Cited by 256Prion Diseases and Protein MisfoldingAlzheimer's disease research and treatmentsSkin and Cellular Biology Research

The DOI matches its Crossref record; 67 of the 67 references it cites were found in a registry or an index.

Mice devoid of the glial fibrillary acidic protein develop normally and are susceptible to scrapie prions

Open access

Gomi, Hiroshi, Yokoyama, Takashi, Fujimoto, Kazushi, Ikeda, Toshio, Katoh, Akira, Itoh, Takeshi, Itohara, Shigeyoshi·1995·Neuron

DOI 10.1016/0896-6273(95)90238-4

Open this paper in CoChat — free account

Abstract

Glial fibrillary acidic protein (GFAP) is an intermediate filament protein specifically expressed in astrocytes in the CNS. To examine the function of GFAP in vivo, the Gfap gene was disrupted by gene targeting in embryonic stem cells. Mice homozygous for the mutation were completely devoid of GFAP but exhibited normal development and showed no obvious anatomical abnormalities in the CNS. When inoculated with infectious scrapie prions, the mutant mice exhibited neuropathological changes typical of prion diseases. Infectious prions accumulated in brains of the mutant mice to a degree similar to that in control littermates. These results suggest that GFAP is not essential for the morphogenesis of the CNS or for astrocytic responses against neuronal injury. The results argue against the hypothesis that GFAP plays a crucial role in the pathogenesis of prion diseases.

Integrity signals

Registry

Crossref · 10.1016/0896-6273(95)90238-4

Cites

67 of 67 references verified0 citation errors · 0 not checkable

Statistics

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

Claims the paper makes

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

Claims other papers make about this one

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

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Novel Proteinaceous Infectious Particles Cause Scrapie
Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,221
CNS stem cells express a new class of intermediate filament protein
Lendahl, U., Zimmerman, L. B., & McKay, R. D. G. (1990) · Cell · doi:10.1016/0092-8674(90)90662-x · Cited by 3,164
FINE STRUCTURAL LOCALIZATION OF A BLOOD-BRAIN BARRIER TO EXOGENOUS PEROXIDASE
Reese, T. S., & Karnovsky, M. J. (1967) · The Journal of Cell Biology · doi:10.1083/jcb.34.1.207 · Cited by 2,629
Mode of cell migration to the superficial layers of fetal monkey neocortex
Rakic, P. (1972) · Journal of Comparative Neurology · doi:10.1002/cne.901450105 · Cited by 2,170
Mice devoid of PrP are resistant to scrapie
Büeler, H., Aguzzi, A., Sailer, A. W., Greiner, R., Autenried, P., Aguet, M., & Weissmann, C. (1993) · Cell · doi:10.1016/0092-8674(93)90360-3 · Cited by 2,107
Altering the Genome by Homologous Recombination
Capecchi, M. R. (1989) · Science · doi:10.1126/science.2660260 · Cited by 2,037
Molecular Biology of Prion Diseases
Prusiner, S. B. (1991) · Science · doi:10.1126/science.1675487 · Cited by 1,975
Astrocytes induce blood–brain barrier properties in endothelial cells
Janzer, R. C., & RAFF, M. C. (1987) · Nature · doi:10.1038/325253a0 · Cited by 1,613
Untitled work
(1991) · Medical Entomology and Zoology · Cited by 1,512

Show all 67 references

Sorted by citations

Items 101–200 of 255

Alexander-disease mutation ofGFAPcauses filament disorganization and decreased solubility of GFAP
Hsiao, V. C., Tian, R., Long, H. A., Perng, M. D., Brenner, M., Quinlan, R. A., & Goldman, J. E. (2005) · Journal of Cell Science · doi:10.1242/jcs.02339 · Cited by 79
Glial scar and axonal regeneration in the CNS: lessons from GFAP and vimentin transgenic mice
Ribotta, M. G. Y., Menet, V., & Privat, A. (2004) · Springer eBooks · doi:10.1007/978-3-7091-0603-7_12 · Cited by 78
Antisense Oligonucleotide Therapy for the Nervous System: From Bench to Bedside with Emphasis on Pediatric Neurology
Amanat, M., Nemeth, C. L., Fine, A. S., Leung, D. G., & Fatemi, A. S. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14112389 · Cited by 78
The Intermediate Filament GFAP Is Important for the Control of Experimental MurineStaphylococcus aureus-Induced Brain Abscess andToxoplasmaEncephalitis
Stenzel, W., Soltek, S., Schlüter, D., & Deckert, M. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.6.631 · Cited by 74
Formation of Normal Desmin Intermediate Filaments in Mouse Hepatic Stellate Cells Requires Vimentin
Geerts, A. E., Eliasson, C., Niki, T., Wielant, A., Vaeyens, F., & Pekny, M. (2001) · Hepatology · doi:10.1053/jhep.2001.21045 · Cited by 75
Enhanced hippocampal neurodegeneration after traumatic or kainate excitotoxicity in GFAP-null mice
Otani, N., Nawashiro, H., Fukui, S., Ooigawa, H., Ohsumi, A., Toyooka, T., Shima, K., Gomi, H., & Brenner, M. (2006) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2005.10.018 · Cited by 73
Self-citation
Prion-mediated neurodegeneration is associated with early impairment of the ubiquitin–proteasome system
McKinnon, C., Goold, R., André, R., Devoy, A., Ortega, Z., Moonga, J., Linehan, J. M., Brandner, S., Lucas, J. J., Collinge, J., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1508-y · Cited by 72
Axonal and Nonneuronal Cell Responses to Spinal Cord Injury in Mice Lacking Glial Fibrillary Acidic Protein
Wang, X., Messing, A., & David, S. (1997) · Experimental Neurology · doi:10.1006/exnr.1997.6702 · Cited by 72
Effects of acute delivery of endothelin-1 on retinal ganglion cell loss in the rat
Lau, J., Dang, M., Hockmann, K., & Ball, A. K. (2005) · Experimental Eye Research · doi:10.1016/j.exer.2005.06.002 · Cited by 71
The AP-1 transcription factor JunB is required for Th17 cell differentiation
Yamazaki, S., Tanaka, Y., Araki, H., Kohda, A., Sanematsu, F., Arasaki, T., Duan, X., Miura, F., Katagiri, T., Shindo, R., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-17597-3 · Cited by 77
Aberrant Maturation of Astrocytes in Thyroid Hormone Receptor α1 Knockout Mice Reveals an Interplay between Thyroid Hormone Receptor Isoforms
Morte, B., Manzano, J., Scanlan, T. S., Vennström, B., & Bernal, J. (2003) · Endocrinology · doi:10.1210/en.2003-1123 · Cited by 68
Effect of elevated K+, hypotonic stress, and cortical spreading depression on astrocyte swelling in GFAP‐deficient mice
Anděrová, M., Kubinová, Š., Mazel, T., Chvátal, A., Eliasson, C., Pekny, M., & Syková, E. (2001) · Glia · doi:10.1002/glia.1084 · Cited by 69
Doc2α is an activity‐dependent modulator of excitatory synaptic transmission
Sakaguchi, G., Manabe, T., Kobayashi, K., Orita, S., Sasaki, T., Naito, A., Maeda, M. H., Igarashi, H., Katsuura, G., Nishioka, H., et al. (1999) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.1999.00855.x · Cited by 66
Self-citation
Untitled work
(1999) · doi:10.1002/(sici)1098-1136(19990215)25:4
Intermediate filaments and their associated proteins: multiple dynamic personalities
Houseweart, M. K., & Cleveland, D. W. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80091-4 · Cited by 67
Insights into the physiological function of cellular prion protein
Martins, V. R., Mercadante, A. F., Cabral, A. L. B., Freitas, A. R. O., & Castro, R. M. R. P. S. (2001) · Brazilian Journal of Medical and Biological Research · doi:10.1590/s0100-879x2001000500005 · Cited by 66
Protective Role of Phosphorylation in Turnover of Glial Fibrillary Acidic Protein in Mice
Takemura, M., Gomi, H., Colucci‐Guyon, E., & Itohara, S. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-16-06972.2002 · Cited by 65
Self-citation
The Impact of Genetic Removal of GFAP and/or Vimentin on Glutamine Levels and Transport of Glucose and Ascorbate in Astrocytes
Pekny, M., Eliasson, C., Siushansian, R., Ding, M., Dixon, S. J., Pekna, M., Wilson, J. X., & Hamberger, A. (1999) · Neurochemical Research · doi:10.1023/a:1022572304626 · Cited by 62
Tetracycline regulated expression of vimentin in fibroblasts derived from vimentin null mice
Holwell, T. A., Schweitzer, S. C., & Evans, R. M. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.16.1947 · Cited by 64
Antisense therapy in a rat model of Alexander disease reverses GFAP pathology, white matter deficits, and motor impairment
Hagemann, T. L., Powers, B. E., Lin, N., Mohamed, A. F., Dague, K. L., Hannah, S. C., Bachmann, G., Mazur, C., Rigo, F., Olsen, A. L., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abg4711 · Cited by 62
Alexander Disease: A Genetic Disorder of Astrocytes
Brenner, M., Goldman, J. E., Quinlan, R. A., & Messing, A. (2008) · Springer eBooks · doi:10.1007/978-0-387-79492-1_24 · Cited by 61
Interaction of prion proteins with cell surface receptors, molecular chaperones, and other molecules
Gauczynski, S., Hundt, C., Leucht, C., & Weiss, S. (2001) · Advances in protein chemistry · doi:10.1016/s0065-3233(01)57024-2 · Cited by 60
Scrapie in Mice Deficient in Apolipoprotein E or Glial Fibrillary Acidic Protein
Tatzelt, J., Maeda, N., Pekny, M., Yang, S.-L., Betsholtz, C., Eliasson, C., Cayetano, J., Camerino, A. P., DeArmond, S. J., & Prusiner, S. B. (1996) · Neurology · doi:10.1212/wnl.47.2.449 · Cited by 59
Strategies for Treatment in Alexander Disease
Messing, A., Daniels, C. M. L., & Hagemann, T. L. (2010) · Neurotherapeutics · doi:10.1016/j.nurt.2010.05.013 · Cited by 60
Changes in visual fields and lateral geniculate nucleus in monkey laser-induced high intraocular pressure model
Sasaoka, M., Nakamura, K., Shimazawa, M., Ito, Y., Araie, M., & Hara, H. (2008) · Experimental Eye Research · doi:10.1016/j.exer.2008.02.004 · Cited by 59
Targeted gene disruption: applications in neurobiology
van der Neut, R. (1997) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(96)00123-9 · Cited by 57
Astrocytosis and amyloid deposition in scrapie-infected hamsters
Ye, X., Scallet, A. C., Kascsak, R. J., & Carp, R. I. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00833-6 · Cited by 57
Development of vimentin and glial fibrillary acidic protein immunoreactivities in the brain of gray mullet (Chelon labrosus), an advanced teleost
Arochena, M., Anadón, R., & Díaz‐Regueira, S. M. (2004) · The Journal of Comparative Neurology · doi:10.1002/cne.11021 · Cited by 56
Effects of inducible glial fibrillary acidic protein on glioma cell motility and proliferation
El‐Obeid, A., Bongcam‐Rudloff, E., Westermark, B., & Nist�r, M. (2000) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(20000415)60:2 · Cited by 46
Self-citation
Cellular Prion Protein (PrPc): Putative Interacting Partners and Consequences of the Interaction
Miranzadeh Mahabadi, H., & Taghibiglou, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197058 · Cited by 52
Disturbance of hippocampal long‐term potentiation after transient ischemia in GFAP deficient mice
Tanaka, H., Katoh, A., Oguro, K., Shimazaki, K., Gomi, H., Itohara, S., Masuzawa, T., & Kawai, N. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.10004 · Cited by 53
Self-citation
Genetic ablation of NMDA receptor subunit NR3B in mouse reveals motoneuronal and nonmotoneuronal phenotypes
Niemann, S., Kanki, H., Fukui, Y., Takao, K., Fukaya, M., Hynynen, M., Churchill, M., Shefner, J. M., Bronson, R. T., Brown, R. H., et al. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05774.x · Cited by 52
Self-citation
Prions prevent brain damage after experimental brain injury: a preliminary report
Hoshino, S., Inoue, K., Yokoyama, T., Kobayashi, S., Asakura, T., Teramoto, A., & Itohara, S. (2003) · Acta neurochirurgica. Supplementum · doi:10.1007/978-3-7091-0651-8_64 · Cited by 52
Self-citation
Intermediate filaments in the nervous system: implications in cancer
Ho, C., & Liem, R. K. H. (1996) · Cancer and Metastasis Reviews · doi:10.1007/bf00054014 · Cited by 52
Prion protein genotype and pathological phenotype studies in sporadic Creutzfeldt‐Jakob disease
MacDonald, S. T., Sutherland, K., & Ironside, J. W. (1996) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.1996.tb01106.x · Cited by 52
Proliferative reactive gliosis is compatible with glial metabolic support and neuronal function
Vázquez-Chona, F., Swan, A. G., Ferrell, W. D., Jiang, L., Baehr, W., Chien, W., Fero, M. L., Marc, R. E., & Levine, E. M. (2011) · BMC Neuroscience · doi:10.1186/1471-2202-12-98 · Cited by 46
Pael receptor is involved in dopamine metabolism in the nigrostriatal system
Imai, Y., Inoue, H., Kataoka, A., Wang, H., Masuda, M., Ikeda, T., Tsukita, K., Soda, M., Kodama, T., Fuwa, T., et al. (2007) · Neuroscience Research · doi:10.1016/j.neures.2007.08.005 · Cited by 45
Self-citation
Rat oligodendrocytes express the vitamin D3 receptor and respond to 1,25-dihydroxyvitamin D3
Baas, D., Pr�fer, K., Ittel, M. E., Kuchler‐Bopp, S., Labourdette, G., Sarli�ve, L. L., & Brachet, P. (2000) · Glia · doi:10.1002/(sici)1098-1136(200007)31:1 · Cited by 146
Aspirin-induced blockade of NF-κB activity restrains up-regulation of glial fibrillary acidic protein in human astroglial cells
Bae, M., Kim, S.-R., Lee, H.-J., Wee, H., Yoo, M., Oh, S. O., Baek, S., Kim, B.-S., Kim, J.-B., Sik-Yoon, et al. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.01.005 · Cited by 44
From structural resilience to cell specification — Intermediate filaments as regulators of cell fate
Sjöqvist, M., Antfolk, D., Rodriguez, F. S., & Sahlgren, C. (2020) · The FASEB Journal · doi:10.1096/fj.202001627r · Cited by 43
Expression of NR1 and NR2A/B subunits of the NMDA receptor in cortical astrocytes
Conti, F., Debiasi, S., Minelli, A., & Melone, M. (1996) · Glia · doi:10.1002/(sici)1098-1136(199607)17:3 · Cited by 143
A P arkinson's disease gene, DJ ‐1, repairs brain injury through S ox9 stabilization and astrogliosis
Choi, D., Eun, J., Kim, B. G., Jou, I., Park, S. M., & Joe, E.-H. (2017) · Glia · doi:10.1002/glia.23258 · Cited by 41
Cholinergic and noncholinergic tegmental pedunculopontine projection neurons in rats revealed by intracellular labeling
Takakusaki, K., Shiroyama, T., Yamamoto, T., & Kitai, S. T. (1996) · The Journal of Comparative Neurology · doi:10.1002/(sici)1096-9861(19960729)371:3 · Cited by 150
Recent molecular approaches to understanding astrocyte function in vivo
Davila, D., Thibault, K., Fiacco, T. A., & Agulhon, C. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00272 · Cited by 42
Doxycycline-inducible and astrocyte-specific HIV-1 Tat transgenic mice (iTat) as an HIV/neuroAIDS model
Langford, D., Kim, B. O., Zou, W., Fan, Y., Rahimain, P., Liu, Y., & He, J. J. (2017) · Journal of NeuroVirology · doi:10.1007/s13365-017-0598-9 · Cited by 37
Radial Glial Cells: New Views on Old Questions
Arellano, J. I., Morozov, Y. M., Micali, N., & RAKIC, P. T. (2021) · Neurochemical Research · doi:10.1007/s11064-021-03296-z · Cited by 39
Selective Binding of Specific Mouse Genomic DNA Fragments by Mouse Vimentin Filaments In Vitro
WANG, X., Tolstonog, G. V., Shoeman, R. L., & Traub, P. (1996) · DNA and Cell Biology · doi:10.1089/dna.1996.15.209 · Cited by 37
AnIn VivoPharmacological Screen Identifies Cholinergic Signaling as a Therapeutic Target in Glial-Based Nervous System Disease
Wang, L., Hagemann, T. L., Messing, A., & Feany, M. Β. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0256-15.2016 · Cited by 36
The role of astrocytes in axonal regeneration in the mammalian CNS
y Ribotta, M. G., Menet, V., & Privat, A. (2001) · Progress in brain research · doi:10.1016/s0079-6123(01)32105-2 · Cited by 35
Increase of glial fibrillary acidic protein fragments in the spinal cord of motor neuron degeneration mutant mouse
Fujita, K., Yamauchi, M., Matsui, T., Titani, K., Takahashi, H., Kato, T., Isomura, G., Ando, M., & Nagata, Y. (1998) · Brain Research · doi:10.1016/s0006-8993(97)00612-4 · Cited by 34
Distribution of phosphorylated glial fibrillary acidic protein in the mouse central nervous system
Takemura, M., Nishiyama, H., & Itohara, S. (2002) · Genes to Cells · doi:10.1046/j.1365-2443.2002.00513.x · Cited by 34
Self-citation
Alternative mRNA Splicing from the Glial Fibrillary Acidic Protein (GFAP) Gene Generates Isoforms with Distinct Subcellular mRNA Localization Patterns in Astrocytes
Thomsen, R., Daugaard, T. F., Holm, I. E., & Nielsen, A. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072110 · Cited by 33
Chapter 14 Glial reactions in the central nervous system following heat stress
CervóAs-Navarro, J., SHARMA, H. S., Westman, J., & Bongcam‐Rudloff, E. (1998) · Progress in brain research · doi:10.1016/s0079-6123(08)62039-7 · Cited by 33
Dual involvement of G-substrate in motor learning revealed by gene deletion
Endo, S., Shutoh, F., Dinh, T. L., Okamoto, T., Ikeda, T., Suzuki, M., Kawahara, S., Yanagihara, D., Sato, Y., Yamada, K., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813341106 · Cited by 32
Self-citation
Characterization of the Human Analogue of a Scrapie-responsive Gene
Dron, M., Dandoy‐Dron, F., Guillo, F., Benboudjema, L., Hauw, J., Lebon, P., Dormont, D., & Tovey, M. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.29.18015 · Cited by 32
The role of gigaxonin in the degradation of the glial-specific intermediate filament protein GFAP
Lin, N., Huang, Y., Opal, P., Goldman, R. D., Messing, A., & Perng, M. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-06-0362 · Cited by 31
Elevated GFAP isoform expression promotes protein aggregation and compromises astrocyte function
Lin, N., Yang, A., Chang, C., & Perng, M. (2021) · The FASEB Journal · doi:10.1096/fj.202100087r · Cited by 29
RNAi‐mediated suppression of vimentin or glial fibrillary acidic protein prevents the establishment of Müller glial cell hypertrophy in progressive retinal degeneration
Hippert, C., Graca, A. B., Basche, M., Kalargyrou, A. A., Georgiadis, A., Ribeiro, J., Matsuyama, A., Aghaizu, N. D., Bainbridge, J. W., Smith, A. J., et al. (2021) · Glia · doi:10.1002/glia.24034 · Cited by 29
Increased adenine nucleotide translocator 1 in reactive astrocytes facilitates glutamate transport
Buck, C. R., Jurynec, M. J., Gupta, D. K., Law, A. K. T., Bilger, J., Wallace, D. C., & McKeon, R. J. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(03)00043-8 · Cited by 28
Novel insights into intermediate-filament function from studies of transgenic and knockout mice
Magin, T. M., Hesse, M., & Schröder, R. (2000) · PROTOPLASMA · doi:10.1007/bf01304482 · Cited by 28
Increases in Fragmented Glial Fibrillary Acidic Protein Levels in the Spinal Cords of Patients with Amyotrophic Lateral Sclerosis
Fujita, K., Kato, T., Yamauchi, M., Ando, M., Honda, M., & Nagata, Y. (1998) · Neurochemical Research · doi:10.1023/a:1022476724381 · Cited by 27
Involvement of p300 in constitutive and HIV‐1 Tat‐activated expression of glial fibrillary acidic protein in astrocytes
Zou, W., Wang, Z., Liu, Y., Fan, Y., Zhou, B. Y., Yang, X., & He, J. J. (2010) · Glia · doi:10.1002/glia.21038 · Cited by 26
Lack of CUL4B leads to increased abundance of GFAP-positive cells that is mediated by PTGDS in mouse brain
Zhao, W., Jiang, B., Hu, H., Zhang, S., Lv, S., Yuan, J., Qian, Y., Zou, Y., Li, X., Jiang, H., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv200 · Cited by 24
Mammalian prion proteins: enigma, variation and vaccination
Westaway, D. A., & Carlson, G. A. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02106-0 · Cited by 24
Loss of glial fibrillary acidic protein marginally accelerates disease progression in a SOD1 transgenic mouse model of ALS
Yoshii, Y., Otomo, A., Pan, L., Ohtsuka, M., & Hadano, S. (2011) · Neuroscience Research · doi:10.1016/j.neures.2011.03.006 · Cited by 23
The Exact Expression of Glial Fibrillary Acidic Protein (GFAP) in Trigeminal Ganglion and Dental Pulp.
Ajima, H., Kawano, Y., Takagi, R., Aita, M., Gomi, H., Byers, M. R., & Maeda, T. (2001) · Archivum histologicum japonicum · doi:10.1679/aohc.64.503 · Cited by 23
Self-citation
The transformation suppressor gene Reck is required for postaxial patterning in mouse forelimbs
Yamamoto, M., Matsuzaki, T., Takahashi, R., Adachi, E., Maeda, Y., Yamaguchi, S., Kitayama, H., Echizenya, M., Morioka, Y., Alexander, D. B., et al. (2012) · Biology Open · doi:10.1242/bio.2012638 · Cited by 23
Self-citation
Genetic knockouts in mice: An update
Shastry, B. S. (1995) · Cellular and Molecular Life Sciences · doi:10.1007/bf01946911 · Cited by 23
Postnatal expression of Cdkl2 in mouse brain revealed by LacZ inserted into the Cdkl2 locus
Sassa, T., Gomi, H., & Itohara, S. (2004) · Cell and Tissue Research · doi:10.1007/s00441-003-0828-8 · Cited by 22
Self-citation
Acute effects of systemic inflammation upon the neuro-glial-vascular unit and cerebrovascular function
Brezzo, G., Simpson, J. E., Ameen‐Ali, K. E., Berwick, J., & Martin, C. J. (2020) · Brain Behavior & Immunity - Health · doi:10.1016/j.bbih.2020.100074 · Cited by 26
Glial fibrillary acidic protein: The component of iintermediate filaments in the vertebrate brain astrocytes
Sukhorukova, E. G., Korzhevsky, D. E., & Alekseeva, O. S. (2015) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s0022093015010019 · Cited by 23
Extracellular adenosine triphosphate induces glutamate transporter‐1 expression in hippocampus
Frizzo, M. E., Frizzo, J. K., Amadio, S., Rodrigues, J. M., Perry, M. L. S., Bernardi, G., & Volonté, C. (2007) · Hippocampus · doi:10.1002/hipo.20269 · Cited by 22
Lessons from Animal Models of Cytoplasmic Intermediate Filament Proteins
Bouameur, J.-E., & Magin, T. M. (2017) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-49674-0_7 · Cited by 21
14 Intermediate Filament Organization, Reorganization, and Function in the Clawed Frog Xenopus
Klymkowsky, M. W. (1996) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(08)60236-7 · Cited by 21
Characterization of glial filament-cytoskeletal interactions in human astrocytomas: An immuno-ultrastructural analysis
Rutka, J. T., Ackerley, C. A., Hubbard, S. L., Tilup, A., Dirks, P. B., Jung, S., Ivanchuk, S. M., Kurimoto, M., Tsugu, A., & Becker, L. E. (1998) · European Journal of Cell Biology · doi:10.1016/s0171-9335(98)80006-x · Cited by 21
Role of GFAP in morphological retention and distribution of reactive astrocytes induced by scrapie encephalopathy in mice
Gomi, H., Yokoyama, T., & Itohara, S. (2009) · Brain Research · doi:10.1016/j.brainres.2009.11.025 · Cited by 19
Self-citation
Retinal G-substrate, potential downstream component of NO/cGMP/PKG pathway, is located in subtype of retinal ganglion cells and amacrine cells with protein phosphatases
Nakazawa, T., Endo, S., Shimura, M., Kondo, M., Ueno, S., & Tamai, M. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.12.006 · Cited by 19
Analysis of Protein Expression Profile in the Cerebellum of Cerebral Infarction Rats After Treadmill Training
Mizutani, K., Sonoda, S., Hayashi, N., Takasaki, A., Beppu, H., Saitoh, E., & Shimpo, K. (2010) · American Journal of Physical Medicine & Rehabilitation · doi:10.1097/phm.0b013e3181b3323b · Cited by 19
Glial fibrillary acidic protein is pathologically modified in Alexander disease
Lin, N., Jian, W.-S., Snider, N. T., & Perng, M. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107402 · Cited by 18
Astrocyte in prion disease: a double-edged sword
Schätzl, H. M., Tahir, W., & Thapa, S. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.332202 · Cited by 20
Persistent retroviral infection with MoMuLV influences neuropathological signature and phenotype of prion disease
Krasemann, S., Neumann, M., Luepke, J.-P., Grashorn, J., Wurr, S., Stocking, C., & Glatzel, M. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0944-1 · Cited by 18
Glial reaction and reactive glia
Kálmán, M. (2003) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(03)31035-5 · Cited by 17
Mammalian-Specific Central Myelin Protein Opalin Is Redundant for Normal Myelination: Structural and Behavioral Assessments
Yoshikawa, F., Sato, Y., Tohyama, K., Akagi, T., Furuse, T., Sadakata, T., Tanaka, M., Shinoda, Y., Hashikawa, T., Itohara, S., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0166732 · Cited by 16
Self-citation
A new monoclonal antibody, A3B10, specific for astrocyte‐lineage cells recognizes calmodulin‐regulated spectrin‐associated protein 1 (Camsap1)
Yamamoto, M., Yoshimura, K., Kitada, M., Nakahara, J., Seiwa, C., Ueki, T., Shimoda, Y., Ishige, A., Watanabe, K., & Asou, H. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21853 · Cited by 17
Role of radial fibers in controlling the onset of myelination
Nakahara, J., Takemura, M., Gomi, H., Tsunematsu, K., Itohara, S., Asou, H., Ogawa, M., Aiso, S., & Tan‐Takeuchi, K. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10593 · Cited by 17
Self-citation
GFAP immunoreactivity and transcription in trigeminal and dental tissues of rats and transgenic GFP/GFAP mice
Byers, M. R., Maeda, T., Brown, A. M., & Westenbroek, R. E. (2004) · Microscopy Research and Technique · doi:10.1002/jemt.20130 · Cited by 16
The astrocyte response to neural injury: a review and reconsideration of key features
O’Callaghan, A. R. L. A. J. P. (2002) · CRC Press eBooks · doi:10.1201/9780203219096-23 · Cited by 15
Transgenesis Applied to Transmissible Spongiform Encephalopathies
Vilotte, J.-L., & Laude, H. (2002) · Transgenic Research · doi:10.1023/a:1021125510220 · Cited by 14
A role of glial fibrillary acidic protein in hippocampal degeneration after cerebral trauma or kainate-induced seizure
Otani, N., Nawashiro, H., Nomura, N., Fukui, S., Tsuzuki, N., Ishihara, S., & Shima, K. (2003) · Springer eBooks · doi:10.1007/978-3-7091-0651-8_58 · Cited by 13
Differences in the activation of the GFAP gene promoter by prion and viral infections
Titeux, M., Galou, M., Gomes, F. C. A., Dormont, D., Moura‐Neto, V., & Paulin, D. (2002) · Molecular Brain Research · doi:10.1016/s0169-328x(02)00547-8 · Cited by 13
Detection of species specific epitopes of mouse and hamster prion proteins (PrPs) by anti-peptide antibodies
Yokoyama, T., Itohara, S., & Yuasa, N. (1996) · Archives of Virology · doi:10.1007/bf01718334 · Cited by 13
Self-citation
Loss of Homeostatic Microglia Signature in Prion Diseases
Wang, Y., Hartmann, K., Thies, E., Mohammadi, B., Altmeppen, H., Sepulveda-Falla, D., Glatzel, M., & Krasemann, S. (2022) · Cells · doi:10.3390/cells11192948 · Cited by 12
Redistribution of GFAP and αB-crystallin after thermal stress in C6 glioma cell line
Tseng, W.-C., Lu, K., Lee, W.-C., & Chien, C. L. (2006) · Journal of Biomedical Science · doi:10.1007/s11373-006-9091-9 · Cited by 12
Reactive astrocytes, their roles in CNS injury, and repair mechanisms
Ridet, J., & Privat, A. (2000) · Advances in structural biology · doi:10.1016/s1064-6000(00)80008-3 · Cited by 11
Glial-Defined Boundaries in Xenopus CNS
Yoshida, M. (2001) · Developmental Neuroscience · doi:10.1159/000048713 · Cited by 11
Structural and biological consequences of increased vimentin expression in simple epithelial cell types
Andreoli, J. M., & Trevor, K. T. (1995) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970320103 · Cited by 11
GFAP and Astrocyte Intermediate Filaments
Pekny, M., & Wilhelmsson, U. (2006) · Springer eBooks · doi:10.1007/0-387-30395-2_14 · Cited by 10
Nestin in the Liver—Lessons From the Brain
Messing, A. (1999) · Hepatology · doi:10.1002/hep.510290234 · Cited by 10
Stress Models for the Study of Intermediate Filament Function
Lane, E. B., & Pekny, M. (2004) · Methods in cell biology · doi:10.1016/s0091-679x(04)78009-7 · Cited by 10
Intermediate filaments as dynamic structures
Klymkowsky, M. W. (1996) · Cancer and Metastasis Reviews · doi:10.1007/bf00054010 · Cited by 9

Authors: Gomi, H., Yokoyama, T., Fujimoto, K., Ikeda, T., Katoh, A., Itoh, T., & Itohara, S.
Affiliations: Kyoto University (JP)
National Institute of Animal Health (JP)
ORCID: Yokoyama, Takashi
Fujimoto, Kazushi
Itohara, Shigeyoshi
Venue: Neuron
Publisher: Elsevier BV
Published: 1995-01
Volume: 14
Issue: 1
Pages: 29-41
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/0896-6273(95)90238-4
OpenAlex: W2059028264
Cited by: 256
References: 67
Citations by year: 2026: 1 · 2025: 2 · 2024: 3 · 2023: 1 · 2022: 4 · 2021: 6 · 2020: 5 · 2019: 1 · 2017: 8 · 2016: 4 · 2015: 6 · 2014: 4 · 2013: 6 · 2012: 6
FWCI: 7.99
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 6772 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Funders: Japan Science and Technology Agency
Ministry of Education, Culture, Sports, Science and Technology
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
Keywords: glial fibrillary acidic protein, prion disease, astrocytes, intermediate filaments, gene targeting, central nervous system development, prion accumulation, neuropathology, prion pathogenesis
MeSH terms: Animals, Astrocytes, beta-Galactosidase, Brain, Brain Chemistry, Female, Glial Fibrillary Acidic Protein, Male, Mice, Inbred C57BL, Mice, Mutant Strains, Prions, RNA, Messenger, Scrapie, Spinal Cord, Vimentin, Mutagenesis, Gene Targeting, Mice

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Mice devoid of the glial fibrillary acidic protein develop normally and are susceptible to scrapie prions

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks