HUMAN:TADBP

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	TARDBP (synonyms: TDP43)
Protein Name(s)	TAR DNA-binding protein 43 TDP-43
External Links
UniProt	Q13148
EMBL	U23731 EF434181 EF434182 EF434183 AK295920 AK312416 CR533534 AK222754 AL050265 AL109811 CH471130 BC071657 BC095435
CCDS	CCDS122.1
PIR	I38977
RefSeq	NP_031401.1
UniGene	Hs.300624
PDB	1WF0 2CQG 4BS2 4IUF
PDBsum	1WF0 2CQG 4BS2 4IUF
ProteinModelPortal	Q13148
SMR	Q13148
BioGrid	117003
DIP	DIP-31167N
IntAct	Q13148
MINT	MINT-5002768
STRING	9606.ENSP00000240185
ChEMBL	CHEMBL2362981
PhosphoSite	Q13148
DMDM	20140568
MaxQB	Q13148
PaxDb	Q13148
PRIDE	Q13148
DNASU	23435
Ensembl	ENST00000240185
GeneID	23435
KEGG	hsa:23435
UCSC	uc001art.3 uc010oap.2
CTD	23435
GeneCards	GC01P011072
GeneReviews	TARDBP
HGNC	HGNC:11571
HPA	CAB003703 HPA017284
MIM	605078 612069
neXtProt	NX_Q13148
Orphanet	803 275872
PharmGKB	PA36336
eggNOG	COG0724
GeneTree	ENSGT00730000110584
HOVERGEN	HBG058671
InParanoid	Q13148
OMA	KHNSSRQ
PhylomeDB	Q13148
TreeFam	TF315657
ChiTaRS	TARDBP
EvolutionaryTrace	Q13148
GeneWiki	TARDBP
GenomeRNAi	23435
NextBio	35472434
PRO	PR:Q13148
Proteomes	UP000005640
Bgee	Q13148
CleanEx	HS_TARDBP
ExpressionAtlas	Q13148
Genevestigator	Q13148
GO	GO:0005634 GO:0003690 GO:0042802 GO:0003730 GO:0000166 GO:0044822 GO:0003723 GO:0001205 GO:0003700 GO:0070935 GO:0006397 GO:0043922 GO:0008380 GO:0006366
Gene3D	3.30.70.330
InterPro	IPR012677 IPR000504
Pfam	PF00076
SMART	SM00360
PROSITE	PS50102

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0071765	nuclear inner membrane organization	PMID:18305152^[1]	ECO:0000315			P	Figure 4 - "The lack of TDP-43 led to an uneven distribution of the nuclear envelope protein emerin along the membrane, with discrete regions of either protein accumulation or lack of protein" This proves that TDP-30 is involved in the organization of the nuclear inner membrane. With the depletion of TDP-30 the proteins that make up the inner membrane of the nucleus began to be disorganized all across the membrane.	complete CACAO 7485
	GO:0042981	regulation of apoptotic process	PMID:18305152^[1]	ECO:0000315			P	Figure 4 - "U2OS showed an increase in TUNEL staining and nuclear fragmentation upon TDP-43 depletion" Part B in the figure shows that with the depletion of TDP-43 nuclear fragmentation involved in apoptosis began. The samples used were also positive for enzymes consistant with programmed cell death.	complete CACAO 7490
	GO:0051726	regulation of cell cycle	PMID:18305152^[1]	ECO:0000315			P	Figure 3 - "U2OS cells showed an alteration of the cell cycle pattern after removal of TDP-43 (Fig. 3B) resulting in a 60% decrease of cells in G0/G1 accompanied by a corresponding increase in S and G2/M cells." This proves that TDP-43 regulates the distribution of the cell cycle phases.	complete CACAO 7497
	GO:0001933	negative regulation of protein phosphorylation	PMID:18305152^[1]	ECO:0000315			P	Figure 3 - shows that when TDP-43 was silenced there was an increase in the phosphorylation of pRb and p130	complete CACAO 7502
	GO:0010629	negative regulation of gene expression	PMID:18305152^[1]	ECO:0000315			P	Figure 2 shows that depletion of TDP-43 led to the up-regulation of Cyclin-Dependent Protein Kinase 6 proving that TDP-43 negatively regulates the gene expression of CDK6.	complete CACAO 7513
	GO:0061158	3'-UTR-mediated mRNA destabilization	PMID:28335005^[2]	ECO:0000314			P	Organism: Homo sapiens. Paper’s Protein Name: Transactive response DNA-binding protein 43 (TDP-43). UniProt’s Protein Name: TAR DNA-binding protein 43. Notes: This is seen in Figure 2B. The paper states that “to study whether TDP-43 promoted tau mRNA instability through the 3΄-UTR of the mRNA, we fused tau 3΄-UTR to the C-terminal of green fluorescence protein (GFP) to make pEGFP/tau 3΄-UTR plasmid. This plasmid allowed us to study the regulation of tau mRNA through its 3΄-UTR by measuring the expression of GFP.” As can be seen in Figure 2B, expression of GFP decreased with an increased dosage of the protein.	complete CACAO 12354
involved_in	GO:0031647	regulation of protein stability	PMID:27123980^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	PMID:18305152^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0001933	negative regulation of protein phosphorylation	PMID:18305152^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051726	regulation of cell cycle	PMID:18305152^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042981	regulation of apoptotic process	PMID:18305152^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0071765	nuclear inner membrane organization	PMID:18305152^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000054	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0070935	3'-UTR-mediated mRNA stabilization	PMID:17481916^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0043922	negative regulation by host of viral transcription	PMID:7745706^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0008380	RNA splicing	PMID:11285240^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:17481916^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:11285240^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003730	mRNA 3'-UTR binding	PMID:17481916^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:11285240^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003690	double-stranded DNA binding	PMID:7745706^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22681889^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0001215 FB:FBgn0004237 FB:FBgn0004838 MGI:MGI:1916394 PANTHER:PTN002689974 UniProtKB:P09651 UniProtKB:P19338 UniProtKB:P22626 UniProtKB:Q14103 UniProtKB:Q96EP5 UniProtKB:Q99729	C	Seeded From UniProt	complete
involved_in	GO:0070935	3'-UTR-mediated mRNA stabilization	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002691014 UniProtKB:Q13148	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002691014 RGD:1310906	C	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002691014 UniProtKB:Q13148	C	Seeded From UniProt	complete
enables	GO:0003730	mRNA 3'-UTR binding	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002691014 UniProtKB:Q13148	F	Seeded From UniProt	complete
enables	GO:0003727	single-stranded RNA binding	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002691014 WB:WBGene00006514	F	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104819 MGI:MGI:1330294 MGI:MGI:893588 MGI:MGI:97286 PANTHER:PTN002689974 RGD:1306751 RGD:1310403 RGD:1310906 RGD:3153 RGD:69234 SGD:S000003391 SGD:S000005483 TAIR:locus:2019622 TAIR:locus:2076096 TAIR:locus:2079874 TAIR:locus:2083810 TAIR:locus:2122009 TAIR:locus:2159401 TAIR:locus:2179939 UniProtKB:P19338 UniProtKB:P22626 UniProtKB:P38159 UniProtKB:P62995 UniProtKB:Q03250 UniProtKB:Q13148 UniProtKB:Q14103 UniProtKB:Q9SVM8	F	Seeded From UniProt	complete
enables	GO:0003690	double-stranded DNA binding	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002691014 UniProtKB:Q13148	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:26735904^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13148	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:26099433^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13148	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23384725^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13148	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22193716^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13148	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21666678^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13148	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19383787^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13148	F	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003700	P	Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0001228	P	Seeded From UniProt	complete
part_of	GO:0035061	interchromatin granule	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:I6L9G6 ensembl:ENSRNOP00000041889	C	Seeded From UniProt	complete
involved_in	GO:0034976	response to endoplasmic reticulum stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:I6L9G6 ensembl:ENSRNOP00000041889	P	Seeded From UniProt	complete
involved_in	GO:0032024	positive regulation of insulin secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:I6L9G6 ensembl:ENSRNOP00000041889	P	Seeded From UniProt	complete
part_of	GO:0016607	nuclear speck	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:I6L9G6 ensembl:ENSRNOP00000041889	C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:I6L9G6 ensembl:ENSRNOP00000041889	C	Seeded From UniProt	complete
part_of	GO:0005726	perichromatin fibrils	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:I6L9G6 ensembl:ENSRNOP00000041889	C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:I6L9G6 ensembl:ENSRNOP00000041889	C	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:I6L9G6 ensembl:ENSRNOP00000041889	F	Seeded From UniProt	complete
enables	GO:1990837	sequence-specific double-stranded DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q921F2 ensembl:ENSMUSP00000081142	F	Seeded From UniProt	complete
involved_in	GO:0042752	regulation of circadian rhythm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q921F2 ensembl:ENSMUSP00000081142	P	Seeded From UniProt	complete
involved_in	GO:0042307	positive regulation of protein import into nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q921F2 ensembl:ENSMUSP00000081142	P	Seeded From UniProt	complete
involved_in	GO:0031647	regulation of protein stability	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q921F2 ensembl:ENSMUSP00000081142	P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q921F2 ensembl:ENSMUSP00000081142	C	Seeded From UniProt	complete
enables	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q921F2 ensembl:ENSMUSP00000081142	F	Seeded From UniProt	complete
enables	GO:0003676	nucleic acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000504 InterPro:IPR035979	F	Seeded From UniProt	complete
involved_in	GO:0006366	transcription by RNA polymerase II	PMID:7745706^[5]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	PMID:7745706^[5]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0048511	rhythmic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0090	P	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
involved_in	GO:0008380	RNA splicing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0508	P	Seeded From UniProt	complete
involved_in	GO:0006397	mRNA processing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0507	P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0694	F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
part_of	GO:0010494	cytoplasmic stress granule	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0496	C	Seeded From UniProt	complete
edit table

Notes

References

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

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 ^1.7 ^1.8 ^1.9 Ayala, YM et al. (2008) TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression. Proc. Natl. Acad. Sci. U.S.A. 105 3785-9 PubMed GONUTS page
↑ Gu, J et al. (2017) TDP-43 suppresses tau expression via promoting its mRNA instability. Nucleic Acids Res. PubMed GONUTS page
↑ Hirano, A et al. (2016) USP7 and TDP-43: Pleiotropic Regulation of Cryptochrome Protein Stability Paces the Oscillation of the Mammalian Circadian Clock. PLoS ONE 11 e0154263 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Strong, MJ et al. (2007) TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein. Mol. Cell. Neurosci. 35 320-7 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Ou, SH et al. (1995) Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J. Virol. 69 3584-96 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Buratti, E et al. (2001) Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. EMBO J. 20 1774-84 PubMed GONUTS page
↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 ^9.7 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Lim, L et al. (2016) ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. PLoS Biol. 14 e1002338 PubMed GONUTS page
↑ Che, MX et al. (2015) TDP-35 sequesters TDP-43 into cytoplasmic inclusions through binding with RNA. FEBS Lett. 589 1920-8 PubMed GONUTS page
↑ Chang, CK et al. (2013) Molecular mechanism of oxidation-induced TDP-43 RRM1 aggregation and loss of function. FEBS Lett. 587 575-82 PubMed GONUTS page
↑ Cohen, TJ et al. (2012) Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking. EMBO J. 31 1241-52 PubMed GONUTS page
↑ Guo, W et al. (2011) An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity. Nat. Struct. Mol. Biol. 18 822-30 PubMed GONUTS page
↑ Zhang, YJ et al. (2009) Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity. Proc. Natl. Acad. Sci. U.S.A. 106 7607-12 PubMed GONUTS page

[PMID:18305152-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 ^1.7 ^1.8 ^1.9 Ayala, YM et al. (2008) TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression. Proc. Natl. Acad. Sci. U.S.A. 105 3785-9 PubMed GONUTS page

[PMID:28335005-2] Gu, J et al. (2017) TDP-43 suppresses tau expression via promoting its mRNA instability. Nucleic Acids Res. PubMed GONUTS page

[PMID:27123980-3] Hirano, A et al. (2016) USP7 and TDP-43: Pleiotropic Regulation of Cryptochrome Protein Stability Paces the Oscillation of the Mammalian Circadian Clock. PLoS ONE 11 e0154263 PubMed GONUTS page

[PMID:17481916-4] 4.0 ^4.1 ^4.2 Strong, MJ et al. (2007) TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein. Mol. Cell. Neurosci. 35 320-7 PubMed GONUTS page

[PMID:7745706-5] 5.0 ^5.1 ^5.2 ^5.3 Ou, SH et al. (1995) Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J. Virol. 69 3584-96 PubMed GONUTS page

[PMID:11285240-6] 6.0 ^6.1 ^6.2 Buratti, E et al. (2001) Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. EMBO J. 20 1774-84 PubMed GONUTS page

[PMID:22681889-7] Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page

[PMID:22658674-8] Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page

[PMID:21873635-9] 9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 ^9.7 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:26735904-10] Lim, L et al. (2016) ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. PLoS Biol. 14 e1002338 PubMed GONUTS page

[PMID:26099433-11] Che, MX et al. (2015) TDP-35 sequesters TDP-43 into cytoplasmic inclusions through binding with RNA. FEBS Lett. 589 1920-8 PubMed GONUTS page

[PMID:23384725-12] Chang, CK et al. (2013) Molecular mechanism of oxidation-induced TDP-43 RRM1 aggregation and loss of function. FEBS Lett. 587 575-82 PubMed GONUTS page

[PMID:22193716-13] Cohen, TJ et al. (2012) Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking. EMBO J. 31 1241-52 PubMed GONUTS page

[PMID:21666678-14] Guo, W et al. (2011) An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity. Nat. Struct. Mol. Biol. 18 822-30 PubMed GONUTS page

[PMID:19383787-15] Zhang, YJ et al. (2009) Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity. Proc. Natl. Acad. Sci. U.S.A. 106 7607-12 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

HUMAN:TADBP

Contents

Annotations

Notes

References

3

c

d

e

h

i

m

n

p

r

s

t

v

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools