Publication for HSPA9 and HSPD1

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
hsa	HSPA9	heat shock protein family A (Hsp70) member 9	3313			[link]
hsa	HSPD1	heat shock protein family D (Hsp60) member 1	3329

Pubmed ID	Priority	Text
25675302	0.98	Hsp60-mtHsp70 complex.
	0.98	Hsp60-mtHsp70 complex
	0.98	Hsp60 and mtHsp70 as Lon-associated proteins that were found on both lists of gel-based and shotgun proteomic analysis (Supplementary Tables S5 and S6).
	0.98	Hsp60-mtHsp70 complex, we first knocked down the expression of Hsp60 and mtHsp70 by shRNA to examine the effect on their interaction.
	0.97	Hsp60-mtHsp70 complex is also involved in cell death and survival as well as mtDNA stability.
	0.97	Hsp60-mtHsp70 complex and potentially suggest a critical role of Lon-Hsp60 interaction in the molecular function of Lon-Hsp60-mtHsp70 complex in mitochondria.
	0.97	Hsp60 and mtHsp70 under heat shock (Figure 5c).
	0.97	Hsp60, and mtHsp70 are binding partners of Lon, and they were validated by Co-IP and co-localization experiments, which is consistent with the finding that Lon interacts with NDUFS8 of mitochondrial complex I that is involved in the ROS generation induced by Lon.
	0.97	Hsp60 within Lon-Hsp60-mtHsp70 complex will affect the activation of apoptosis and the cell survival.
	0.97	Hsp60-mtHsp70 complex.
	0.97	Hsp60-mtHsp70 complex as a cytoprotective chaperone network to enhance cell survival under oxidative stress.
	0.97	Hsp60 and mtHsp70, suggesting that the protein stability of Hsp60-mtHsp70 complex is dependent on Lon.
	0.96	Hsp60-mtHsp70 complex.
	0.96	Hsp60-mtHsp70 complex in cells.
	0.96	Hsp60 decreases the binding ability of Lon with mtHsp70 according to the Co-IP experiment (Figures 4b and c).
	0.96	Hsp60-mtHsp70 complex.
	0.95	Hsp60 and mtHsp70 depends on the level of Lon under oxidative stress.
	0.95	Hsp60 and mtHsp70 levels were downregulated beginning from 1 h after the treatment (Figure 5b, right panel).
	0.95	Hsp60 and mtHsp70 after cellular stress challenge in 293 cells, especially Hsp60 (Figures 5b and c).
	0.95	Hsp60, and mtHsp70 as Lon-associated proteins through a proteomic approach that combines Co-IP and in-solution digestion.
	0.94	mtHsp70 has no significant effect on the binding ability of Lon with Hsp60 (Figure 4d).
	0.94	Hsp60-mtHsp70 complex
	0.94	Hsp60-mtHsp70 complex are stress proteins, and they are responsible for the PQC in mitochondria under cellular stress, such as UV and oxidative stress.
	0.94	Hsp60-mtHsp70 complex under environmental stress.
	0.94	Hsp60 and mtHsp70 is dependent on the level of Lon under oxidative stress.
	0.93	Hsp60-mtHsp70 complex under oxidative stress.
	0.93	Hsp60 and mtHsp70 level was reversely correlated to the one in cleaved caspase 3 and p53 apoptotic markers (Figures 5b and 6A), confirming that Hsp60 and mtHsp70 are involved in the regulation of apoptosis.
	0.93	Hsp60 and mtHsp70 under heat-shock stress.
	0.92	Hsp60-mtHsp70 complex
	0.92	Hsp60-mtHsp70 complex in apoptosis regulation.
	0.92	Hsp60-mtHsp70 complex.
	0.92	mtHsp70, or (d and g) anti-Hsp60 to examine the interaction between endogenous Lon and either Hsp60 or mtHsp70 as well as the interaction between Hsp60 and mtHsp70.
	0.92	Hsp60-mtHsp70 complex has an essential role in Lon-mediated inhibition of apoptosis under oxidative stress.
	0.90	Hsp60-mtHsp70 and further protects cell from apoptosis under environmental stress through binding with Hsp60 or mtHsp70.
	0.89	Hsp60 and mtHsp70 under oxidative stress, suggesting that the protein stability of Hsp60-mtHsp70 complex is dependent on Lon.
	0.89	Hsp60 leads to the instability of Lon-mtHsp70 interaction.
	0.87	mtHsp70 (red) or anti-Hsp60 (green) and anti-myc (red) antibodies, respectively.
	0.86	Hsp60, mtHsp70, or Lon.
	0.85	mtHsp70 and Hsp60 were found in the same interaction network (Supplementary Figure S3C).
	0.85	Hsp60 and mtHsp70 either (Figure 4e).
	0.85	Hsp60 and mtHsp70 are proposed.
	0.83	mtHsp70 and Hsp60 in either 293/Lon cells (Figure 3d) or 293 cells under oxidative stress (Supplementary Figure S5), in which the interaction between Hsp60 and mtHsp70 was used as a positive control.
	0.83	Hsp60-mtHsp70 complex after oxidative stress challenge.
	0.82	mtHsp70 (red), anti-Hsp60 (green), or anti-myc (red) as indicated, following image capture by fluorescence microscopy.
	0.81	Hsp60 and mtHsp70 (Figure 7).
	0.80	Hsp60-mtHsp70 complex and inhibits apoptosis via stabilizing the Hsp60-p53 complex.
	0.79	Hsp60 and mtHsp70 to allow them to execute their anti-apoptotic function.
	0.74	Hsp60 with mtHsp70 (Figure 4g).
	0.72	Hsp60-mtHsp70 complex
	0.71	mtHSP70, Hsp60, and ATPB (Table 1), which are associated with mtDNA to form nucleoids.
	0.61	Hsp60-mtHsp70 complex was first examined by Co-IP experiment.
	0.57	Hsp60 and mtHsp70 forms a complex and are overexpressed in cancer cells and have crucial roles in modulating the apoptotic pathways and in cancer development.
	0.54	Hsp60 and mtHsp70 was similar to that of Lon, which was increased after 4 h in a time-dependent manner (Figure 5b, left panel).
31439814	0.98	HSP60 and GRP75, were unchanged, while the quality-control proteases CLPP and paraplegin showed trends toward a decrease (Fig. 7 B and C).
	0.97	HSP60, GRP75, and CS.
	0.97	HSP60, GRP75, and CS were measured by Western blot.
	0.96	HSP60 and GRP75, typical biomarkers for activation of UPRmt.
	0.95	HSP60 and GRP75 under mitochondrial stress.
	0.93	HSP60 and GRP75, showed no nuclear translocation.
	0.60	HSP60/HSP10 and GRP75/TID1 (also known as mtHSP70/DNAJA3) and proteases is involved in the folding and quality control processes, respectively.
	0.58	HSP60, GRP75, and CLPP.
30107089	0.97	mot-2 can consequently lead to a reduction in mot-2's protein partner, HSP60.
	0.97	mot-2/HSP60 in cancer cells could be one of the molecular mechanisms behind the VTD-induced apoptosis and growth arrest.
	0.96	Mot-2-dependent internalization of nuclear-coded proteins to mitochondria is a necessary step for importing cytosolic proteins before they go through folding and protein quality control steps dominantly maintained by mot-2's chaperone partner, HSP60, in the mitochondrial matrix (Agsteribbe et al., 1993; Deocaris et al., 2008; Langer and Neupert, 1991).
	0.95	mot-2/HSP60 chaperone complexes in both cytoplasm and mitochondrial compartments
	0.95	mot-2 and its chaperone partner, HSP60, in both cytoplasmic and mitochondrial compartments.
	0.92	mot-2 and HSP60 proteins by the VTD-UBXN2A axis in cancer cells.
	0.87	mot-2, anti-HSP60, and anti-HSC70 antibodies.
	0.81	HSP60, a major partner of mot-2, shows a similar reduction in both cytoplasmic and mitochondrial compartments alongside reduction in mot-2 proteins.
	0.52	mot-2 and its chaperone partner, HSP60.
	0.52	mot-2 and HSP60 in both cytosolic- and mitochondrial-enriched fractions, whereas HSC70 levels slightly decreased in the presence of VTD.
18371210	0.97	GRP75 and HSP60 increased significantly, compared with the pre-intervention values (Table 2).
	0.96	HSP60 and GRP75 was associated with increased skeletal muscle citrate synthase activity (CS).
	0.94	HSP60 and glucose-regulated protein 75 (GRP75) are located in the mitochondria, where they are involved in the trafficking and processing of nuclear encoded peptides.
	0.92	HSP60 and GRP75 in the IGT subjects while no response was found in cytoplasmic chaperones HSP72 and HSP90.
	0.91	GRP75 and HSP60 are essential for mitochondrial function and biogenesis.
	0.88	HSP60 or GRP75 expression.
	0.87	HSP60 increased (79% in the IGTslow and 38% IGTfast group) significantly in both groups (IGTslow: P = 0.034 and IGTfast: P = 0.029) and GRP75 increased (38%) significantly in the IGTslow group (P = 0.022), while only a tendency was recorded in the IGTfast group (P = 0.072; Figure 2).
	0.66	GRP75 and HSP60 in the vastus lateralis muscle of subjects with impaired glucose tolerance (IGT), divided into slow (n = 10) and fast (n = 12) fibre type sub-groups.
21056633	0.97	GRP75, and HSP60.
	0.89	GRP75, in concert with HSP60, is thought to participate in the refolding of proteins translocated into the mitochondria.
31100073	0.97	HSPA9, HSP60 and LonP1 were all increased in cells expressing either Wt- or A315T-mutant TDP-43 (Fig 5A).
	0.82	HSPA9 and HSP60 proteins were not changed in the patient brains.
25606560	0.97	Hsp60 and mtHsp70 (mortalin), all of which perform the vital functions of importing, transporting, refolding, and preventing aggregation of mitochondrial proteins.
19332121	0.96	HSP60 and mortalin/GRP75/mtHSP70 are key protein processing chaperones in the mitochondria, with roles in matrix protein folding and mitochondrial protein import, respectively.
	0.90	heat shock protein 60 (HSP60, chaperonin), and mortalin, also known as glucose regulated protein 75 or mitochondrial heat shock protein 70 (mortalin/GRP75/mtHSP70).
	0.90	HSP60 and Mortalin/GRP75/mtHSP70 interacted with frataxin, a protein involved in iron-sulfur (Fe-S) cluster biogenesis for Fe-S cluster-dependent enzymes.
	0.86	HSP60 and mortalin/GRP75/mtHSP70.
27426517	0.96	HSP60, mtHSP70, LONP1 and impaired cell growth (Figures 4G and S3E) in an oncocytic cell line harboring multiple mtDNA lesions that impair respiratory chain activity further supporting the role for ATF5-dependent transcription during mitochondrial dysfunction.
	0.78	HSP60, mtHSP70, LONP1, and HD-5 mRNA in control or ATF5 shRNA HEK 293T cells with or without paraquat (PQ) (n=3, mean +- SEM, *p<0.05).
	0.56	HSP60, mtHSP70, LONP1 and HD-5, a secreted anti-microbial peptide (Figure 2A), consistent with activation of a UPRmt.
	0.55	HSP60, mtHSP70, and LONP1 mRNA in control or ATF5 shRNA HEK 293T cells with or without DeltaOTC expression
22445420	0.96	mtHsp70 and Hsp60, the contribution of each is unclear.
	0.95	Hsp60 and mtHsp70 in order to restore protein homeostasis.
	0.79	Hsp60 or mtHsp70 driving expression of GFP.
22799578	0.96	HSP60, HSP70, mitochondrial heat shock protein 70 (mt-HSP70) and phospholipase C (Table 1).
25215595	0.96	HSPD1), Stress-70 protein (MTHSP75/HSPA9) and lon protease 1 (LONP1) (Table 2 and 3).
26258774	0.96	mtHSP70 and HSPD1.
27677587	0.96	Hsp60 with mtHSP70 emphasizes its critical role in mitochondrial biogenesis.
12082077	0.95	GRP75/mtHSP70, and HSP60), and with another mitochondrial ATP-dependent protease, Yme1.
21616143	0.95	HSP60 and glucose-regulated protein 75 (GRP75) expression in skeletal muscle in middle-aged subjects with impaired glucose tolerance, suggesting a protective role of HSP60, or possibly the UPRmt in glucose metabolism and antioxidative capacity.
24391771	0.95	GRP75 HSPA8 HSPD1, HSPE1 and HSPB1) were up-regulated in HBV(+)/AFB1(+), HBV(+)/AFB1(-) and HBV(-)/AFB1(+) groups, suggesting these proteins not only play a role in HBV-related HCC but also in AFB1-related HCC.
25858032	0.94	mitochondrial HSP70 (mtHSP70), HSP60, HSP56, HSP10, Frataxin, CyPA, CyPB.
	0.94	mtHSP70, HSP60, HSP40, HSP10, ABCB1, and ABCG2.
	0.83	mtHSP70 or HSP60 (Fig. 9C and D).
	0.58	mtHSP70, HSP60, HSP40 and HSP10, and reduced expression of the iron-sulphur regulatory protein Frataxin in glioblastoma tumor cells (Fig. 5).
21437181	0.94	GRP75, HSP60, LRPPRC, and TUFM).
	0.86	GRP75, HSP60, LRPPRC, and TUFM
	0.65	GRP75: 75 kDa glucose-regulated protein; HSP60: Heat shock 60 kDa protein; LRPPRC: Leucine-rich PPR motif-containing protein; MT-CO1: Mitochondrially encoded cytochrome c oxidase I; MTS-GRP75: GRP75 with mitochondrial targeting sequence; TUFM: Elongation factor Tu; VDAC1: Voltage-dependent anion channel 1.
29902206	0.93	HSPA9 (HSP70), HSPB1 (HSP27), HSP90AA1 (HSP90), HSPD1 (HSP60) mRNA from the sample of YTHDF2 knockdown in HepG2 cells (B and C).
	0.90	HSPA9, and HSP60 mRNA showed significant changes, but no differences were observed for HSP90AA1 and HSF1 mRNA.
	0.86	HSPA9, and HSPD1 transcripts were found to have m6A enrichments in both the 5'UTR and 3'UTR.
	0.81	HSPA9, HSPB1, and HSPD1.
	0.52	HSPA9, HSP90AA1, HSPD1, HSF1 transcripts mainly distribute on exons and around stop codons (Fig 6A-6F).
	0.50	HSPA9, HSP90AA1, HSPD1, HSF1, and HSPB1 using m6A-seq in HepG2 cells.
29509794	0.93	Hsp60 and mtHsp70 (Fig 1E) suggesting that the exogenous expression did not cause a significant stress for the cells.
	0.64	Hsp60 and mtHsp70.
31987035	0.92	mtHSP70, HSP60, or even both proteins.
	0.85	GRP75, CH60, and PHB, which are also known as mtHSP70/mortalin, HSP60, and prohibitin, respectively), OXPHOS complex subunits (ATP synthase, complexes I and IV), channel/carrier proteins (TOM/TIM complexes, VDACs), and other mitochondrial enzymes (YMEL1, FAS, ECHA).
	0.84	GRP75 (mtHSP70), CH60 (HSP60), and PHB2 are the main TRAP1 interactors while all other interactors segregate into the second less abundant group (Fig. 4a, inset).
18274801	0.92	HSP 60 (Spot 1), which was upregulated by preload in the preloaded/CsA group, was not upregulated by preload without inhibition of calcineurin.
22357162	0.92	HSPA9, HSPA1L, HSPB1, HSPD1, PSMB1, PSMC2, PSMC4, and PSME1) out of a possible 274 associated with the pathway.
29899330	0.90	Hsp60-mtHsp70 complex and the protein stability/level of Hsp60 and mtHsp70 depends on the level of Lon under oxidative stress.
28499833	0.87	HSP60, mtHSP70) and mitochondrial proteases (LONP1, ClpP) are required for the growth and survival of multiple cancers.
25762445	0.86	HSP60, HSP10 and mtHSP70, and proteases, such as Lon and ClpP. Although this response is regulated by ATFS-1 in C. elegans, a mammalian homologue of ATFS-1 has not yet been identified.
30072094	0.86	HSP60 and mtHSP70 (HSPA9), however the dependence of apoptosis on LON protease activity is currently undefined.
31189611	0.86	HSP60 and GRP-75, coincident with PRODH decay and consistent with mechanistic induction of UPRmt.
31746214	0.82	GRP75), malate dehydrogenase (MDHM), and 60 kDa heat shock protein (Hsp60) have more than 100 self-links.
31097976	0.75	mtHSP70/mortalin, and HSP60 that interact with each other and perform several house-keeping functions.
29954368	0.65	HSPD1 (upregulated in Basal, Luminal B and HER2), SEC63 (upregulated in HER2), TCP1, CCT4, CCT7, CCT8 (upregulated in HER2 and Basal), HSP90AA1 (upregulated with a near 0.9 log2 fold-change in Luminal B, HER2 and Basal), HSPH1 (upregulated in Luminal B, HER2), DNAJA2, HSPA9, HSPA4, DNAJC13, and HSPA8.
	0.58	HSPD1, CCT2, HSPA4, DNAJC6, CCT5, SEC63, HSPH1, CCT8, CCT4, HSP90AA1, HSPA8, DNAJC13, HSPA9 and TCP1) with a poor prognosis (Table 1).
26687188	0.62	Hsp60-immunoreactive signals normalized to mtHsp70 reveals a step-wise increase in Hsp60 protein levels in sAD and fAD, respectively, compared to CTL.
26627475	0.54	mtHSP70 (also known as HSPA9 and mortalin) and HSP60 (also known as HSPD1) and their cofactors and five different AAA+ proteases.