DNAJA1 Antibody, FITC conjugated

1. that DNAJA1 controls the fate of misfolded stabilization of mutant p53 PMID: 27775703
2. Therefore, we propose that DnaJA1 is co-opted by the influenza A virus to enter the nucleus and to enhance its RNA polymerase activity in an Hsp70 cochaperone-independent manner. PMID: 25253355
3. structure and function of human DNAJA1 and its relationship to pancreatic cancer PMID: 24512202
4. we combined the Hsp70-NEF pairs with cochaperones of the J protein family (DnaJA1, DnaJA2, DnaJB1, and DnaJB4) to generate 16 permutations. PMID: 24318877
5. Moreover, the levels of DnaJA1 and Hsp70 seem to play against each other with regard to tau: as DnaJA1 levels increase, tau levels are reduced, but this can be prevented if Hsp70 levels are simultaneously induced. PMID: 22343013
6. Hdj2 directly associates with Japanese encephalitis virus nonstructural protein NS5 and facilitates viral replication. PMID: 21999493
7. Hsc70 and a dimer of DjA1 independently bind to an unfolded protein PMID: 20363747
8. Hsp40 type 1 chaperones DJA1 (DNAJA1/Hdj2) and DJA2 (DNAJA2) as key modulators of hERG degradation PMID: 19940115
9. Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy PMID: 11796717
10. HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor PMID: 11809754
11. sequence analysis of two isoforms PMID: 12974469
12. Multiple tissue polymerase chain reaction (PCR) results showed that nDnaJA1 expressed highly in testis and lung but low in thymus, prostate, colon and liver PMID: 15595953
13. Results indicate that DjA1 and DjB4 of subfamilies A and B of human Hsp40 have different quaternary structures and chaperone functions. PMID: 15661747
14. DJA1 was inhibitory of refolding with DJA2 and Hsc70. PMID: 18684711

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HGNC: 5229

OMIM: 602837

KEGG: hsa:3301

STRING: 9606.ENSP00000369127

UniGene: Hs.445203