Publication for Hspa9 and Lonp1

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Hspa9	heat shock protein 9	15526			[link]
mmu	Lonp1	lon peptidase 1, mitochondrial	74142

Pubmed ID	Priority	Text
30822691	0.99	Lon, a mitochondrial matrix protein, stabilizes the complex of HSP60-mtHSP70-Lon that leads to the sequestration of HSP60 in mitochondria.
12082077	0.98	Lon and GRP75/mtHSP70 under ER stress (Fig. 4 D).
23201123	0.98	LONP1, K378), and the chaperone proteins, 100 kDa chaperone (CLPX, K127), heat shock protein 70 (HSPA9, K653), 10 kDa heat shock protein (HSPE1, K36).
23593476	0.98	mtHsp70, mtHsp40) and mitochondrial proteases (LONP1, ClpP, YME1L1, AFG3L2), were up-regulated in SMS1-KO WAT (Fig. 4B, Table S1).
25543897	0.98	mtHsp70, ClpP, Lonp1 and Ubl5 form a tight coexpression network in mice GRPs and human populations, suggestive of their transcriptional control.
26833085	0.98	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).
31358769	0.98	Lonp1, Clpp, and Hspa9), ATF4-mediated stress pathways (Atf4, Ddit3, Asns, Chac1, Pck2, and Trib3), along with genes involved in de novo serine/glycine synthesis pathways (Phgdh, Psat1, Shmt2) (Supplementary Fig. 10e).
32010709	0.98	HSPA9, LonP1, and YME1L.
32302062	0.98	mtHSP70, in mouse embryonic fibroblasts during inhibition of matrix chaperone TRAP1, protease Lon, or electron transfer complex 1 activity.
28433661	0.97	GRP75, 75 kDa glucose-regulated protein), presequence protease, lon protease, HSP 60, and MPP, which proteins mediates mitochondrial protein translocation and folding.
	0.91	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
31903419	0.97	LONP1 and AFG3L2, and the chaperone mtHSP70 in the Mtif3 knockout mice indicate an imbalance in the OXPHOS polypeptides and are a consequence of the impaired assembly of the OXPHOS system.