Publication for Hspd1 and Hspa9

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Hspd1	heat shock protein 1 (chaperonin)	15510			[link]
mmu	Hspa9	heat shock protein 9	15526

Pubmed ID	Priority	Text
30822691	0.99	HSP60-mtHSP70-Lon that leads to the sequestration of HSP60 in mitochondria.
31428613	0.99	HSP60 is able to interact with different HSPs, such as HSP10, forming a complex that mediates protein folding, and with mitochondrial HSP70 (HSP70A), also known as mortalin, that have a role in cell proliferation and stress.
31601784	0.98	HSP60 in tumor cells could directly bind with Cyclophilin D (CypD), an important modulator conferring sensitivity of the opening of the mitochondrial permeability transition pore (mPTP) to Cyclosporin A (CsA).
	0.98	CsA resulted in a decrease in cell apoptosis of yolk sac erythrocytes in mutant mice, further supporting the significant protective role of HSP60 in regulating mPTP opening and cell apoptosis in early erythropoiesis.
	0.96	HSP60 and restored at least partially due to CsA treatment.
	0.91	CsA on cell survival of yolk sac erythrocytes after HSP60 deletion, and found that injection of CsA using the same protocol was also able to dramatically reduce cell apoptosis in HSP60CKO yolk sac erythrocytes (Fig. 6a-c), even though the inhibition of cell apoptosis by CsA treatment (about 80%) was slightly lower than that by the direct caspase inhibitor.
	0.90	HSP60 functions as the inhibitor CsA, preventing CypD from binding to mPTP and sensitizing the pore opening.
	0.86	HSP60 in these cells reduced mitochondrial membrane potential and resulted in cell apoptosis, suggesting that HSP60 might play a similar function as CsA, inhibiting the opening of mPTP via binding to CypD. Therefore, we isolated single cells from E8.5 control and HSP60CKO yolk sacs, and performed flow cytometry to examine whether HSP60 deficiency could also affect the mitochondrial membrane potential of yolk sac erythrocytes.
28433661	0.98	GRP75) and HSP 60 are constitutively expressed in the cytosol and mitochondria and are involved in various chaperoning functions in aiding the translocation of nascent polypeptides and the correct refolding of proteins from the cytoplasm into the mitochondrial matrix.
	0.96	GRP75, 75 kDa glucose-regulated protein), presequence protease, lon protease, HSP 60, and MPP, which proteins mediates mitochondrial protein translocation and folding.
	0.93	HSP 60, HSP 70 (GRP 75), presequence protease, lon protease, and MPP in the SOD2-tg mouse heart
	0.90	GRP 75), HSP 60, matrix processing peptidase (MPP), presequence protease (PREP), and lon protease (LONM) in the murine SOD2-tg heart
20043987	0.98	Hsp60 and mtHsp70, which are part of a poorly understood molecular motor.
	0.97	Hsp60 and mtHsp70 SNO protein formation, but after E. coli administration, SNO levels for both proteins increased only in Wt mice (Fig. 8A; left panel).
	0.96	Hsp60 (Fig. 6C) and mtHsp70 (mortalin; Fig. 6D).
26890141	0.98	HSP60 (Hspd1), 3 HSP70s (Hspa1a, Hspa1b and Hspa9), 2 small HSPs family members (Hspb7/Hsp27 and Serpinh1/Hsp47) and 4 other chaperones (Bag3, Cct4, Cryab and Pfdn1) are possible targets of PGC1alpha given that their expression levels are dependent on PGC1alpha (Figure 1c).
	0.98	Hspd1/HSP60 and Hspa9/mtHSP70 devoted to organelle protection from proteotoxic stress are regulated by PGC1alpha.
	0.96	HSPd1, HSPa1a, HSPa9 and Bag3, were further validated by real-time PCR in 10T1/2 cells overexpressing PGC1alpha (Figure 1d).
27684481	0.98	mtHsp70 (encoded by Hspa9) and Hsp60 (encoded by Hspd1) family members have been recognized as major players that facilitate the folding of nuclear-encoded proteins when they are imported into mitochondria (Fig 4D).
	0.98	Hsp60, Hsp10, and mtHsp70 are organelle-specific biomarkers that are considered to reflect mitochondria stress.
	0.98	Hsp60 and Grpel1, known regulators of mtHsp70 (Table 1).
25543897	0.98	mtHsp70, Hsp60 and Hsp10 fold and assemble proteins that are imported into the mitochondria and refold damaged mitochondrial proteins.
	0.98	Hsp60, Hsp10, mtHsp70, ClpP, Lonp1 and Ubl5 form a tight coexpression network in mice GRPs and human populations, suggestive of their transcriptional control.
28943839	0.98	Hsp60 associated with Hsp10, as well as the mitochondrial Hsp70 (mtHsp70) and the mitochondrial Hsp90 analog TRAP1.
	0.98	Hsp60, and mitochondrial Hsp70 (HspA9) while it also leads to a transcriptional repression of a number of nuclear genes, in order to reduce the load of protein misfolding.
29132502	0.98	Hsp60/Hspd1), 10 kDa heat shock protein (Hspe1) and mitochondrial stress-70 protein (mtHsp70/Hspa9).
	0.95	HSPD1, HSPE1, and HSPA9 in all five knockouts (Figure 5D; Figure 5:figure supplement 1B; box plots in Supplementary file 8).
30761259	0.98	HSP60, HSP90, and GRP75, chaperone proteins 34, CoQ10 treatment significantly suppressed the induction of these proteins.
	0.64	heat shock protein (HSP) 60, HSP90, and glucose-regulated protein (GRP) 75 (also known as mtHSP70) (Fig. 6C-F).
19786549	0.98	75-kDa glucose-regulated protein (GRP75/HSP75/mortalin/TRAP-1), HSP60 and HSP70 are essential mitochondrial chaperones.
22860010	0.98	Hspd1, Hspa2, Hspa9, Table 1), which are modulated in other models of cellular stress (e.g.).
23870130	0.98	mtHSP70, HSP60 and HSP10 and the protease CLPP.
25762445	0.98	HSP60, HSP10 and mtHSP70 during heat shock in mouse cells, and SSBP1, which localizes mostly in the mitochondria, enhances their expression by potentiating the transcriptional activity of HSF1 (Figs 6, 7).
26833085	0.98	Hspd1, Hspa9, Clpx and Lonp1 that all encode components of the mitochondrial unfolded protein response (UPRmt) (ref.):a still poorly characterized mitochondrial stress response pathway in mammals:show strong association with Fh1 (Fig. 3d and Supplementary Data 16).
28636406	0.98	HSPA9, HSP90AA1, HSPB90, HSPBP1, HSPD1, HSPG2, HSPH1 (Figure 5).
28664093	0.98	Hsp60, mtHsp70, and Hsp70, which are integral to the stabilization, import, and refolding of precursor proteins into mitochondria.
29082112	0.98	mtHSP70 and HSP60-HSP10.
29755410	0.98	mtHsp70 and the Hsp60/10 complexes.
31752429	0.98	HSPD1, and HSPA9), regulators of cell cycle (CDK1 and BUB3) components of insulin/IGF1 signalling (INSR and IGF1R) and the zinc metallopeptidase ZMPSTE24, highlighting the fact that HSF1 may play a role in ageing via maintaining cellular proteostasis and affecting the insulin/IGF1 pathway (Figure 4B and Table S12).
24658151	0.97	HSPD1, HSPA5, HSPA8 and HSPA9) were decreased in female mice, but not males.
	0.95	HSPA9 and HSPD1), one serum carrier protein (TF), and one energy production protein (PCX), were also increased after chronic alcohol feeding.
27992860	0.97	mtHSP70, there is some evidence to suggest that HSP60/HSP10 are pro-apoptotic.
	0.96	mtHSP70, HSP60/HSP10 chaperonin system interacts with the incompletely folded protein.
26913604	0.97	hspa9 (closest hsp-6 homolog in mouse); however, no induction of hspd1 was observed (closest hsp-60 homolog) (Supplementary Figure S5).
29765493	0.97	HSP60 protein expression and a more significant increase (41.1%, p < 0.01) in GRP75 protein expression (Table 1, Figure 2).
30538632	0.97	HSPA9 and HSPD1 mRNAs were significantly upregulated in CCl4-treated mice, but STF-083010 had no effect on their expression.
30830936	0.97	Hsp60 (also known as Hspd1), a major mitochondrial chaperon, was not significantly altered, the expression of mtHsp70 (also known as Grp75, Mortalin, or Hspa9), a key factor for protein folding in the matrix and for protein import from the cytosol to the mitochondrion, was slightly up-regulated (Fig 3D).
31279933	0.97	HSP60, mtHSP70, and peptidase ClpP, tended to increase during CR (Figure 4C).
21819105	0.95	Hsp60 or Hsp10, proteins known to associate with HspA9, were found equally distributed in immunoprecipitation eluates collected from DJ-1 knockout and wild-type extracts.
24815183	0.94	HSPD1, HSPA9 and DSPE1) and the Clpp1 protease were not changed in any of comparisons, whereas heat-shock proteins HSPA5 and HSP90D1 were decreased under DR (Supplementary Data 1-3).
28851515	0.93	HSP60, TNF Receptor-Associated Protein 1 (TRAP1), and Mortalin.
23134655	0.92	Hspd1 (60 kDa heat shock protein), Trap1 (Heat shock protein 75 kDa) and Hspa9 (Stress-70 protein).
31033440	0.92	Hspa9, Hspd1) unfolded-protein responses (UPR) were not significantly increased.
24324727	0.59	GRP75, but not HSP60, associated with TFAM in the Sod2 +/-