Publication for Ctsb and Ctsl

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Ctsb	cathepsin B	13030			[link]
mmu	Ctsl	cathepsin L	13039

Pubmed ID	Priority	Text
31446224	0.98	CatB and CatL expression in mouse kidney tubular epithelial cells (TECs).
	0.98	CatB, CatL, CatS, and CatK and demonstrated that individual members of this highly related class of cathepsins contributed in opposing manners to TGF-beta signaling, Smad activation, and profibrotic protein production.
	0.98	CatB and CatL in mouse kidney TECs.
	0.98	CatB and CatL in profibrotic protein production (Figure 1), Smad activation (Figure 2), interactions with nuclear membrane Smad transporter proteins (Figure 3), and interactions with plasma membrane TGF-beta receptors (Figure 4) all suggest that these cathepsins contribute differently to tissue fibrosis.
	0.98	CatB and CatL activities but increased CatS and CatK activities, as determined by cathepsin active site labeling with biotinylated-JPM (Figure 5A).
	0.98	Ctsb-/- and Ctsl-/- mice showed greatly enhanced accumulation of these ECM constituents, in contrast to those from Ctss-/-and Ctsk-/- mice.
	0.98	CatB and CatL may mediate TGFBR1 degradation, which could explain the increased TGFBR1 in kidney extracts from Ctsb-/- and Ctsl-/- mice (Figure 7B).
	0.98	Ctsb-/- and Ctsl-/- mice but not in those from Ctss-/-and Ctsk-/- mice (Figure 3B bottom panel), suggesting that only CatB and CatL increased RanBP3 expression, which may increase Smad-2/3 export from the nucleus to cytoplasm, thereby reducing nuclear pSmad-2/3 activity.
	0.98	CatB and CatL exert opposite activities to those of CatS and CatK in controlling TGF-beta signaling and tissue fibrosis.
	0.98	CatB, CatL, CatS, and CatK contribute to tissue fibrosis by regulating TGF-beta signaling and ECM protein expression.
	0.97	CatB or CatL increased the expression of these fibrotic proteins in TECs after TGF-beta stimulation, as compared with TECs from WT control mice.
	0.97	Ctsb-/- and Ctsl-/- mice showed reduced nuclear exporter RanBP3, although CatS- and CatK-deficiency in TECs did not affect RanBP3 expression (Figures 3A and 3B).
	0.97	CatB and CatL remained negligible by immunoblot analysis (Figures 4A and 4B).
	0.97	CatB or CatL, TGF-beta-induced serine phosphorylation on TGFBR1 increased in TECs from Ctsb-/- and Ctsl-/- mice, as determined by TGFBR1 immunoprecipitation followed by anti-p-serine (p-Ser) monoclonal antibody immunoblot analysis.
	0.97	CatB and CatL in interacting with and inhibiting TGFBR1 activation.
	0.97	CatB or CatL activity but increased CatS or CatK activity in UUO-injured kidneys (Figure 5A) suggest their differential roles in post-UUO injury kidney fibrosis.
	0.97	Ctsb-/- and Ctsl-/- mice developed greater tubular dilatation and collagen deposition than WT control mice, yet Ctss-/- and Ctsk-/- mice were protected from post-UUO tubular dilatation and collagen deposition.
	0.97	Ctsb-/- and Ctsl-/- mice.
	0.97	CatB and CatL negatively regulate TGFBR1.
	0.97	CatB and CatL and TGFBR1 may prevent the interaction between TGFBR1 and TGFBR2, another site of interference with downstream signaling.
	0.97	CatB and CatL may facilitate the interaction between the two receptors on the plasma membrane.
	0.97	CatB and CatL inhibited importin-beta expression (Figures 3A and 3B top panel).
	0.97	Ctsb-/- and Ctsl-/- mice and suppressed nuclear pSmad-2/3 in TECs from Ctss-/-and Ctsk-/- mice (Figures 2B-2E).
	0.96	CatB or CatL. Immunofluorescent double staining co-localized these cathepsins to nuclear membrane importin-beta and RanBP3 (Figure S2).
	0.96	CatB and CatL in the proteolysis of importin-beta or RanBP3, but rather formed immunocomplexes with or affected the expression of these nuclear membrane transporters, thereby facilitating pSmad-2/3 translocation by CatS and CatK or reducing pSmad-2/3 translocation by CatB and CatL. Of note, CatS- and CatK-induced TGF-beta signaling may in turn increase the expression of CatS and CatK. CatB- and CatL-reduced TGF-beta signaling may also reduce the expression of CatB and CatL (Figures 1A and 1B).
	0.95	Ctsb-/- and Ctsl-/- mice but reduced nuclear pSmad-2/3 in those from Ctss-/- and Ctsk-/- mice.
	0.94	CatB and CatL inhibited pSmad-2/3 nuclear translocation but that CatS and CatK promoted pSmad-2/3 nuclear translocation.
	0.94	CatB and CatL, interacted with the nuclear membrane importer importin-beta and formed immunocomplexes (Figure 3C).
	0.92	Ctsb-/- and Ctsl-/- mice but decreased expression in TECs from Ctss-/- and Ctsk-/- mice via immunofluorescent staining and immunoblot analysis (Figures 3A and 3B).
	0.92	Ctsb-/- and Ctsl-/- mice and reduced nucleus pSmad-2/3 in TECs from Ctss-/- and Ctsk-/- mice (Figures 2B-2E).
	0.91	CatB or CatL (Figure 3D).
	0.91	Ctsb-/- and Ctsl-/- mice but blunted in kidneys from Ctss-/-and Ctsk-/- mice, as determined by both immunoblot analysis and immunostaining (Figures 7B-7D).
	0.91	CatB and CatL acted differently from CatS and CatK. The interaction between CatB and CatL and TGFBR1 (Figure 4A) reduced TGFBR1 activity (p-Ser) (Figure 4C).
	0.89	CatB in TECs from Ctsl-/- mice or the remaining CatL in TECs from Ctsb-/- mice may bind and activate TGFBR1.
	0.89	CatB and CatL, although CatB and CatL also colocalized to importin-beta and RanBP3 by immunofluorescent double staining (Figure S2).
	0.88	CatB and CatL formed immunocomplexes with the TGFBR1, whereas CatS and CatK preferentially formed immunocomplexes with the TGFBR2.
	0.88	CatB and CatL may further increase TGFBR1 activation, although this study did not test this possibility.
	0.85	CatB and CatL.
	0.53	Ctsl-/- or Ctsb-/- mice may not support this possibility.
28121218	0.98	CTSB and CTSL, causes early pathologies in obese adipose tissue including autophagosome accumulation, enhanced cellular senescence and activated inflammasomes.
	0.98	CTSL and/or CTSB play an important role in autophagy for adipocytes (Fig. S1).
	0.98	Ctsl and Ctsb mRNA was induced through TFEB.
	0.98	CTSL inhibition induces compensatory transcriptional upregulation and enzymatic activation of CTSB in 3T3L1 adipocytes and obese WAT.
	0.98	Ctsl and Ctsb mRNA, pro- and mature proteins in obese WAT, particularly within stromal vascular fractions.
	0.98	CTSB promotes CTSL cleavage, resulting in further suppression of CTSL enzymatic activity.
	0.98	CTSL induces compensatory upregulation of CTSB expression, leading to activation of inflammasomes.
	0.97	CTSL deteriorated autophagic clearance, upregulated expression of CTSB, promoted cellular senescence and activated inflammasomes.
	0.97	CTSL was significantly decreased in obese WAT (Fig. S2D); in contrast, expression of both pro- and mature forms of CTSB was upregulated in obese WAT (Fig. S2A, F and G).
	0.97	CTSL protein and its activity were suppressed, while the activity of CTSB was significantly enhanced in WAT derived from both HFD-induced and genetically obese mice.
	0.97	CTSL to be primarily suppressed in obese WAT, whereby compensatory activation of CTSB expression subsequently occurred in a transcription- and/or post-transcription-dependent manner.
	0.97	CTSB activity, indicating CTSL suppression caused compensatory activation of CTSB (Fig. 4B).
	0.97	CTSL suppressed adipocyte differentiation while inducing autophagosome accumulation and compensatory activation of CTSB.
	0.97	CTSL knockdown promoted senescence-like changes, and complementary activation of CTSB enhanced inflammasome activity.
	0.97	CTSL and CTSB induces senescence-like features and inflammasome activation in 3T3L1 adipocytes.
	0.97	CTSB and CTSL are suppressed.
	0.96	CTSL (cathepsin L) were suppressed in obese adipose tissue, while the activity of CTSB (cathepsin B) was significantly enhanced.
	0.96	CTSB, CTSL and CTSD (cathepsin D) are the most abundant lysosomal proteases.
	0.96	Ctsl and Ctsb mRNA expressions were significantly increased in 4HFD, 8HFD and 18HFD animals (Fig. 3E and I).
	0.96	CTSL inhibition impaired autophagic flux in 3T3L1 adipocytes and enhanced CTSB activity.
	0.96	CTSB upregulation inhibited CTSL activity and CA074ME treatment ameliorated this reduction in enzymatic activity (Fig. 5F).
	0.96	CTSL and CTSB, both of which are ubiquitously expressed, are a cysteine endopeptidase and exopeptidase, respectively.
	0.96	CTSL dysfunction directly caused accumulation of autophagosomes and compensatory activation of CTSB only in vitro using Ctsl knockdown 3T3-L1 cells.
	0.95	CTSL function and compensatory activation of CTSB, caused cellular senescence and inflammasome activation.
	0.95	CTSB in WAT of HFD mice are similar, with the exception of our result indicating that mature CTSL protein is downregulated.
	0.95	CTSL inhibition and compensatory activation of CTSB.
	0.93	Ctsl and Ctsb mRNA expression (Fig. 4F and G).
	0.91	CTSL enzymatic activity appeared to precede upregulation of CTSB expression based on these findings.
	0.88	CTSL- and CTSB-deficient mice have a lifespan of 2 to 4 wk and exhibit early-onset postnatal brain atrophy.
	0.82	CTSL inhibition on CTSB expression in 3T3L1 adipocytes
	0.82	CTSL knockdown promoted complementary activation of CTSB, and CTSB overexpression did not affect autophagic clearance.
	0.82	CTSB, which is synthesized as pro-CTSB (44 kDa) and then subsequently processed into mature CTSB (33 kDa), is far more stable than CTSL under neutral conditions.
	0.75	Ctsl and Ctsb mRNA expression is unlikely to be dependent on TFEB.
	0.69	CTSB-deficient mice do not exhibit a characteristic phenotype, CTSL-deficient mice exhibit skin abnormalities and impaired bone development.
	0.67	CTSL and CTSB are required.
23236527	0.98	CatB, CatL), which have been shown to cleave ZEBOV-GP leading to subsequent exposure of the putative receptor-binding and fusion domain and productive infection.
	0.98	CatB, CatL) cleave the viral glycoprotein (GP) allowing exposure of its core receptor-binding and fusion domain thus facilitating subsequent infection.
	0.98	CatB) and cathepsin L (CatL), which are also present in endosomes, as important factors for ZEBOV entry.
	0.98	CatB and CatL are functionally active.
	0.97	CatB and CatL, and proteolytic processing of GP can also be mediated by other endosomal proteases.
	0.97	CatB- and CatL-independent manner suggesting that other endosomal proteases might functionally replace CatB in virus entry.
	0.97	CatB and CatL, such as in corresponding knockout mice, other endosomal proteases will mediate EBOV-GP cleavage enabling cathepsin-independent EBOV entry into target cells.
	0.95	CatB, but not CatL in cell culture.
	0.95	CatB and/or CatL activity is blocked.
	0.95	CatB and CatL, indicating that both of these cathepsins are not required for ZEBOV replication in vivo.
	0.95	CatB- and CatL-independent.
	0.94	CatB, but not CatL, on ZEBOV entry into cultured cells.
	0.94	CatB- and CatL-dependent was initially described in 2005 by Chandran and colleagues.
	0.94	CatB and CatL dependent uptake of ZEBOV and supports more recent studies showing that only CatB mediates ZEBOV entry into target cells.
	0.94	CatB-dependent but CatL-independent (Fig. 1).
	0.93	CatB, but not CatL, mediates ZEBOV uptake into Vero E6 cells.
	0.92	CatB resulted in significantly reduced virus entry, whereas CatL proteolytic activity did not appear to be obligatory for ZEBOV uptake into Vero E6 cells, although CatL is highly expressed in these cells.
	0.91	CatB or CatL as was EBOV replication in general.
	0.91	CatB- and CatL-independent as we could demonstrate here for a different SEBOV strain (strain Boniface).
	0.90	CatB and CatL-independent.
	0.83	CatB and CatL activity is not required for EBOV replication.
	0.79	catB-/-, catL-/- and control mice in susceptibility to viral infections and the development of immune responses.
	0.75	catB-/- and catL-/- as well as control mice were able to efficiently clear the virus.
	0.75	CatB and CatL are not absolutely required for EBOV replication.
	0.71	catB-/- and catL-/- mice are well characterized and therefore ideal to determine the importance of CatB and CatL for ZEBOV replication in vivo.
	0.68	catB-/- nor the catL-/- mice do possess an increased susceptibility to virus infection.
	0.68	CatB or CatL knockout mice (catB-/- or catL-/-) did not show an increased susceptibility to viral infection in general as determined here with VSV (Fig. 4C,D).
	0.61	CatB, rather than CatL, plays a role in ZEBOV entry.
	0.59	CatB-/- and catL-/- mice succumb to ZEBOV infection
	0.57	catB-/- and catL-/- mice were equally susceptible to lethal challenge with mouse-adapted ZEBOV with no difference in virus replication and time to death.
	0.53	CatB-/- and catL-/- mice succumb to Ebola virus but not to VSV infection.
19900452	0.98	CTSL and CTSB are both localized in the lysosomal as well as the pancreatic secretory compartment and that their colocalization with zymogens further increases during pancreatitis and may even spread to the cytosol.
	0.97	CTSL exhibits a much stronger endoproteolytic activity than CTSB, and could therefore, if it were expressed in the pancreas, be an even more important regulator of protease activation in pancreatitis.
	0.97	CTSB is a trypsinogen-activating enzyme, our data show that CTSL degrades trypsinogen and trypsin.
	0.97	CTSL may therefore indicate that a significant portion of TAP in wild-type animals is generated via the pathway identified above, in which CTSL rapidly generates TAP-IVG and this is subsequently converted to TAP by CTSB.
	0.97	CTSB or autoactivation which prevents further processing of the N terminus by CTSL.
	0.96	CTSL inactivates trypsinogen and counteracts the ability of CTSB to form active trypsin.
	0.96	ctsl gene, which does not affect the pancreas under physiological conditions, has two effects in experimental pancreatitis: 1) it greatly increases intrapancreatic trypsin activity because CTSL is a trypsin(ogen) inactivator and thus an antagonist of CTSB and 2) it greatly reduces the severity of pancreatitis possibly by shifting the cellular effects of pancreatitis towards apoptosis.
	0.96	CTSB and CTSL are widely expressed members of the papain family of cysteine proteinases.
	0.95	CTSL induced cleavage of trypsinogen occurred 3 amino acids toward the C terminus from the CTSB activation site and resulted in a truncated, inactive form of trypsin and an elongated propeptide (TAP).
	0.95	CTSL, the second most abundant cysteine proteinase, shares the same intracellular compartment and confirmed that it possesses a much higher endoproteolytic activity than CTSB.
	0.94	CTSL and CTSB knockout animals, confirmed this fundamental difference between the two lysosomal hydrolases.
	0.94	Ctsl-/- with Ctsb-/- mice results in a lethal phenotype around postnatal day 12 and is caused by significant neuronal cell apoptosis, whereas neither the CTSL nor the CTSB knock-out alone has such an effect.
	0.92	CTSB cleavage of trypsinogen results in active trypsin and immunoreactive TAP, the cleavage by CTSL three amino acids towards the C terminus from the CTSB-processing-site degrades trypsinogen to an inactive degradation product and a non-immunoreactive TAP-IVG peptide.
	0.92	CTSL with the exoproteolytic activity of CTSB.
	0.92	CTSL increased whereas absence of CTSB decreased intra-acinar cell trypsin activity.
	0.90	CTSL cleaves trypsinogen to a lighter protein that corresponds to active trypsin generated by enterokinase (EK) but is processed much more rapidly than by CTSB.
	0.90	CTSL increased and the inhibition of CTSB decreased intra-acinar cell trypsin activity.
	0.89	CTSL as a potent trypsin(ogen)-inactivating factor in vivo and in vitro and thus as an antagonist of CTSB in the digestive protease cascade that triggers pancreatitis.
	0.87	CTSB was confirmed as an activator of trypsinogen and of the intracellular protease cascade, whereas CTSL was identified as its antagonist and a potent inactivator of trypsinogen and trypsin.
	0.86	CTSB-inhibition reduced trypsinogen activation by more than 70% whereas the inhibition of CTSL led to an increased level of active trypsin (+50%).
	0.86	CTSB and CTSL in pancreatic acini
	0.85	CTSB and could also be operative for CTSL because of great similarities between the two lysosomal proteases.
	0.84	CTSB, CTSL was found to very effectively inactivate trypsinogen and trypsin in vivo, in isolated acini, and in vitro.
	0.80	CTSL and subsequently CTSB generates very large amounts of TAP (50% of equimolar enterokinase).
	0.66	CTSL (TAP-IVG or APFDDDDKIVG), that is not immunoreactive in the TAP-ELISA, and exposed it to CTSB it was rapidly converted to TAP (six fold faster compared to the TAP generation from trypsinogen by CTSB).
	0.65	CTSB can be compensated for by CTSL and vice versa.
	0.56	CTSB, in which the cleavage resulted in the generation of trypsin activity (fig.5B) and the formation of TAP (fig.5C), the trypsinogen processing by CTSL resulted neither in active trypsin nor in the generation of TAP.
25255101	0.98	Ctsb) and L (Ctsl) play important roles in Th1/Th2 polarization during L. major infection in both susceptible and resistant mouse strains.
	0.98	Ctsb -/- BMDC display more pro-Th1 properties than their WT and Ctsl -/- counterparts, and therefore suggest that Ctsb down-regulates the Th1 response to L. major.
	0.98	Ctsb-/- BMDC and BMM presented a significant up-regulation of the Th1 promoter cytokine IL-12 in response to L. major and LPS, in comparison with WT and Ctsl-/- cells.
	0.98	Ctsb or Ctsl activities during L. major infection would lead to changes in Th cell polarization due to differences in antigen presentation, our results indicate that Ctsb-/- BMDC up-regulate two of the three types of signals used for instructing Th cell polarization: expression of MHC class II molecules and cytokine expression.
	0.97	Ctsb-/- mice and, to a lesser extent, in BMDC from Ctsl-/- mice in response to L. major compared to WT BMDC (Figure 4A).
	0.97	Ctsb-/- BMDC, on the basis of MHC class II expression, display an enhanced maturation compared to WT and Ctsl-/ - BMDC in response to L. major promastigotes.
	0.97	cathepsin B-deficient mice express higher levels of IL-12 in response to L. major than cells derived from WT and cathepsin L-deficient mice.
	0.97	cathepsin B-deficient mice express higher levels of IL-12 in response to LPS than cells from WT and cathepsin L-deficient mice.
	0.97	Ctsb-selective inhibitor CA074 and the Ctsl-specific inhibitor CLIK148 showed drastic changes in the Th cell response of mice infected with L. major , and it was hypothesized that these effects resulted from differences in antigen processing.
	0.97	Ctsb-/- BMDC than in WT and Ctsl-/- BMDC in response to L. major.
	0.97	Ctsb-/- BMDC were able to express significantly higher levels of IL-12 (both p70 and p40 forms) than WT and Ctsl-/- BMDC in response to L. major promastigotes.
	0.96	Ctsb-/- BMDC in response to L. major in comparison with WT and Ctsl-/- BMDC (Figures 5A and 5B).
	0.96	Ctsb and Ctsl.
	0.95	Ctsb or Ctsl would lead to different patterns for proteolytic processing of L. major antigens.
	0.95	Ctsb-/-)- and cathepsin L (Ctsl-/-)-deficient bone marrow-derived DC (BMDC) and bone marrow-derived macrophages (BMM) to determine the role of these proteases for the signals that DC use to instruct Th cell polarization in response to L. major promastigotes: the expression of MHC class II and co-stimulatory molecules, and the production of cytokines.
	0.95	cathepsin B-deficient mice express higher levels of MHC class II molecules in comparison with BMDC from cathepsin L-deficient and WT mice, but no differences were observed in the expression of co-stimulatory molecules.
	0.95	Ctsb-/- BMDC appeared to be a specific response to living parasites, since stimulation of Ctsb-/- BMDC with LmAg or HK parasites did not result in enhanced expression levels of MHC class II molecules and co-stimulatory molecules in comparison with WT and Ctsl-/- mice (Figure 4).
	0.94	cathepsin B and cathepsin L. The inhibition of cathepsin B resulted in immune-mediated protection, while inhibition of cathepsin L caused susceptibility to the parasite.
	0.93	Ctsb and Ctsl activity could have such effects in Th polarization.
	0.91	Ctsb -/- BMDC express higher levels of MHC class II molecules than wild-type (WT) and Ctsl -/- BMDC, while there were no significant differences in the expression of co-stimulatory molecules between cathepsin-deficient and WT cells.
	0.89	Ctsb -/- and Ctsl -/- mice, and studied the effects of Ctsb and Ctsl deficiency on the survival of L. major in infected cells.
	0.88	Ctsb-/- BMM in comparison with WT and Ctsl-/- BMM (Figures 5D to F).
	0.85	Ctsb-/- and Ctsl-/- mice are able to generate BMDC and BMM with comparable yields and phenotypes as WT mice.
	0.84	Ctsb and Ctsl in the immune response during leishmaniasis.
	0.71	Ctsb-/- BMDC stimulated with LPS did not show a significantly higher expression of MHC class II molecules in comparison with WT BMDC or Ctsl-/- BMDC but they did display higher levels of IL-12.
	0.51	Ctsb-/- and Ctsl-/- BMDC.
32051238	0.98	CPB and CPL.
	0.98	CPB maturation is dependent on the expression of active CPL.
	0.98	CPL, not CPB, is the major protease necessary for the turnover of autophagosomes in the VAC in bradyzoites.
	0.98	CPB in RDeltacpl tachyzoites (Fig. 5B), indicating the accumulation of immature species of these proteases in the absence of CPL expression.
	0.98	CPL, CPB, and ASP1 each are upregulated in chronic-stage bradyzoites compared to acute-stage tachyzoites, which is further supported by our immunoblotting results for CPB and ASP1 in tachyzoites and bradyzoites.
	0.97	CPB was shown to be dependent on another VAC-residing protease, CPL.
	0.97	CPB was observed in DeltacplB1CPL*, confirming that CPL activity is necessary for maturation of CPB in bradyzoites.
	0.97	CPB, ASP1 does not play a major role in the proteolytic turnover of autophagic material in the VAC in bradyzoites, whereas CPL has a dominant role in this activity.
	0.97	CPL is also necessary for the maturation of T. gondii CPB.
	0.97	CPB and CPL colocalize in chronic-stage bradyzoites.
	0.96	CPL for correct maturation, and it resides in the T. gondii VAC, where, similar to CPB, it plays a dispensable role in protein digestion.
	0.96	CPB maturation being dependent on the proteolytic activity of CPL, parasites deficient in CPL will also be deficient in active CPB.
	0.96	CPB and CPL colocalization in tachyzoites, these two proteases were also found to colocalize in bradyzoite cysts (Fig. 3B).
	0.95	CPL and CPB had a profound effect on mouse health, including pronounced neurodegeneration, defects in motility, and, most significantly, lethality 3 weeks after birth.
	0.95	CPB is dependent on expression of CPL, which is consistent with previous findings in a type I strain.
	0.95	CPB maturation depends on CPL activity in bradyzoites.
	0.95	CPL expression is required for maturation of CPB, we reasoned that CPL might also contribute to the maturation of ASP1.
	0.93	CPB), is dependent on CPL, it remained unknown whether these defects result directly from ablation of CPL or indirectly from a lack of CPB maturation.
	0.92	cathepsin L (CPL), cathepsin B (CPB), and cathepsin D (aspartyl protease 1, or ASP1) in its genome.
	0.92	CPL-deficient tachyzoites and bradyzoites is not due to a defect in CPB maturation.
	0.90	CPL, CPB, and ASP1 contribute to bradyzoite viability, we measured the ability of bradyzoites lacking these proteases to invade, differentiate to tachyzoites, and replicate within HFF monolayers, which, if left undisturbed, results in the formation of plaques (Fig. 8A).
	0.83	CPL is a key enzyme in bradyzoites, CPB and ASP1 do not play a substantial role in bradyzoite survival.
	0.81	CPB and indicate that neither CPB nor ASP1 is a major contributor to tachyzoite growth or endolysosomal digestive function, whereas CPL has a dominant role.
	0.73	CPL activity in the maturation of itself and CPB in chronic-stage bradyzoites.
	0.69	CPL-deficient parasites was actually due to a lack of active CPB.
	0.56	CPL-deficient parasites are due to a lack of active CPB.
29500339	0.98	CTSB and CTSL (not CTSD) were implicated in I/R triggered NLRP3 inflammasome activation.
	0.98	CTSB and CTSL are involved in H/R triggered NLRP3 inflammasome activation.
	0.98	CTSB and CTSL activity in kidney were down-regulated by Ca074Me pretreatment (Fig. 6b).
	0.98	CTSB and CTSL activity.
	0.98	CTSL/CTSB activity (Fig. 8).
	0.97	CTSB and CTSL are capable of inducing NLRP3 inflammasome activation.
	0.97	CTSB and CTSL activity.
	0.97	CTSB and CTSL activity.
	0.97	CTSB/CTSL (not CTSD) are involved in I/R-induced NLRP3 inflammasome activation.
	0.96	CTSB, CTSD, and CTSL in whole kidney and in HK-2 cells were significantly decreased by HCQ pretreatment (Fig. 5b).
	0.96	CTSB and CTSL attenuates renal I/R injury and blocks NLRP3 inflammasome activation.
	0.96	CTSB and CTSL.
	0.95	cathepsin (CTS) B, CTSD and CTSL activity, and their redistribution from lysosomes to cytoplasm.
	0.95	CTSB and CTSL-mediated NLRP3 inflammasome activation.
	0.95	CTSB and CTSL activity
	0.95	CTSB and CTSL are essential in H/R-induced cell injury.
	0.95	CTSB and CTSL activity.
	0.94	CTSB and CTSL effectively blocked I/R injury triggered NLRP3 inflammasome activation.
	0.93	CTSB, CTSD, and CTSL siRNA into HK-2 cells to determine which one was responsible for H/R-induced NLRP3 inflammasome activation.
	0.93	CTSB activity in HK-2 cells was selectively inhibited by Ca074Me at low concentrations (<1 mumol/L), and at higher concentrations it inhibited CTSL activity as well (Fig. 6a).
	0.92	CTSB and CTSL are involved in H/R triggered NLRP3 inflammasome activation
	0.91	CTSB and CTSL attenuates renal I/R injury and blocks NLRP3 inflammasome activation
	0.90	CTSB and CTSL activity.
	0.70	CTSB and CTSL activity, we compared the effects of HCQ and Ca074Me on H/R-induced HK-2 cell injury and NLRP3 inflammasome activation.
22244880	0.98	cathepsin L in neuronal media, and both cathepsin L and cathepsin B were demonstrated to be important for increasing LG3 levels after IL-1alpha treatment.
	0.98	cathepsin L levels secreted by neurons and that IL-1alpha mediates increased levels of LG3 through cathepsin L and cathepsin B activity.
	0.98	cathepsin B becomes more involved in LG3 cleavage from perlecan during neuronal exposure to OGD as compared to cathepsin L.
	0.97	cathepsin L activity was seen to be marginally important to generate LG3 during normoxic conditions, cathepsin B activity was found to be important to generate increased levels of LG3 following OGD and reperfusion.
	0.97	cathepsin L and cathepsin B inhibitors decreased LG3 levels increased by IL-1alpha.
	0.97	cathepsin B, but not cathepsin L, is involved in increasing LG3 levels during OGD and reperfusion in FCN.
	0.97	cathepsin L and cathepsin B caused the increase in LG3 levels caused by IL-1alpha exposure in FCN.
	0.96	Cathepsin L and Cathepsin B Specific Inhibitors Cause Decreased LG3 levels Following IL-1alpha but NOT after IL-1beta Treatment
	0.95	cathepsin B and cathepsin L double knockout mice die in infancy and show massive neuronal apoptosis.
	0.93	cathepsin B null mice have normal phenotype, cathepsin L null mice show non-fatal phenotypes such as reduction in major histocompatibility complex (MHC) invariant chain degradation and periodic hair loss.
	0.91	cathepsin B specific inhibitor CA074 were examined due to the redundancy of function between cathepsin L and cathepsin B. Also, we were concerned that the previous work which implicated cathepsin L in the generation of LG3 from apoptotic human umbilical vein endothelial cells used non-specific protease inhibitors that could block the function of both cathepsin L and cathepsin B. CA074 is charged and is unable to penetrate the cell membrane, while its cell permeable methyl ester form has previously been shown to act on other cysteine proteases as well. But, CA074 has previously been shown to be endocytosed such that its concentration inside the cell increases by 12 h of incubation.
	0.90	cathepsin L which generates LG3, but also indicate that IL-1alpha may stimulate perlecan degradation through both cathepsin L and cathepsin B. On the other hand, neither Z-FY-CHO nor CA074 could decrease the levels of LG3 elevated by IL-1beta, indicating that IL-1beta may increase LG3 levels via a non-cathepsin L/B mediated proteolytic mechanism.
	0.82	cathepsin L and cathepsin B inhibitors on LG3 levels in conditioned media of FCN exposed to various stressors.
31357643	0.98	CTSL and CTSB double-deficient mice exhibit postnatal cerebral atrophy and die at 2 to 4 weeks of age, indicating that the mutual interaction of cathepsins in lysosomes maintains lysosomal function.
	0.98	CTSB and CTSL are reduced in primary culture hepatocytes from genetically obese mice.
	0.98	cathepsin L (CTSL) protein, leading to complementary activation of CTSB.
	0.98	cathepsin L (CTSL), CTSB and CTSD.
	0.97	CTSB, CTSL and CTSD are the most abundant cathepsins in tissues.
	0.97	CTSB induced by the downregulation of CTSL in obese WAT.
	0.97	CTSL downregulation leads to complementary CTSB activation that can contribute to obesity-induced inflammation reactions in WAT (Figure 1).
	0.97	CTSB and CTSL in autolysosomes was suppressed in ob/ob mice because of the decreased lysosomal acidification.
	0.96	CTSL and CTSB expressions in WAT are very complicated, likely depending on the degree of obesity status, type of food, timing of tissue sampling, or animal species.
	0.95	CTSL, CTSB and CTSD, as a mechanism of obesity-related lysosomal dysfunction in WAT and liver.
	0.89	CTSL in the epididymal fat depot, but failed to alter the expression of CTSB.
	0.85	CTSB-deficient mice show no obvious phenotype, whereas CTSL-deficient mice display periodic hair loss and bone developmental disorder and develop a progressive dilated cardiomyopathy in the heart.
	0.78	cathepsin B (CTSB), L (CTSL) and many other cathepsins).
28617446	0.98	CTSL and CTSB mRNA were significantly upregulated in 4-week-old Abcb4-/- mice compared with their age-matched wild-type littermates (P=0.02; Figure 1e).
	0.97	CTSL and CTSB mRNA levels (P=0.02) were markedly increased in Abcb4-/- (ATP-binding cassette transporter knockout) mice compared with wild-type littermates.
	0.97	CTSL and CTSB levels were transiently increased during the active phase of biliary fibrosis in Abcb4-/- mice.
	0.97	CTSL and CTSB secreted by hepatic cells may disrupt the bile duct junctions and basement membrane, resulting in concomitant leakage of toxic bile acids into portal spaces, thereby contributing to the pathogenesis of biliary fibrosis in Abcb4-/- mice.
	0.96	CTSL and CTSB expression in different murine models as well as in two independent cohorts of patients with liver fibrosis.
	0.96	CTSL mRNA expression was significantly increased in the liver of CCl4-treated mice while CTSB levels were comparable.
	0.95	CTSL and CTSB mRNA at 4 weeks of age that gradually declined and thereafter reached the basal level at 16 weeks.
	0.92	CTSL and CTSB was further validated in Abcb4-/-mice that spontaneously develop liver injury and morphological features resembling primary sclerosing cholangitis.
	0.91	CTSL and CTSB expression were significantly higher in Abcb4-/- at 4 weeks but gradually decreased to the basal levels by 16 weeks (mean+-s.e.m., n=at least 7 mice in each group).
	0.75	CTSL and CTSB in experimental models, including carbon tetrachloride (CCl4)-induced liver fibrosis and Abcb4-/- knockout mice.
31323747	0.98	cathepsin B (CTSB), cathepsin D (CTSD) and cathepsin L (CTSL) are the crucial lysosomal proteases.
	0.98	CTSB, pro-CTSD and pro-CTSL, suggesting that Lie impaired mitophagy flux by de-maturing the formation of lysosomal cathepsin (p < 0.05) (Figure 3B).
	0.97	cathepsin B (pro-CTSB), pro-cathepsin D (pro-CTSD) and pro-cathepsin L (pro-CTSL), ultimately maintaining the beige adipocytes characteristics in vitro.
	0.97	CTSB, pro-CTSD and pro-CTSL, which subsequently inhibited mitophagy flux, ultimately preventing mitochondria degradation.
	0.97	CTSB, CTSD and CTSL) degradation determines autophagic flux.
	0.97	CTSB, mat-CTSD and mat-CTSL, Lie blocked the degradation of mitochondria in beige adipocytes after Rosi withdrawal.
	0.96	CTSB, pro-CTSD and pro-CTSL, which subsequently inhibited mitophagy flux, and ultimately inhibited the beige adipocytes recovering to white adipocytes and maintained the characteristics of beige adipocyte after stimuli withdrawal.
	0.95	CTSB, pro-CTSD and pro-CTSL, which subsequently inhibited mitophagy flux, ultimately retaining the characteristics of beige adipocytes.
	0.92	CTSB, mat-CTSD and mat-CTSL, Lie blocked mitophagy flux.
30180904	0.98	CatL might be directly involved in lysosomal processing of PGRN into granulins and CatL and CatB cleave and inactivate the secretory leucoprotease inhibitor (SLPI) which protects extracellular PGRN from processing.
	0.98	CatB, CatL and CatS (Fig. 5c, e, g, i).
	0.98	CatB and CatL (Fig. 8).
	0.97	CatB and CatL expression, processing and activity were elevated (Fig. 2h, i, l, m; Additional file 1: Figure S1).
	0.97	CatB, and CatL were increased in total brain of aged Grn-/- mice.
	0.97	CatB, and CatL in the microglia enriched fraction, total brain lysates and MEF of Grn-/- mice.
	0.96	CatB and CatL showed altered maturation (Fig. 3c, e) and a robust increase of in vitro activity (Fig. 3d, f).
	0.95	CatB and CatL are slightly elevated in young Grn-/- mice (Fig. 2f, j) but no significant change in their catalytic activity was observed (Fig. 2g, k).
19551814	0.98	CTSB and CTSL may be involved in trophoblast invasion if, when they are secreted, they reach the extracellular space of the endometrium and are present in an active state.
	0.98	CTSB and CTSL.
	0.98	CTSB and CTSL, which are found in the mouse endometrium during decidualization.
	0.97	cathepsins B (CTSB) and L (CTSL) are C1A clan cysteine cathepsins that play diverse roles in several intracellular compartments; they may also be secreted into the extracellular space.
	0.97	CTSB and CTSL are the trophoblast giant cells.
	0.97	CTSB and CTSL activities in other tissues.
	0.92	CTSB and CTSL.
29187882	0.98	CTSB and CTSL are predominantly localized in the lysosome, but are also commonly secreted in the extracellular environment, where they interact with proteins of the plasma membrane.
	0.98	CTSB and CTSL, which is facilitated by binding to glycosaminoglycans.
	0.97	CTSB or CTSL delayed tumor growth and impaired tumor invasion.
	0.96	CTSB and CTSL overexpression
	0.95	Ctsb or Ctsl reduced neo-angiogenesis in the primary tumors.
	0.91	CTSB and CTSL in tumor progression, there are differences in the effects of these cathepsins in others.
	0.86	CTSB and CTSL influence metastasis formation.
26075905	0.98	cathepsin B and cathepsin L are both necessary, but not individually sufficient, to compensate for the loss of cathepsin S in macrophages.
	0.97	cathepsin B, cathepsin S has been shown to be necessary for efficient presentation of a variety of antigens in DCs and B cells which do not typically express cathepsin L,.
	0.96	cathepsin L, but not mice deficient in cathepsin B or S, had significantly reduced numbers of CD4+ T cells in these lymphoid tissues (Fig 2E, S3 Fig).
	0.92	cathepsin B or S are susceptible to MOG-induced EAE, while mice deficient in cathepsin L are protected from EAE due to a systemic CD4+ T cell deficiency
	0.92	cathepsin B or S are susceptible to MOG35-55 induced EAE while mice deficient in cathepsin L are protected from EAE and have a systemic deficiency of CD4+ T cells.
	0.83	cathepsin L had a significantly reduced clinical score (Fig 2A), 4 fold lower incidence (Fig 2B), and a five day delay (Fig 2C) when compared to WT and cathepsin B or S deficient mice.
23884585	0.98	cathepsin B or cathepsin L leads to an initial cleavage of sigma3 most likely near the C-terminus of the protein.
	0.97	cathepsin L or cathepsin B is required for reovirus entry into murine fibroblasts and indicate that cathepsin L is the primary mediator of reovirus disassembly in these cells.
	0.96	cathepsin B and cathepsin L activity completely abrogates disassembly and growth of reovirus.
	0.96	cathepsin B and cathepsin L are capable of ISVP formation in other types of cells.
	0.95	cathepsin L mediates reovirus disassembly more efficiently than cathepsin B in vitro.
28126413	0.98	cathepsin L in the cytosol, a surrogate measure for leaked cathepsin B, which was associated with less NLRP3 inflammasome activity.
	0.97	cathepsin B, and possibly cathepsin L, in activating the NLRP3 inflammasome after LMP in vitro.
	0.95	cathepsin B and partial specificity to cathepsin L, and CA-074-Me inhibition of cathepsin L is increased in reducing conditions.
	0.65	cathepsin B and L. However, cathepsin B and or cathepsin L may have marginal or indirect roles in LMP with silica exposure.
24902901	0.98	cathepsin L positive vesicles did not contain cathepsin B (Figures 2b and Supplementary figure 2) suggesting that there may be an alternative transport system that delivers cathepsin L to discrete vesicles.
	0.95	cathepsin B, which shows a modest 4-fold increase at the onset of involution ( and Figure 3d), cathepsin L shows a striking induction within 24h involution, as shown by immunofluorescence staining and a corresponding 22-fold induction at the mRNA level (Figure 2a and 3d) and .
	0.92	cathepsin L at 24h and 48h involution in p55alpha-/-/p50alpha-/- glands when compared with controls, as opposed to unchanged cathepsin B activity shown by subcellular fractionation and subsequent cathepsin activity measurement.
25601403	0.98	cathepsin B (CtsB) and CtsL (Fig. 1 A), and a complete loss of immunoreactive CtsZ and CtsS were observed (Fig. 1 B).
	0.87	CtsB and CtsL (~20% of WT), and CtsZ immunoreactivity was still detectable (Fig. 1, D and E).
	0.84	CtsB, CtsL, betaHex, betaGal, alphaFuc, and alphaMan in extracts of B cell blasts.
17765022	0.98	cathepsin B-/- mice and cathepsin L-/- mice was in part attributed to maintenance of E-cadherin protein levels.
	0.97	cathepsin B-/- cells to TNF-alpha-triggered apoptosis, cathepsin L-deficient lung carcinoma cells showed increased sensitivity to apoptosis which is in agreement with increased tumor cell death in the mouse model of multistage pancreatic tumorigenesis after deletion of cathepsin L. Increased apoptosis in the absence of cathepsin L could be rescued by inhibition of the aspartic protease cathepsin D whose single-chain isoform was subsequently shown to be specifically degraded by cathepsin L. Therefore, it was proposed that cathepsin L contributes to control death receptor-induced apoptosis via proteolysis of cathepsin D.
23152408	0.98	cathepsin B- and cathepsin L-deficient mice have significantly increased protein levels of collagen IV in their intestine compared with WT animals.
	0.97	cathepsin B (A), cathepsin L (B), and cathepsin X (C) were significantly elevated in the colon of Ctsk-/- mice when compared with WT controls.
30559339	0.98	CtsB, CtsL, CtsD and CtsH (Fig. 6e and Supplementary Fig. 7) consistent with an increase in protease activity levels (Fig. 6g).
	0.98	CtsB and CtsL and increased uptake of milk fat globules which, upon hydrolysis, released lysosome-permeabilising unsaturated fatty acids which were essential for the induction of LM-PCD.
27626662	0.98	CtsB, CtsL, CtsS and CtsZ (Supplemental Fig. S2B).
24170975	0.97	cathepsin B, cathepsin L, and especially cathepsin D, as well as MMP activity, increased several-fold in heart tissue (Korolenko et al.,).
	0.95	cathepsin B, cathepsin L, and cathepsin D was significantly increased 1 month after P-407 administration and attained even greater levels at 4 months (Korolenko et al.,).
	0.94	cathepsin B and cathepsin L was shown to increase significantly (p<0.01) at the 24 h time point when compared to controls (Table 1).
	0.91	cathepsin B and cathepsin L) in heart and liver, and especially, of aspartate protease cathepsin D in heart tissue without significant changes in MMP activity.
	0.90	cathepsin L is contrary to that of the cysteine protease cathepsin B (Brix et al.,).
	0.89	cathepsin B and cathepsin L (at 24 h) and aspartate protease cathepsin D (at both 24 h and 5 days) was determined in heart tissue following P-407 administration.
	0.88	cathepsin B and cathepsin L in liver tissue relative to the control at both 24 h and 5 days following the last P-407 injection (Table 1).
	0.85	cathepsin B, cathepsin L, and cathepsin D, relative to heart tissue.
25744631	0.97	cathepsin B (Ctsb) and cathepsin L (Ctsl), to cancer progression and metastasis.
	0.97	Ctsb and Ctsl could partially be explained by compensational transcriptional upregulation upon their inhibition (Figure 6E).
	0.96	Ctsb, Ctsl, and Ctsd , acid ceramidase, lysosomal alpha glucosidase, and bleomycin hydrolase) and lysosomal membrane proteins (i.e. lysosome associated membrane protein (Lamp) 1-3, Niemann-Pick C1 and C2 protein, and V-type ATPase).
	0.83	Ctsl but not Ctsb activity in both cell lines (Figure 1D).
	0.83	Ctsb and Ctsl in cells treated with TGFbeta-1 + E64d was confirmed by Western blot and was also found in cells treated with E64d alone (Figure 6B).
28835281	0.97	cathepsin B and L have minimal ability to process PGRN (Fig. 3a, b) despite cathepsin B being minorly active towards PGRN in vitro (Fig. 3d), indicating that cathepsin B is not the enzyme directly processing PGRN in cathepsin L - deficient MEFs.
	0.96	cathepsin B is responsible for processing PGRN in the absence of cathepsin L.
	0.87	cathepsin B and D were capable of cleaving PGRN to a minor degree, incubation of recombinant PGRN with cathepsin L led to the generation of bands of approximately 10 kDa, corresponding to the size of granulin peptides (Fig. 3c, d).
	0.84	cathepsin L, K or Z had no effect on PGRN processing, while ablation of either cathepsin B or D resulted in ~50% reduction in the ratio of processed PGRN peptides versus full-length PGRN (Fig. 3a and b).
29079517	0.97	CTSB-/- mice while it was increased in macrophages from CTSL-/- mice (Figure 3D), which is in accordance with the counteracting role of CTSL to CTSB.
	0.95	CTSB or CTSL-deficient macrophages showed significantly decreased trypsin activity in CTSB-deleted macrophages and increased activity in CTSL-deleted cells (D).
	0.92	CTSB-dependent manner within phagocytosing macrophages came from experiments using CTSB- and CTSL-deleted mouse macrophages incubated with bovine trypsinogen.
31077130	0.97	Ctsb and Ctsl (p <= 0.05) at 24 hpi in JAWS II cells (Fig. 3a).
	0.96	Ctsb, Ctsl and Ctss in peritoneal macrophages isolated from BALB/c and C57BL/6 mice.
	0.68	Ctsb, Ctsl and Ctss expression (Fig. 2b) and reduced level of cathepsin L (Fig. 3b).
29169406	0.97	cathepsin L and cathepsin B clearly demonstrated a brain-specific phenotype, such as neuronal death in the cerebral cortex and cerebellum, an increase in hypertrophic astrocytes, and axonal degeneration, which resulted in death in infancy.
	0.75	cathepsin L and cathepsin B might be necessary for brain development, the specific role of extracellular cathepsin L on neurons remains to be elucidated.
31959889	0.97	CTSB caused by the downregulation of CTSL enhanced inflammasome activation, leading to inflammatory responses in obese WAT.
	0.61	cathepsin B (CTSB), and cathepsin L (CTSL), CTSB, CTSL and CTSD are the most abundant lysosomal proteases.
19924255	0.97	ctsB and ctsL, we observed that both C57BL/6Nlrp1b(129S1) BMDMs and RAW 264.7 cells were protected from LT (Figure 3A and 3B).
21767668	0.97	cathepsin B, cathepsin L or IL-1beta.
21897848	0.97	Ctsb and cathepsin L (Ctsl) double KO mice exhibit severe brain damage, with neuronal loss and brain atrophy, underscoring the important role of Ctsb in brain physiology.
22163006	0.97	cathepsin B- and cathepsin L-dependent necrosis.
25866783	0.97	cathepsin B inhibitor or cathepsin L inhibitor in the tumor cells, regardless of susceptibility to reovirus.
29088746	0.97	cathepsin B, asparaginyl endopeptidase (legumain)) to sub-pM (cathepsin L) affinity.
32093427	0.97	CATB activity among others cathepsins (CATK and CATL) in cortex tissue, showed that the specific CATB inhibitor Ca074-ME at 100 nM (three-fold higher than its IC50) was able to suppress the majority of total cathepsin activity against Z-Phe-Arg-AMC in tissues from both Idua +/+ (~90% reduction) and Idua -/- mice (~80% reduction), indicating that CATB is the most prominent Z-Phe-Arg-converting enzyme in the mouse cortex (Figure 2B).
28596234	0.96	CtsB is a ubiquitously expressed cysteine protease, belonging to the papain family, similar to CtsL. It has been shown to act as a dominant protease in cellular apoptosis and senescence and to play a role in lysosomal cathepsin-dependent apoptosis pathways.
	0.96	CtsL ablation on proteins important for mouse skin biology corresponds to the fact that CtsL-deficient mice show an overt skin phenotype, while CtsB-deficient mice do not.
	0.84	CtsB and CtsL are essential for HF maintenance.
	0.56	CtsL-deficient mice are known for their prominent periodic hair loss phenotype, manifesting together with epidermal hyperplasia, acanthosis, and hyperkeratosis, CtsB-deficient mice do not display any obvious skin or fur phenotype.
23667900	0.96	cathepsin B knockout and cathepsin L knockout mice are both viable, the double knockout of cathepsins B and L is lethal, thus supporting functional redundancy of the two proteases.
	0.95	cathepsin B increases proliferation and progression of these tumors in part by negatively regulating the levels of active cathepsin L. Although a reduction in cathepsin B activity has been associated with increased apoptosis, others have shown that cathepsin B induces apoptosis (; for a general review on lysosomal cathepsins and cell death, see).
	0.94	cathepsin B leads to increases in the levels of active cathepsin L. Thus, the interactions between these two cysteine cathepsins may regulate the proliferation of tumors.
19781728	0.96	cathepsin L is required for the Eco-MLV infection in the cathepsin B-undetectable NIH3T3 cells, but not in cathepsin B-expressing cells.
	0.61	cathepsin L mRNA, but not the cathepsin B mRNA.
23516607	0.96	cathepsin L-, but not cathepsin B-deficient mice was largely suppressed, compared with wt mice.
	0.94	cathepsin B, L or D. Our data showed that processing from the 30-kDa form to the 23-kDa form is dependent, at least in part, on cathepsin L, a cysteine proteinase in the liver.
24591744	0.96	cathepsin B, cathepsin C and cathepsin L) and positive (cathepsin H) role of cathepsins in aspergillosis but also prove the role of cytokines in remodelling of immune response.
	0.95	cathepsin B, cathepsin C and cathepsin L); and increase in interferon gamma and cathepsin H levels in the mice treated with antifungal compounds were observed.
31235832	0.96	CTSL, which is expected to further enhance CTSB-mediated activation in the acinar cell.
	0.70	CTSB, the other major lysosomal cysteine protease CTSL does not activate trypsinogen.
21794126	0.96	cathepsin L is significantly upregulated, as well as in the brain of Ctsd-/- mice, where elevated levels of cathepsin B have been detected.
27345423	0.95	CTSB and CTSL reduced hippocampal Bdnf expression.
	0.90	CTSB, but not CTSL (Felbor et al., 2012), levels increased after 4 months of exercise and were positively correlated with fitness levels.
	0.89	CTSB and Cathepsin L (CTSL) there is brain atrophy.
27997605	0.95	cathepsin B (Fig 1A) and cathepsin L (Fig 1B).
	0.95	cathepsin B (Fig 2A) and cathepsin L (Fig 2B).
17488522	0.95	Cathepsin L, although less well studied than cathepsin B, has been linked to tumor invasion and metastasis.
19664906	0.94	Ctsl-/- mice are protected from type 1 diabetes (IDDM), and demonstrated a significant reduction in IDDM incidence for Ctss-/- and Ctsb-/- NOD mice.
	0.94	Cathepsin B, or Cathepsin L offers protection from type I diabetes mellitus development on the NOD background.
	0.86	Ctsl, Ctss, or Ctsb heterozygous mice were able to develop IDDM, although incidence levels were significantly lower for Ctsb+/- (50%) and Ctsl+/- (55%) as compared to NODs (69%; p<0.03).
	0.77	Ctsl-deficient NOD mice, the roles of Ctsb and Ctss in autoimmune diabetes deserve further examination.
	0.68	Cathepsin B led to a decrease in diabetes incidence, whereas deficiency in Cathepsin L provided complete resistance to the disease.
	0.50	Ctsb+/- and Ctsl+/- showed modest but significantly reduced values as compared with NOD mice (50% [p=0.0061] and 55% [p=0.035], respectively) (Figure 1A).
31092553	0.94	CtsB, CtsL, and asparagine endopeptidase.
	0.92	CtsB or CtsL, a loss in activity for one could be rescued by the other, because of a shared substrate site, cutting alpha-synf at Asn-122/Glu-123 to generate the peptide fragment 1-122.
	0.67	cathepsins B (CtsB), L (CtsL), and AEP can generate these peptides, with the majority attributable to cysteine cathepsins.
29615904	0.94	cathepsin B activity and the amount of cathepsin L were only mildly diminished in the taar1-/- thyroids vs. WT, but higher cystatin levels prevailed, we conclude that Taar1 deficiency might have limited effects on the expression of thyrocyte-typical genes, but might rather affect proteostasis, resulting in altered balances of proteolytic to anti-proteolytic activities in taar1-/- vs. WT controls.
	0.86	cathepsin B activity and smaller amounts of cathepsin L were observed in taar1-/- follicles (Table 2).
28546539	0.94	cathepsin B activity and the increase of cathepsin L activity.
21925292	0.93	cathepsin L for producing active peptides for neurotransmission and of the key role of cathepsin B for production of Abeta involved in the development of Alzheimer's disease.
	0.87	Cathepsin L Generates Peptide Neurotransmitters and Cathepsin B Produces Beta-Amyloid of Alzheimer's Disease
20877570	0.92	CatL-inh protected diabetes-prone NOD mice from subsequently occurring diabetes such as high blood sugar and urine sugar while there was no therapeutic effect of cathepsin B inhibitor (CatB-inh) and cathepsin S inhibitor (CatS-inh) (Figure 1A, B).
9151667	0.89	cathepsin L contained cathepsin B labeling at only low levels (Fig. 11 C).
18957203	0.88	Cathepsin B upon in vivo chemical inhibition of Cathepsin L, nor do we observe the same pattern of H3 cleavage with recombinant Cathepsin B compared to Cathepsin L in vitro, we cannot exclude the possibility that redundancy in H3 cleavage function may exist between these or other related enzymes at other stages or lineages of differentiation.
	0.79	Cathepsin L/Cathepsin B double knockout mice exhibit severe brain atrophy and die two to four weeks after birth.
	0.52	Cathepsin B levels between those cells treated with Cathepsin L Inhibitor I and control cells suggests that the inhibitor is indeed specific for Cathepsin L. Markers of cell lineage were also analyzed by Q-PCR, and suggest modest changes in neural/ectodermal expression patterns and levels of endodermal marker expression between inhibitor treated and control cells (Supplemental Figure S8).
18820745	0.88	cathepsin B and cathepsin L (brucipain) in the pathogenesis of Trypansoma brucei brucei in both an in vivo mouse model and an in vitro model of the blood-brain barrier.
25122166	0.87	cathepsin L or cathepsin B family, eliciting high activation of the immune response.
26195813	0.87	cathepsin L. However, cathepsin B-/-, L-/- or B&L-/- PMs showed no attenuation of IL-1beta secretion in response to the lysosome-disrupting agent Leu-Leu-OMe (LLOMe), silica, nigericin or dAdT (Fig. 4a).
18604209	0.86	cathepsin B inhibited microglial IL-1beta release in a dose-dependent way (Fig. 4b), whereas inhibitors of cathepsin D and cathepsin L had no effect (Fig. 4b).
22798952	0.84	Cathepsin B is networking with other proteases as it was shown for cathepsin X/Z. In contrast, deletion of cathepsin L was beneficial in the RiP1-Tag2 model, but enhanced tumorigenesis in the APCmin, and the K14-HPV16 mice.
24474939	0.83	cathepsin B activates trypsinogen, forming trypsin, whereas cathepsin L degrades both trypsin and trypsinogen.
31932607	0.82	Ctsb and Ctsl (Fig. 4g, h).
30655525	0.80	CTSB-/-, and CTSL-/- mice were equally susceptible to lethal challenge with mouse-adapted EBOV.
26984939	0.75	cathepsin B and cathepsin L in live cardiomyocytes examined by FACS.
	0.59	cathepsin B and cathepsin L, two important lysosomal enzymes, using substrate-based assays.
21944884	0.58	cathepsin B (CtsB), cathepsin D (CtsD), cathepsin L (CtsL), and the MMP-activating enzyme urokinase plasminogen activator (uPA) were also significantly elevated, although the magnitude was not as high.