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Article ; Online: Sigma-2 Receptors-From Basic Biology to Therapeutic Target: A Focus on Age-Related Degenerative Diseases.

Lizama, Britney N / Kahle, Jennifer / Catalano, Susan M / Caggiano, Anthony O / Grundman, Michael / Hamby, Mary E

International journal of molecular sciences

2023 Volume 24, Issue 7

Abstract: There is a large unmet medical need to develop disease-modifying treatment options for individuals with age-related degenerative diseases of the central nervous system. The sigma-2 receptor (S2R), encoded ... ...

Abstract	There is a large unmet medical need to develop disease-modifying treatment options for individuals with age-related degenerative diseases of the central nervous system. The sigma-2 receptor (S2R), encoded by
MeSH term(s)	Animals ; Alzheimer Disease/drug therapy ; Receptors, sigma/metabolism ; alpha-Synuclein/metabolism ; Amyloid beta-Peptides ; Biology ; Lewy Body Disease
Chemical Substances	sigma-2 receptor ; Receptors, sigma ; alpha-Synuclein ; Amyloid beta-Peptides
Language	English
Publishing date	2023-03-26
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms24076251
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Article ; Online: A pilot study to evaluate the effect of CT1812 treatment on synaptic density and other biomarkers in Alzheimer's disease.

van Dyck, Christopher H / Mecca, Adam P / O'Dell, Ryan S / Bartlett, Hugh H / Diepenbrock, Nina G / Huang, Yiyun / Hamby, Mary E / Grundman, Michael / Catalano, Susan M / Caggiano, Anthony O / Carson, Richard E

Alzheimer's research & therapy

2024 Volume 16, Issue 1, Page(s) 20

Abstract: Background: Effective, disease-modifying therapeutics for the treatment of Alzheimer's disease (AD) remain a large unmet need. Extensive evidence suggests that amyloid beta (Aβ) is central to AD pathophysiology, and Aβ oligomers are among the most toxic ...

Abstract	Background: Effective, disease-modifying therapeutics for the treatment of Alzheimer's disease (AD) remain a large unmet need. Extensive evidence suggests that amyloid beta (Aβ) is central to AD pathophysiology, and Aβ oligomers are among the most toxic forms of Aβ. CT1812 is a novel brain penetrant sigma-2 receptor ligand that interferes with the binding of Aβ oligomers to neurons. Preclinical studies of CT1812 have demonstrated its ability to displace Aβ oligomers from neurons, restore synapses in cell cultures, and improve cognitive measures in mouse models of AD. CT1812 was found to be generally safe and well tolerated in a placebo-controlled phase 1 clinical trial in healthy volunteers and phase 1a/2 clinical trials in patients with mild to moderate dementia due to AD. The unique objective of this study was to incorporate synaptic positron emission tomography (PET) imaging as an outcome measure for CT1812 in AD patients. Methods: The present phase 1/2 study was a randomized, double-blind, placebo-controlled, parallel-group trial conducted in 23 participants with mild to moderate dementia due to AD to primarily evaluate the safety of CT1812 and secondarily its pharmacodynamic effects. Participants received either placebo or 100 mg or 300 mg per day of oral CT1812 for 24 weeks. Pharmacodynamic effects were assessed using the exploratory efficacy endpoints synaptic vesicle glycoprotein 2A (SV2A) PET, fluorodeoxyglucose (FDG) PET, volumetric MRI, cognitive clinical measures, as well as cerebrospinal fluid (CSF) biomarkers of AD pathology and synaptic degeneration. Results: No treatment differences relative to placebo were observed in the change from baseline at 24 weeks in either SV2A or FDG PET signal, the cognitive clinical rating scales, or in CSF biomarkers. Composite region volumetric MRI revealed a trend towards tissue preservation in participants treated with either dose of CT1812, and nominally significant differences with both doses of CT1812 compared to placebo were found in the pericentral, prefrontal, and hippocampal cortices. CT1812 was safe and well tolerated. Conclusions: The safety findings of this 24-week study and the observed changes on volumetric MRI with CT1812 support its further clinical development. Trial registration: The clinical trial described in this manuscript is registered at clinicaltrials.gov (NCT03493282).
MeSH term(s)	Mice ; Animals ; Humans ; Alzheimer Disease/diagnostic imaging ; Alzheimer Disease/drug therapy ; Alzheimer Disease/metabolism ; Amyloid beta-Peptides/cerebrospinal fluid ; Pilot Projects ; Fluorodeoxyglucose F18 ; Positron-Emission Tomography ; Biomarkers/cerebrospinal fluid
Chemical Substances	Amyloid beta-Peptides ; Fluorodeoxyglucose F18 (0Z5B2CJX4D) ; Biomarkers
Language	English
Publishing date	2024-01-25
Publishing country	England
Document type	Randomized Controlled Trial ; Clinical Trial, Phase I ; Clinical Trial, Phase II ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2506521-X
ISSN	1758-9193 ; 1758-9193
ISSN (online)	1758-9193
ISSN	1758-9193
DOI	10.1186/s13195-024-01382-2
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Article ; Online: Sigma-2 Receptors—From Basic Biology to Therapeutic Target

Britney N. Lizama / Jennifer Kahle / Susan M. Catalano / Anthony O. Caggiano / Michael Grundman / Mary E. Hamby

International Journal of Molecular Sciences, Vol 24, Iss 6251, p

A Focus on Age-Related Degenerative Diseases

2023 Volume 6251

Abstract	There is a large unmet medical need to develop disease-modifying treatment options for individuals with age-related degenerative diseases of the central nervous system. The sigma-2 receptor (S2R), encoded by TMEM97 , is expressed in brain and retinal cells, and regulates cell functions via its co-receptor progesterone receptor membrane component 1 (PGRMC1), and through other protein–protein interactions. Studies describing functions of S2R involve the manipulation of expression or pharmacological modulation using exogenous small-molecule ligands. These studies demonstrate that S2R modulates key pathways involved in age-related diseases including autophagy, trafficking, oxidative stress, and amyloid-β and α-synuclein toxicity. Furthermore, S2R modulation can ameliorate functional deficits in cell-based and animal models of disease. This review summarizes the current evidence-based understanding of S2R biology and function, and its potential as a therapeutic target for age-related degenerative diseases of the central nervous system, including Alzheimer’s disease, α-synucleinopathies, and dry age-related macular degeneration.
Keywords	S2R ; TMEM97 ; PGRMC1 ; MAC30 ; σ2R ; Alzheimer’s disease (AD) ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	610
Language	English
Publishing date	2023-03-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article: The Role of APOE4 in Disrupting the Homeostatic Functions of Astrocytes and Microglia in Aging and Alzheimer's Disease.

Fernandez, Celia G / Hamby, Mary E / McReynolds, Morgan L / Ray, William J

Frontiers in aging neuroscience

2019 Volume 11, Page(s) 14

Abstract: APOE4 is the greatest genetic risk factor for late-onset Alzheimer's disease (AD), increasing the risk of developing the disease by 3-fold in the 14% of the population that are carriers. Despite 25 years of research, the exact mechanisms underlying how ... ...

Abstract	APOE4 is the greatest genetic risk factor for late-onset Alzheimer's disease (AD), increasing the risk of developing the disease by 3-fold in the 14% of the population that are carriers. Despite 25 years of research, the exact mechanisms underlying how APOE4 contributes to AD pathogenesis remain incompletely defined. APOE in the brain is primarily expressed by astrocytes and microglia, cell types that are now widely appreciated to play key roles in the pathogenesis of AD; thus, a picture is emerging wherein APOE4 disrupts normal glial cell biology, intersecting with changes that occur during normal aging to ultimately cause neurodegeneration and cognitive dysfunction. This review article will summarize how APOE4 alters specific pathways in astrocytes and microglia in the context of AD and the aging brain. APOE itself, as a secreted lipoprotein without enzymatic activity, may prove challenging to directly target therapeutically in the classical sense. Therefore, a deeper understanding of the underlying pathways responsible for APOE4 toxicity is needed so that more tractable pathways and drug targets can be identified to reduce APOE4-mediated disease risk.
Language	English
Publishing date	2019-02-11
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2558898-9
ISSN	1663-4365
ISSN	1663-4365
DOI	10.3389/fnagi.2019.00014
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Article: A phase 1b randomized clinical trial of CT1812 to measure Aβ oligomer displacement in Alzheimer's disease using an indwelling CSF catheter.

Translational neurodegeneration

2023 Volume 12, Issue 1, Page(s) 24

MeSH term(s)	Humans ; Alzheimer Disease/diagnostic imaging ; Alzheimer Disease/therapy ; Amyloid beta-Peptides ; Catheters
Chemical Substances	Amyloid beta-Peptides
Language	English
Publishing date	2023-05-12
Publishing country	England
Document type	Randomized Controlled Trial ; Clinical Trial, Phase I ; Letter ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2653701-1
ISSN	2047-9158
ISSN	2047-9158
DOI	10.1186/s40035-023-00358-w
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Article ; Online: Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer's disease.

Colom-Cadena, Martí / Toombs, Jamie / Simzer, Elizabeth / Holt, Kristjan / McGeachan, Robert / Tulloch, Jane / Jackson, Rosemary J / Catterson, James H / Spires-Jones, Maxwell P / Rose, Jamie / Waybright, Lora / Caggiano, Anthony O / King, Declan / Gobbo, Francesco / Davies, Caitlin / Hooley, Monique / Dunnett, Sophie / Tempelaar, Robert / Meftah, Soraya /

Tzioras, Makis / Hamby, Mary E / Izzo, Nicholas J / Catalano, Susan M / Durrant, Claire S / Smith, Colin / Dando, Owen / Spires-Jones, Tara L

Acta neuropathologica

2024 Volume 147, Issue 1, Page(s) 32

Abstract: Synapse loss correlates with cognitive decline in Alzheimer's disease, and soluble oligomeric amyloid beta (Aβ) is implicated in synaptic dysfunction and loss. An important knowledge gap is the lack of understanding of how Aβ leads to synapse ... ...

Abstract	Synapse loss correlates with cognitive decline in Alzheimer's disease, and soluble oligomeric amyloid beta (Aβ) is implicated in synaptic dysfunction and loss. An important knowledge gap is the lack of understanding of how Aβ leads to synapse degeneration. In particular, there has been difficulty in determining whether there is a synaptic receptor that binds Aβ and mediates toxicity. While many candidates have been observed in model systems, their relevance to human AD brain remains unknown. This is in part due to methodological limitations preventing visualization of Aβ binding at individual synapses. To overcome this limitation, we combined two high resolution microscopy techniques: array tomography and Förster resonance energy transfer (FRET) to image over 1 million individual synaptic terminals in temporal cortex from AD (n = 11) and control cases (n = 9). Within presynapses and post-synaptic densities, oligomeric Aβ generates a FRET signal with transmembrane protein 97. Further, Aβ generates a FRET signal with cellular prion protein, and post-synaptic density 95 within post synapses. Transmembrane protein 97 is also present in a higher proportion of post synapses in Alzheimer's brain compared to controls. We inhibited Aβ/transmembrane protein 97 interaction in a mouse model of amyloidopathy by treating with the allosteric modulator CT1812. CT1812 drug concentration correlated negatively with synaptic FRET signal between transmembrane protein 97 and Aβ. In human-induced pluripotent stem cell derived neurons, transmembrane protein 97 is present in synapses and colocalizes with Aβ when neurons are challenged with human Alzheimer's brain homogenate. Transcriptional changes are induced by Aβ including changes in genes involved in neurodegeneration and neuroinflammation. CT1812 treatment of these neurons caused changes in gene sets involved in synaptic function. These data support a role for transmembrane protein 97 in the synaptic binding of Aβ in human Alzheimer's disease brain where it may mediate synaptotoxicity.
MeSH term(s)	Animals ; Humans ; Mice ; Alzheimer Disease ; Amyloid beta-Peptides ; Brain ; Cognitive Dysfunction ; Synapses ; Membrane Proteins/metabolism
Chemical Substances	Amyloid beta-Peptides ; TMEM97 protein, human ; Membrane Proteins
Language	English
Publishing date	2024-02-06
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1079-0
ISSN	1432-0533 ; 0001-6322
ISSN (online)	1432-0533
ISSN	0001-6322
DOI	10.1007/s00401-023-02679-6
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Article ; Online: Reactive astrocytes as therapeutic targets for CNS disorders.

Hamby, Mary E / Sofroniew, Michael V

Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics

2010 Volume 7, Issue 4, Page(s) 494–506

Abstract: Reactive astrogliosis has long been recognized as a ubiquitous feature of CNS pathologies. Although its roles in CNS pathology are only beginning to be defined, genetic tools are enabling molecular dissection of the functions and mechanisms of reactive ... ...

Abstract	Reactive astrogliosis has long been recognized as a ubiquitous feature of CNS pathologies. Although its roles in CNS pathology are only beginning to be defined, genetic tools are enabling molecular dissection of the functions and mechanisms of reactive astrogliosis in vivo. It is now clear that reactive astrogliosis is not simply an all-or-nothing phenomenon but, rather, is a finely gradated continuum of molecular, cellular, and functional changes that range from subtle alterations in gene expression to scar formation. These changes can exert both beneficial and detrimental effects in a context-dependent manner determined by specific molecular signaling cascades. Dysfunction of either astrocytes or the process of reactive astrogliosis is emerging as an important potential source of mechanisms that might contribute to, or play primary roles in, a host of CNS disorders via loss of normal or gain of abnormal astrocyte activities. A rapidly growing understanding of the mechanisms underlying astrocyte signaling and reactive astrogliosis has the potential to open doors to identifying many molecules that might serve as novel therapeutic targets for a wide range of neurological disorders. This review considers general principles and examines selected examples regarding the potential of targeting specific molecular aspects of reactive astrogliosis for therapeutic manipulations, including regulation of glutamate, reactive oxygen species, and cytokines.
MeSH term(s)	Animals ; Astrocytes/pathology ; Astrocytes/physiology ; Central Nervous System Diseases/pathology ; Central Nervous System Diseases/therapy ; Cytokines/metabolism ; Enzyme Inhibitors/pharmacology ; Enzyme Inhibitors/therapeutic use ; Free Radical Scavengers/metabolism ; Free Radical Scavengers/therapeutic use ; Gene Expression Regulation/drug effects ; Glutamic Acid/metabolism ; Humans ; Reactive Oxygen Species/metabolism ; Signal Transduction/drug effects ; Signal Transduction/physiology
Chemical Substances	Cytokines ; Enzyme Inhibitors ; Free Radical Scavengers ; Reactive Oxygen Species ; Glutamic Acid (3KX376GY7L)
Language	English
Publishing date	2010-10-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2316693-9
ISSN	1878-7479 ; 1933-7213
ISSN (online)	1878-7479
ISSN	1933-7213
DOI	10.1016/j.nurt.2010.07.003
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Article ; Online: Dual Leucine Zipper Kinase Is Constitutively Active in the Adult Mouse Brain and Has Both Stress-Induced and Homeostatic Functions.

Goodwani, Sunil / Fernandez, Celia / Acton, Paul J / Buggia-Prevot, Virginie / McReynolds, Morgan L / Ma, Jiacheng / Hu, Cheng Hui / Hamby, Mary E / Jiang, Yongying / Le, Kang / Soth, Michael J / Jones, Philip / Ray, William J

International journal of molecular sciences

2020 Volume 21, Issue 14

Abstract: Dual leucine zipper kinase (DLK, Map3k12) is an axonal protein that governs the balance between degeneration and regeneration through its downstream effectors c-jun N-terminal kinase (JNK) and phosphorylated c-jun (p-c-Jun). In peripheral nerves DLK is ... ...

Abstract	Dual leucine zipper kinase (DLK, Map3k12) is an axonal protein that governs the balance between degeneration and regeneration through its downstream effectors c-jun N-terminal kinase (JNK) and phosphorylated c-jun (p-c-Jun). In peripheral nerves DLK is generally inactive until induced by injury, after which it transmits signals to the nucleus via retrograde transport. Here we report that in contrast to this mode of regulation, in the uninjured adult mouse cerebellum, DLK constitutively drives nuclear p-c-Jun in cerebellar granule neurons, whereas in the forebrain, DLK is similarly expressed and active, but nuclear p-c-Jun is undetectable. When neurodegeneration results from mutant human tau in the rTg4510 mouse model, p-c-Jun then accumulates in neuronal nuclei in a DLK-dependent manner, and the extent of p-c-Jun correlates with markers of synaptic loss and gliosis. This regional difference in DLK-dependent nuclear p-c-Jun accumulation could relate to differing levels of JNK scaffolding proteins, as the cerebellum preferentially expresses JNK-interacting protein-1 (JIP-1), whereas the forebrain contains more JIP-3 and plenty of SH3 (POSH). To characterize the functional differences between constitutive- versus injury-induced DLK signaling, RNA sequencing was performed after DLK inhibition in the cerebellum and in the non-transgenic and rTg4510 forebrain. In all contexts, DLK inhibition reduced a core set of transcripts that are associated with the JNK pathway. Non-transgenic forebrain showed almost no other transcriptional changes in response to DLK inhibition, whereas the rTg4510 forebrain and the cerebellum exhibited distinct differentially expressed gene signatures. In the cerebellum, but not the rTg4510 forebrain, pathway analysis indicated that DLK regulates insulin growth factor-1 (IGF1) signaling through the transcriptional induction of IGF1 binding protein-5 (IGFBP5), which was confirmed and found to be functionally relevant by measuring signaling through the IGF1 receptor. Together these data illuminate the complex multi-functional nature of DLK signaling in the central nervous system (CNS) and demonstrate its role in homeostasis as well as tau-mediated neurodegeneration.
MeSH term(s)	Animals ; Axons/metabolism ; Brain/metabolism ; Brain/physiology ; Homeostasis/physiology ; JNK Mitogen-Activated Protein Kinases/metabolism ; MAP Kinase Kinase Kinases/metabolism ; MAP Kinase Signaling System/physiology ; Male ; Mice ; Mice, Inbred C57BL ; Neurons/metabolism ; Neurons/physiology ; Signal Transduction/physiology ; Stress, Physiological/physiology ; Transcriptome/physiology
Chemical Substances	JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; MAP Kinase Kinase Kinases (EC 2.7.11.25) ; mitogen-activated protein kinase kinase kinase 12 (EC 2.7.11.25)
Language	English
Publishing date	2020-07-09
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms21144849
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Article ; Online: Smad3-dependent signaling underlies the TGF-β1-mediated enhancement in astrocytic iNOS expression.

Hamby, Mary E / Hewett, James A / Hewett, Sandra J

Glia

2010 Volume 58, Issue 11, Page(s) 1282–1291

Abstract: We previously demonstrated that transforming growth factor-beta1 (TGF-beta1), while having no effect alone, enhances nitric oxide (NO) production in primary, purified mouse astrocytes induced by lipopolysaccharide (LPS) plus interferon-gamma (IFN-gamma), ...

Abstract	We previously demonstrated that transforming growth factor-beta1 (TGF-beta1), while having no effect alone, enhances nitric oxide (NO) production in primary, purified mouse astrocytes induced by lipopolysaccharide (LPS) plus interferon-gamma (IFN-gamma), by recruiting a latent population of astrocytes to respond, thereby enhancing the total number of cells that express Nos2. In this investigation, we evaluated the molecular signaling pathway by which this occurs. We found that purified murine primary astrocytes express mRNA for TGFbetaRII as well as the TGFbetaRI subunit activin-like kinase 5 (ALK5), but not ALK1. Immunofluorescence microscopy confirmed the expression of TGFbetaRII and ALK5 protein in astrocytes. Consistent with ALK5 signaling, Smad3 accumulated in the nucleus of astrocytes as early as 30 min after TGF-beta1 (3 ng/mL) treatment and persisted upto 32 hr after TGF-beta1 administration. Addition of ALK5 inhibitors prevented TGF-beta1-mediated Smad3 nuclear accumulation and NO production when given prior to the Nos2 induction stimuli, but not after. Finally, astrocyte cultures derived from Smad3 null mutant mice did not exhibit a TGF-beta1-mediated increase in iNOS expression. Overall, this data suggests that ALK5 signaling and Smad3 nuclear accumulation is required for optimal enhancement of LPS plus IFNgamma-induced NO production in astrocytes by TGF-beta1.
MeSH term(s)	Active Transport, Cell Nucleus/genetics ; Active Transport, Cell Nucleus/physiology ; Animals ; Astrocytes/enzymology ; Astrocytes/metabolism ; Astrocytes/pathology ; Cell Differentiation/genetics ; Cell Differentiation/physiology ; Cell Nucleus/enzymology ; Cell Nucleus/genetics ; Cell Nucleus/metabolism ; Cells, Cultured ; Female ; Gene Expression Regulation, Enzymologic/physiology ; Lipopolysaccharides/pharmacology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Nitric Oxide/biosynthesis ; Nitric Oxide/genetics ; Nitric Oxide Synthase Type II/biosynthesis ; Nitric Oxide Synthase Type II/genetics ; Protein-Serine-Threonine Kinases/physiology ; Receptor, Transforming Growth Factor-beta Type I ; Receptors, Transforming Growth Factor beta/physiology ; Recombinant Proteins/pharmacology ; Signal Transduction/genetics ; Signal Transduction/physiology ; Smad3 Protein/metabolism ; Smad3 Protein/physiology ; Transforming Growth Factor beta1/physiology ; Up-Regulation/genetics ; Up-Regulation/physiology
Chemical Substances	Lipopolysaccharides ; Receptors, Transforming Growth Factor beta ; Recombinant Proteins ; Smad3 Protein ; Smad3 protein, mouse ; Tgfb1 protein, mouse ; Transforming Growth Factor beta1 ; Nitric Oxide (31C4KY9ESH) ; Nitric Oxide Synthase Type II (EC 1.14.13.39) ; Nos2 protein, mouse (EC 1.14.13.39) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Receptor, Transforming Growth Factor-beta Type I (EC 2.7.11.30) ; Tgfbr1 protein, mouse (EC 2.7.11.30)
Language	English
Publishing date	2010-07-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	639414-0
ISSN	1098-1136 ; 0894-1491
ISSN (online)	1098-1136
ISSN	0894-1491
DOI	10.1002/glia.21005
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Article: Transcriptional regulation of neuronal differentiation: the epigenetic layer of complexity.

Hamby, Mary E / Coskun, Volkan / Sun, Yi E

Biochimica et biophysica acta

2008 Volume 1779, Issue 8, Page(s) 432–437

Abstract: The transcriptional programs of neural progenitor cells change dynamically during neurogenesis, a process regulated by both intrinsic and extrinsic factors. Although many of the transcription factors required for neuronal differentiation have long been ... ...

Abstract	The transcriptional programs of neural progenitor cells change dynamically during neurogenesis, a process regulated by both intrinsic and extrinsic factors. Although many of the transcription factors required for neuronal differentiation have long been identified, we are only at the brink of understanding how epigenetic mechanisms influence transcriptional activity and the accessibility of transcription factors to bind consensus cis-elements. Herein, we delineate the chief epigenetic modifications and the machinery responsible for these alterations. Further, we review the epigenetic modifications presently known to participate in the maintenance of the neural progenitor cell state and in the regulation of neuronal differentiation.
MeSH term(s)	Animals ; Brain/cytology ; Brain/metabolism ; Cell Differentiation/physiology ; Epigenesis, Genetic ; Humans ; Neuronal Plasticity/physiology ; Neurons/cytology ; Neurons/physiology ; Stem Cells/cytology ; Stem Cells/physiology ; Transcription Factors/genetics ; Transcription Factors/physiology ; Transcription, Genetic/genetics ; Transcription, Genetic/physiology
Chemical Substances	Transcription Factors
Language	English
Publishing date	2008-07-28
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagrm.2008.07.006
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