RAT:TAU

Species (Taxon ID)	Rattus norvegicus (Rat). (10116)
Gene Name(s)	Mapt (synonyms: Mtapt, Tau)
Protein Name(s)	Microtubule-associated protein tau Neurofibrillary tangle protein Paired helical filament-tau PHF-tau
External Links
UniProt	P19332
EMBL	M84156 X79321 D30628 D30629
PIR	A38235 JS0306 S46264
UniGene	Rn.2455
DIP	DIP-41779N
IntAct	P19332
MINT	MINT-1037362
BindingDB	P19332
ChEMBL	CHEMBL1075117
PhosphoSite	P19332
PaxDb	P19332
PRIDE	P19332
UCSC	RGD:69329
RGD	69329
eggNOG	NOG148882
HOGENOM	HOG000231029
HOVERGEN	HBG000991
InParanoid	P19332
PhylomeDB	P19332
PRO	PR:P19332
Proteomes	UP000002494
Genevestigator	P19332
GO	GO:0030424 GO:0044295 GO:0005829 GO:0030426 GO:0005874 GO:0043005 GO:0005886 GO:0045298 GO:0019899 GO:0008017 GO:0032403 GO:0019904 GO:0019901 GO:0051721 GO:0006915 GO:0007420 GO:0007565 GO:0008631 GO:0000226 GO:0007017 GO:0030182 GO:0045773 GO:0031116 GO:0007584 GO:0010033
InterPro	IPR027324 IPR001084 IPR002955
PANTHER	PTHR11501
Pfam	PF00418
PRINTS	PR01261
PROSITE	PS00229 PS51491

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0005874	microtubule	PMID:1396588^[1]	ECO:0000314			C		Figure 3 shows that Tau was localized to microtubules using an anti-Tau and an anti-tubulin antibody.	complete CACAO 9307
enables	GO:0051879	Hsp90 protein binding	PMID:19363271^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07900	F	occurs_in:(UBERON:0000955)	Seeded From UniProt	complete
part_of	GO:0044304	main axon	PMID:2509111^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:1001611) exists_during:(GO:0048666)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:2509111^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:1001611) exists_during:(GO:0048666)	Seeded From UniProt	complete
part_of	GO:0030425	dendrite	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P10636	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P10636	C		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:19228967^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P14659	F	occurs_in:(CL:0002608)\|occurs_in:(CL:0002609)	Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:19228967^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q91YN9	F	occurs_in:(CL:0002608)\|occurs_in:(CL:0002609)	Seeded From UniProt	complete
part_of	GO:0030424	axon	PMID:28521134^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
colocalizes_with	GO:0005874	microtubule	PMID:17491008^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000955)	Seeded From UniProt	complete
part_of	GO:0009898	cytoplasmic side of plasma membrane	PMID:10747907^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
part_of	GO:0005874	microtubule	PMID:1396588^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0010288	response to lead ion	PMID:22387731^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(UBERON:0001885) causally_upstream_of:(GO:0007416) causally_upstream_of:(GO:0007611)	Seeded From UniProt	complete
involved_in	GO:0045773	positive regulation of axon extension	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P10636	P		Seeded From UniProt	complete
part_of	GO:0045298	tubulin complex	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P10636	C		Seeded From UniProt	complete
part_of	GO:0044295	axonal growth cone	PMID:20133804^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0031116	positive regulation of microtubule polymerization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P10636	P		Seeded From UniProt	complete
part_of	GO:0030426	growth cone	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P10636	C		Seeded From UniProt	complete
part_of	GO:0030424	axon	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P10636	C		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:20133804^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9QVC8	F		Seeded From UniProt	complete
enables	GO:0008017	microtubule binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P10636	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P10636	C		Seeded From UniProt	complete
involved_in	GO:0000226	microtubule cytoskeleton organization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P10636	P		Seeded From UniProt	complete
involved_in	GO:1900454	positive regulation of long-term synaptic depression	PMID:24298146^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051879	Hsp90 protein binding	PMID:19363271^[2]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:631409	F		Seeded From UniProt	complete
enables	GO:0051721	protein phosphatase 2A binding	PMID:11032905^[11]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:3380 RGD:620919	F		Seeded From UniProt	complete
involved_in	GO:0051028	mRNA transport	PMID:25847153^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	PMID:11032905^[11]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:3380 RGD:620919	F		Seeded From UniProt	complete
part_of	GO:0044304	main axon	PMID:8795614^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0044295	axonal growth cone	PMID:8795614^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	PMID:28785724^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	PMID:15623521^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030425	dendrite	PMID:24298146^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030424	axon	PMID:28785724^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030424	axon	PMID:15623521^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030182	neuron differentiation	PMID:15043998^[16]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:16982696^[17]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:3668	F		Seeded From UniProt	complete
involved_in	GO:0010976	positive regulation of neuron projection development	PMID:25847153^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010033	response to organic substance	PMID:16389547^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0008631	intrinsic apoptotic signaling pathway in response to oxidative stress	PMID:12420308^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008017	microtubule binding	PMID:12805366^[20]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0007613	memory	PMID:15698894^[21]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007584	response to nutrient	PMID:16495207^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007565	female pregnancy	PMID:22884690^[23]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007420	brain development	PMID:19540327^[24]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007017	microtubule-based process	PMID:12805366^[20]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:15750210^[25]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:97175 PANTHER:PTN000161190 RGD:3044 RGD:69329 WB:WBGene00004212	C		Seeded From UniProt	complete
involved_in	GO:0031175	neuron projection development	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000161190 UniProtKB:P11137	P		Seeded From UniProt	complete
enables	GO:0008017	microtubule binding	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0266579 MGI:MGI:97175 MGI:MGI:97178 MGI:MGI:97180 PANTHER:PTN000161190 RGD:3044 RGD:69329 UniProtKB:P10636 WB:WBGene00004212	F		Seeded From UniProt	complete
involved_in	GO:0000226	microtubule cytoskeleton organization	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0266579 MGI:MGI:97175 MGI:MGI:97178 MGI:MGI:97180 PANTHER:PTN000161190 UniProtKB:P10636	P		Seeded From UniProt	complete
enables	GO:0008017	microtubule binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002955	F		Seeded From UniProt	complete
enables	GO:0015631	tubulin binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001084	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:10747907^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
enables	GO:0008017	microtubule binding	PMID:10747907^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0015630	microtubule cytoskeleton	PMID:10747907^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:10747907^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:10747907^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:10747907^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206 UniProtKB-SubCell:SL-0090	C		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0966	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0005874	microtubule	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0493	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
part_of	GO:0030424	axon	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0279	C		Seeded From UniProt	complete
part_of	GO:0030425	dendrite	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0283	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0091	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Kanai, Y et al. (1992) Microtubule bundling by tau proteins in vivo: analysis of functional domains. EMBO J. 11 3953-61 PubMed GONUTS page
↑ ^2.0 ^2.1 Tortosa, E et al. (2009) Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein. J. Alzheimers Dis. 17 319-25 PubMed GONUTS page
↑ ^3.0 ^3.1 Ferreira, A et al. (1989) Microtubule formation and neurite growth in cerebellar macroneurons which develop in vitro: evidence for the involvement of the microtubule-associated proteins, MAP-1a, HMW-MAP2 and Tau. Brain Res. Dev. Brain Res. 49 215-28 PubMed GONUTS page
↑ ^4.0 ^4.1 Carrettiero, DC et al. (2009) The cochaperone BAG2 sweeps paired helical filament- insoluble tau from the microtubule. J. Neurosci. 29 2151-61 PubMed GONUTS page
↑ Tortosa, E et al. (2017) Dynamic Palmitoylation Targets MAP6 to the Axon to Promote Microtubule Stabilization during Neuronal Polarization. Neuron 94 809-825.e7 PubMed GONUTS page
↑ Hou, Z et al. (2007) Microtubule association of the neuronal p35 activator of Cdk5. J. Biol. Chem. 282 18666-70 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 Maas, T et al. (2000) Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments. J. Biol. Chem. 275 15733-40 PubMed GONUTS page
↑ Rahman, A et al. (2012) Over activation of hippocampal serine/threonine protein phosphatases PP1 and PP2A is involved in lead-induced deficits in learning and memory in young rats. Neurotoxicology 33 370-83 PubMed GONUTS page
↑ ^9.0 ^9.1 Chambraud, B et al. (2010) A role for FKBP52 in Tau protein function. Proc. Natl. Acad. Sci. U.S.A. 107 2658-63 PubMed GONUTS page
↑ ^10.0 ^10.1 Kimura, T et al. (2014) Microtubule-associated protein tau is essential for long-term depression in the hippocampus. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 369 20130144 PubMed GONUTS page
↑ ^11.0 ^11.1 Goedert, M et al. (2000) Reduced binding of protein phosphatase 2A to tau protein with frontotemporal dementia and parkinsonism linked to chromosome 17 mutations. J. Neurochem. 75 2155-62 PubMed GONUTS page
↑ ^12.0 ^12.1 Seiberlich, V et al. (2015) Downregulation of the microtubule associated protein tau impairs process outgrowth and myelin basic protein mRNA transport in oligodendrocytes. Glia 63 1621-35 PubMed GONUTS page
↑ ^13.0 ^13.1 Kempf, M et al. (1996) Tau binds to the distal axon early in development of polarity in a microtubule- and microfilament-dependent manner. J. Neurosci. 16 5583-92 PubMed GONUTS page
↑ ^14.0 ^14.1 Kneynsberg, A & Kanaan, NM () Aging Does Not Affect Axon Initial Segment Structure and Somatic Localization of Tau Protein in Hippocampal Neurons of Fischer 344 Rats. eNeuro 4 PubMed GONUTS page
↑ ^15.0 ^15.1 Farah, CA et al. (2005) Interaction of microtubule-associated protein-2 and p63: a new link between microtubules and rough endoplasmic reticulum membranes in neurons. J. Biol. Chem. 280 9439-49 PubMed GONUTS page
↑ Cappelletti, G et al. (2004) The nitration of tau protein in neurone-like PC12 cells. FEBS Lett. 562 35-9 PubMed GONUTS page
↑ Yang, YC et al. (2006) Serum- and glucocorticoid-inducible kinase 1 (SGK1) increases neurite formation through microtubule depolymerization by SGK1 and by SGK1 phosphorylation of tau. Mol. Cell. Biol. 26 8357-70 PubMed GONUTS page
↑ Esposito, G et al. (2006) The marijuana component cannabidiol inhibits beta-amyloid-induced tau protein hyperphosphorylation through Wnt/beta-catenin pathway rescue in PC12 cells. J. Mol. Med. 84 253-8 PubMed GONUTS page
↑ Goldbaum, O & Richter-Landsberg, C (2002) Activation of PP2A-like phosphatase and modulation of tau phosphorylation accompany stress-induced apoptosis in cultured oligodendrocytes. Glia 40 271-82 PubMed GONUTS page
↑ ^20.0 ^20.1 Makrides, V et al. (2003) Microtubule-dependent oligomerization of tau. Implications for physiological tau function and tauopathies. J. Biol. Chem. 278 33298-304 PubMed GONUTS page
↑ Chen, YG (2005) Specific tau phosphorylation sites in hippocampus correlate with impairment of step-down inhibitory avoidance task in rats. Behav. Brain Res. 158 277-84 PubMed GONUTS page
↑ Iuvone, T et al. (2006) The spice sage and its active ingredient rosmarinic acid protect PC12 cells from amyloid-beta peptide-induced neurotoxicity. J. Pharmacol. Exp. Ther. 317 1143-9 PubMed GONUTS page
↑ González-Arenas, A et al. (2012) Expression pattern of Tau in the rat brain during pregnancy and the beginning of lactation. Brain Res. Bull. 89 108-14 PubMed GONUTS page
↑ Bullmann, T et al. (2009) Pattern of tau isoforms expression during development in vivo. Int. J. Dev. Neurosci. 27 591-7 PubMed GONUTS page
↑ Fasulo, L et al. (2005) Apoptotic effect of caspase-3 cleaved tau in hippocampal neurons and its potentiation by tau FTDP-mutation N279K. J. Alzheimers Dis. 7 3-13 PubMed GONUTS page
↑ ^26.0 ^26.1 ^26.2 ^26.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:1396588-1] 1.0 ^1.1 Kanai, Y et al. (1992) Microtubule bundling by tau proteins in vivo: analysis of functional domains. EMBO J. 11 3953-61 PubMed GONUTS page

[PMID:19363271-2] 2.0 ^2.1 Tortosa, E et al. (2009) Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein. J. Alzheimers Dis. 17 319-25 PubMed GONUTS page

[PMID:2509111-3] 3.0 ^3.1 Ferreira, A et al. (1989) Microtubule formation and neurite growth in cerebellar macroneurons which develop in vitro: evidence for the involvement of the microtubule-associated proteins, MAP-1a, HMW-MAP2 and Tau. Brain Res. Dev. Brain Res. 49 215-28 PubMed GONUTS page

[PMID:19228967-4] 4.0 ^4.1 Carrettiero, DC et al. (2009) The cochaperone BAG2 sweeps paired helical filament- insoluble tau from the microtubule. J. Neurosci. 29 2151-61 PubMed GONUTS page

[PMID:28521134-5] Tortosa, E et al. (2017) Dynamic Palmitoylation Targets MAP6 to the Axon to Promote Microtubule Stabilization during Neuronal Polarization. Neuron 94 809-825.e7 PubMed GONUTS page

[PMID:17491008-6] Hou, Z et al. (2007) Microtubule association of the neuronal p35 activator of Cdk5. J. Biol. Chem. 282 18666-70 PubMed GONUTS page

[PMID:10747907-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 Maas, T et al. (2000) Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments. J. Biol. Chem. 275 15733-40 PubMed GONUTS page

[PMID:22387731-8] Rahman, A et al. (2012) Over activation of hippocampal serine/threonine protein phosphatases PP1 and PP2A is involved in lead-induced deficits in learning and memory in young rats. Neurotoxicology 33 370-83 PubMed GONUTS page

[PMID:20133804-9] 9.0 ^9.1 Chambraud, B et al. (2010) A role for FKBP52 in Tau protein function. Proc. Natl. Acad. Sci. U.S.A. 107 2658-63 PubMed GONUTS page

[PMID:24298146-10] 10.0 ^10.1 Kimura, T et al. (2014) Microtubule-associated protein tau is essential for long-term depression in the hippocampus. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 369 20130144 PubMed GONUTS page

[PMID:11032905-11] 11.0 ^11.1 Goedert, M et al. (2000) Reduced binding of protein phosphatase 2A to tau protein with frontotemporal dementia and parkinsonism linked to chromosome 17 mutations. J. Neurochem. 75 2155-62 PubMed GONUTS page

[PMID:25847153-12] 12.0 ^12.1 Seiberlich, V et al. (2015) Downregulation of the microtubule associated protein tau impairs process outgrowth and myelin basic protein mRNA transport in oligodendrocytes. Glia 63 1621-35 PubMed GONUTS page

[PMID:8795614-13] 13.0 ^13.1 Kempf, M et al. (1996) Tau binds to the distal axon early in development of polarity in a microtubule- and microfilament-dependent manner. J. Neurosci. 16 5583-92 PubMed GONUTS page

[PMID:28785724-14] 14.0 ^14.1 Kneynsberg, A & Kanaan, NM () Aging Does Not Affect Axon Initial Segment Structure and Somatic Localization of Tau Protein in Hippocampal Neurons of Fischer 344 Rats. eNeuro 4 PubMed GONUTS page

[PMID:15623521-15] 15.0 ^15.1 Farah, CA et al. (2005) Interaction of microtubule-associated protein-2 and p63: a new link between microtubules and rough endoplasmic reticulum membranes in neurons. J. Biol. Chem. 280 9439-49 PubMed GONUTS page

[PMID:15043998-16] Cappelletti, G et al. (2004) The nitration of tau protein in neurone-like PC12 cells. FEBS Lett. 562 35-9 PubMed GONUTS page

[PMID:16982696-17] Yang, YC et al. (2006) Serum- and glucocorticoid-inducible kinase 1 (SGK1) increases neurite formation through microtubule depolymerization by SGK1 and by SGK1 phosphorylation of tau. Mol. Cell. Biol. 26 8357-70 PubMed GONUTS page

[PMID:16389547-18] Esposito, G et al. (2006) The marijuana component cannabidiol inhibits beta-amyloid-induced tau protein hyperphosphorylation through Wnt/beta-catenin pathway rescue in PC12 cells. J. Mol. Med. 84 253-8 PubMed GONUTS page

[PMID:12420308-19] Goldbaum, O & Richter-Landsberg, C (2002) Activation of PP2A-like phosphatase and modulation of tau phosphorylation accompany stress-induced apoptosis in cultured oligodendrocytes. Glia 40 271-82 PubMed GONUTS page

[PMID:12805366-20] 20.0 ^20.1 Makrides, V et al. (2003) Microtubule-dependent oligomerization of tau. Implications for physiological tau function and tauopathies. J. Biol. Chem. 278 33298-304 PubMed GONUTS page

[PMID:15698894-21] Chen, YG (2005) Specific tau phosphorylation sites in hippocampus correlate with impairment of step-down inhibitory avoidance task in rats. Behav. Brain Res. 158 277-84 PubMed GONUTS page

[PMID:16495207-22] Iuvone, T et al. (2006) The spice sage and its active ingredient rosmarinic acid protect PC12 cells from amyloid-beta peptide-induced neurotoxicity. J. Pharmacol. Exp. Ther. 317 1143-9 PubMed GONUTS page

[PMID:22884690-23] González-Arenas, A et al. (2012) Expression pattern of Tau in the rat brain during pregnancy and the beginning of lactation. Brain Res. Bull. 89 108-14 PubMed GONUTS page

[PMID:19540327-24] Bullmann, T et al. (2009) Pattern of tau isoforms expression during development in vivo. Int. J. Dev. Neurosci. 27 591-7 PubMed GONUTS page

[PMID:15750210-25] Fasulo, L et al. (2005) Apoptotic effect of caspase-3 cleaved tau in hippocampal neurons and its potentiation by tau FTDP-mutation N279K. J. Alzheimers Dis. 7 3-13 PubMed GONUTS page

[PMID:21873635-26] 26.0 ^26.1 ^26.2 ^26.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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