurochem Int. 1984;6(2):223-35doi: 10.1016/0197-0186(84)90097-4.
Waehneldt, T. V., Kiene, M. L., Malotka, J., Kiecke, C., & Neuhoff, V. (1984). Nervous system myelin in the electric ray, Torpedo marmorata: Morphological characterization of the membrane and biochemical analysis of its protein components. Neurochemistry international, 6(2), 223-35. https://doi.org/10.1016/0197-0186(84)90097-4
Waehneldt, T V, et al. "Nervous system myelin in the electric ray, Torpedo marmorata: Morphological characterization of the membrane and biochemical analysis of its protein components." Neurochemistry international vol. 6,2 (1984): 223-35. doi: https://doi.org/10.1016/0197-0186(84)90097-4
Waehneldt TV, Kiene ML, Malotka J, Kiecke C, Neuhoff V. Nervous system myelin in the electric ray, Torpedo marmorata: Morphological characterization of the membrane and biochemical analysis of its protein components. Neurochem Int. 1984;6(2):223-35. doi: 10.1016/0197-0186(84)90097-4. PMID: 20488042.
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A 13C NMR spin-lattice relaxation study of the interaction of myelin proteins with lipid vesicles.

Biophysical chemistry

A Keniry M, Smith R.
PMID: 17000147
Biophys Chem. 1980 Aug;12(1):133-41.

Natural abundance 13C nuclear magnetic spin-lattice relaxation times have been measured for bovine brain phosphatidylserine vesicles with and without bound proteins. The relaxation times were lower than published values for the corresponding nuclei in egg phosphatidylcholine, but showed the...

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A Keniry M, Smith R. A 13C NMR spin-lattice relaxation study of the interaction of myelin proteins with lipid vesicles. Biophys Chem. 1980;12(1):133-41
A Keniry, M., & Smith, R. (1980). A 13C NMR spin-lattice relaxation study of the interaction of myelin proteins with lipid vesicles. Biophysical chemistry, 12(1), 133-41.
A Keniry, M, and Smith, R. "A 13C NMR spin-lattice relaxation study of the interaction of myelin proteins with lipid vesicles." Biophysical chemistry vol. 12,1 (1980): 133-41.
A Keniry M, Smith R. A 13C NMR spin-lattice relaxation study of the interaction of myelin proteins with lipid vesicles. Biophys Chem. 1980 Aug;12(1):133-41. PMID: 17000147.
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Changes in protein content of developing brain synaptic membranes, mitochondria and myelin.

Neuroscience letters

Jones DH, Matus AI.
PMID: 19604778
Neurosci Lett. 1975 Sep;1(3):153-8. doi: 10.1016/0304-3940(75)90031-2.

The development of myelin, synaptosomal plasma membranes (SPM) and mitochondria in neonatal rat cortex has been followed by examining the electrophoretic profiles of protein in brain subcellular fractions. The appearance of the myelin proteins parallels the time course of...

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Jones DH, Matus AI. Changes in protein content of developing brain synaptic membranes, mitochondria and myelin. Neurosci Lett. 1975;1(3):153-8doi: 10.1016/0304-3940(75)90031-2.
Jones, D. H., & Matus, A. I. (1975). Changes in protein content of developing brain synaptic membranes, mitochondria and myelin. Neuroscience letters, 1(3), 153-8. https://doi.org/10.1016/0304-3940(75)90031-2
Jones, D H, and Matus, A I. "Changes in protein content of developing brain synaptic membranes, mitochondria and myelin." Neuroscience letters vol. 1,3 (1975): 153-8. doi: https://doi.org/10.1016/0304-3940(75)90031-2
Jones DH, Matus AI. Changes in protein content of developing brain synaptic membranes, mitochondria and myelin. Neurosci Lett. 1975 Sep;1(3):153-8. doi: 10.1016/0304-3940(75)90031-2. PMID: 19604778.
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Crystallographic anomalous diffraction data for the experimental phasing of two myelin proteins, gliomedin and periaxin.

Data in brief

Han H, Kursula P.
PMID: 28861438
Data Brief. 2017 Mar 06;11:552-556. doi: 10.1016/j.dib.2017.02.049. eCollection 2017 Apr.

We present datasets that can be used for the experimental phasing of crystal structures of two myelin proteins. The structures were recently described in the articles "Periaxin and AHNAK nucleoprotein 2 form intertwined homodimers through domain swapping" (H. Han,...

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Han H, Kursula P. Crystallographic anomalous diffraction data for the experimental phasing of two myelin proteins, gliomedin and periaxin. Data Brief. 2017;11:552-556doi: 10.1016/j.dib.2017.02.049.
Han, H., & Kursula, P. (2017). Crystallographic anomalous diffraction data for the experimental phasing of two myelin proteins, gliomedin and periaxin. Data in brief, 11552-556. https://doi.org/10.1016/j.dib.2017.02.049
Han, Huijong, and Kursula, Petri. "Crystallographic anomalous diffraction data for the experimental phasing of two myelin proteins, gliomedin and periaxin." Data in brief vol. 11 (2017): 552-556. doi: https://doi.org/10.1016/j.dib.2017.02.049
Han H, Kursula P. Crystallographic anomalous diffraction data for the experimental phasing of two myelin proteins, gliomedin and periaxin. Data Brief. 2017 Mar 06;11:552-556. doi: 10.1016/j.dib.2017.02.049. eCollection 2017 Apr. PMID: 28861438; PMCID: PMC5567927.
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Showing 13 to 24 of 71 entries