GO:0008240 tripeptidyl-peptidase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0008240 (tripeptidyl-peptidase activity) is a molecular function defined as the catalysis of the release of an N-terminal tripeptide from a polypeptide.
• The two best-characterized human enzymes carrying this activity are tripeptidyl-peptidase 1 (TPP1) and tripeptidyl-peptidase 2 (TPP2), which differ in localization, substrate specificity and regulation.
• TPP1 is a lysosomal serine exopeptidase whose deficiency causes the neurodegenerative lysosomal storage disorder CLN2 disease.
• TPP2 is a large cytosolic/nuclear multi-purpose peptidase that also displays endopeptidase activity and is linked to senescence, calcium/lipid homeostasis and presenile dementia in model systems.
• Altered tripeptidyl-peptidase activity has been detected in malignant pancreatic cysts and in spinal ganglia, indicating roles beyond lysosomal catabolism.
• CRISPR knockout, point-mutation, knock-in and overexpression models are essential to dissect the causal contribution of TPP1 and TPP2 to disease and to validate them as therapeutic targets.
Description
Tripeptidyl-peptidase activity (GO:0008240) is a molecular function that removes a three-amino-acid peptide from the N-terminus of a polypeptide substrate. This exopeptidase activity is distinct from dipeptidyl-peptidase and aminopeptidase activities because it cleaves after the third peptide bond, generating a tripeptide product and a truncated polypeptide. In humans, the function is best represented by tripeptidyl-peptidase 1 (TPP1) and tripeptidyl-peptidase 2 (TPP2), two enzymes with different subcellular localizations and physiological roles. TPP1 is a lysosomal enzyme, whereas TPP2 is a large cytosolic and nuclear peptidase. Because proteolysis is central to protein turnover, antigen presentation and cellular quality control, tripeptidyl-peptidase activity is relevant to a wide range of biomedical research areas, including neurodegeneration, lysosomal biology and cancer. Research on GO:0008240 has accelerated because mutations in the gene encoding TPP1 cause a severe childhood neurodegenerative disease, and because TPP2 has been implicated in aging-related phenotypes and in the regulation of transcription factors and signaling proteins. Histochemical and biochemical studies have also revealed tripeptidyl-peptidase activity in tissues such as porcine lumbar spinal ganglia, suggesting roles in the peripheral nervous system. In addition, increased TPP1 activity has been reported in malignant pancreatic cysts, raising the possibility that this activity could serve as a biomarker or functional marker in oncology. For researchers, GO:0008240 provides a precise functional annotation that can be used to interpret enzyme assays, proteomics datasets and genetic screens. Understanding which proteins carry this activity, how it is regulated, and which substrates it acts on is essential for linking genotype to phenotype in models of lysosomal storage disorders, neurodegeneration and cancer.
tripeptidyl-peptidase activity At A Glance
| GO ID | GO:0008240 |
|---|---|
| GO term | tripeptidyl-peptidase activity |
| Ontology | molecular_function |
| Synonym | none |
| Definition | Catalysis of the release of an N-terminal tripeptide from a polypeptide. |
| Major function | Exopeptidase cleavage of three N-terminal amino acids from polypeptide substrates |
| Representative enzymes | TPP1 (tripeptidyl-peptidase 1) and TPP2 (tripeptidyl-peptidase 2) |
| Subcellular context | Lysosomal (TPP1) and cytosolic/nuclear (TPP2) |
| Disease relevance | CLN2 disease, neurodegeneration, senescence, pancreatic cysts |
What Is GO:0008240?
In our own words, GO:0008240 describes the catalytic activity of an enzyme that cleaves a polypeptide chain specifically after the third amino acid from the N-terminus, releasing a free tripeptide and a shortened polypeptide. This is an exopeptidase activity, meaning it acts at the end of a peptide chain rather than in the middle. The activity is defined by its products and cleavage position, not by a single gene or protein, so multiple enzymes can share this GO annotation.
Why Is tripeptidyl-peptidase activity Important in Cell Biology?
Tripeptidyl-peptidase activity is important because it sits at the interface of protein degradation, cellular quality control and disease. TPP1, the lysosomal enzyme carrying this activity, is directly linked to a fatal neurodegenerative lysosomal storage disorder, and its activity can be measured in patient samples and model systems. TPP2, the cytosolic/nuclear enzyme, has been implicated in the regulation of senescence and in the homeostasis of calcium and lipids in the central nervous system, with its depletion causing presenile dementia in female mice. Beyond these genetic diseases, altered tripeptidyl-peptidase activity has been observed in malignant pancreatic cysts and in spinal ganglia, suggesting broader roles in cancer biology and neurobiology. For researchers, GO:0008240 provides a functional handle to study proteolytic pathways, to interpret omics data, and to design CRISPR-based models that test causality.
• TPP1 deficiency causes a severe lysosomal storage disorder with neurodegeneration, making tripeptidyl-peptidase activity a direct disease-relevant function.
• TPP2 depletion in mice causes presenile dementia through calcium/lipid dyshomeostasis and autophagic degradation of CYP19A1, linking the activity to CNS homeostasis.
• Tripeptidyl-peptidase activity is increased in malignant pancreatic cysts, suggesting a potential biomarker or functional alteration in cancer.
• Histochemical detection of TPP1 activity in porcine lumbar spinal ganglia indicates roles in the peripheral nervous system.
• TPP2 displays endopeptidase activity in addition to tripeptidyl-peptidase activity, expanding its functional repertoire.
• A serpinB2-TPP2 signaling axis has been described during senescence, connecting the activity to aging-related pathways.
• The activity is amenable to biochemical assays, histochemistry and genetic perturbation, making it tractable for mechanistic studies.
• CRISPR-based knockout and knock-in models allow causal testing of TPP1 and TPP2 variants in disease-relevant cell types.
Molecular Mechanism of tripeptidyl-peptidase activity
Substrate recognition and N-terminal tripeptide release
In simple terms: The enzyme grabs the end of a protein chain and cuts off the first three amino acids as a small peptide.
Tripeptidyl-peptidase activity is defined by the release of an N-terminal tripeptide from a polypeptide. The enzyme must recognize the free N-terminus of a substrate and catalyze hydrolysis of the peptide bond after the third residue, generating a tripeptide and a truncated polypeptide. This exopeptidase mode of action distinguishes it from endopeptidases, which cleave internal peptide bonds. The reaction is typically assayed using fluorogenic or chromogenic tripeptide substrates that release a detectable product upon cleavage.
Catalytic mechanism and enzyme classes
In simple terms: Different enzymes can perform the same cut using different chemical tools.
TPP1 is a lysosomal serine protease that belongs to the sedolisin family and uses a catalytic triad to hydrolyze peptide bonds. TPP2 is a large, multi-domain serine peptidase that also exhibits endopeptidase activity in addition to its tripeptidyl-peptidase activity. The endopeptidase activity of TPP2 has been characterized biochemically, showing that the same enzyme can cleave internal peptide bonds under certain conditions. These mechanistic differences mean that GO:0008240 can be carried out by structurally distinct enzymes with different substrate preferences and regulatory features.
Subcellular localization and substrate access
In simple terms: Where the enzyme lives determines which proteins it can cut.
TPP1 is targeted to the lysosome, where it participates in the degradation of proteins delivered by autophagy and endocytosis. TPP2 is predominantly cytosolic and nuclear, giving it access to a different pool of substrates, including signaling proteins and transcription factors. The distinct localizations of TPP1 and TPP2 mean that tripeptidyl-peptidase activity contributes to proteolysis in different cellular compartments and pathways. This compartmentalization is important when interpreting activity assays from whole-cell lysates, because the measured activity may reflect different enzymes depending on the assay conditions.
Regulation by cellular stress and signaling
In simple terms: The cell can tune this activity up or down depending on its state.
TPP2 has been linked to senescence through a serpinB2-TPP2 signaling axis, indicating that its activity or abundance can be modulated during aging-related processes. In models of motoneuron degeneration, trehalose induces autophagy via lysosomal-mediated TFEB activation, a pathway that can influence lysosomal enzymes such as TPP1. TPP2 depletion causes calcium/lipid dyshomeostasis and autophagic degradation of CYP19A1 in the CNS, showing that loss of this activity can trigger compensatory or pathological changes in cellular homeostasis. These observations suggest that tripeptidyl-peptidase activity is not constitutive but is integrated into stress-responsive and metabolic networks.
Physiological and pathological consequences of activity changes
In simple terms: Too much or too little of this activity can harm cells and tissues.
Loss of TPP1 activity causes a lysosomal storage disorder with neurodegeneration, demonstrating that tripeptidyl-peptidase activity is essential for neuronal survival. TPP2 depletion in female mice causes presenile dementia through calcium/lipid dyshomeostasis-induced autophagic degradation of CYP19A1, linking the activity to endocrine and metabolic regulation in the brain. Increased TPP1 activity has been observed in malignant pancreatic cysts, suggesting that upregulation of this activity may accompany certain neoplastic processes. In the peripheral nervous system, TPP1 activity has been detected histochemically in porcine lumbar spinal ganglia, indicating a role in sensory neurons. Together, these findings show that both loss and gain of tripeptidyl-peptidase activity can have significant physiological consequences.
Key Genes Involved in GO:0008240 tripeptidyl-peptidase activity
The following genes and proteins are the principal carriers or regulators of tripeptidyl-peptidase activity (GO:0008240) in human and model systems.
| Gene | Major Role | Research Relevance |
|---|---|---|
| TPP1 | Lysosomal serine exopeptidase that releases N-terminal tripeptides | Mutations cause CLN2 disease; target for lysosomal storage disorder research |
| TPP2 | Cytosolic/nuclear multi-purpose peptidase with tripeptidyl-peptidase and endopeptidase activity | Linked to senescence, calcium/lipid homeostasis and presenile dementia in mice |
| CLN2 | Alternative name for the gene encoding TPP1 | Used in clinical and genetic studies of neuronal ceroid lipofuscinosis |
| SERPINB2 | Serine protease inhibitor implicated in a signaling axis with TPP2 | Studied in senescence and protease regulation |
| TFEB | Transcription factor that promotes lysosomal biogenesis and autophagy | Modulates lysosomal enzyme expression including TPP1 in neurodegeneration models |
| CYP19A1 | Aromatase enzyme involved in estrogen biosynthesis | Its autophagic degradation downstream of TPP2 loss contributes to presenile dementia phenotypes |
| MAP1LC3B | Autophagy marker protein | Used to monitor autophagic flux in TPP2 depletion models |
| SQSTM1 | Autophagy receptor and signaling scaffold | Readout of autophagic degradation in TPP2-related studies |
| LAMP1 | Lysosomal membrane protein | Marker for lysosomal localization of TPP1 |
| CTSB | Lysosomal protease cathepsin B | Often studied alongside TPP1 in lysosomal catabolism |
| CTSD | Lysosomal protease cathepsin D | Context for lysosomal protease networks involving TPP1 |
| BECN1 | Autophagy regulator | Relevant to autophagy-lysosome crosstalk in TPP1/TPP2 models |
| ATG5 | Core autophagy protein | Used to dissect autophagy dependence of phenotypes linked to tripeptidyl-peptidase activity |
| ATG7 | Core autophagy protein | Genetic tool for autophagy studies in TPP2 models |
| MTOR | Kinase that inhibits autophagy | Upstream regulator of lysosomal and autophagic pathways relevant to TPP1/TPP2 |
| XBP1 | Transcription factor in unfolded protein response | Potential link between proteostasis and tripeptidyl-peptidase activity |
| HSPA5 | ER chaperone BiP | Marker of proteostasis stress in models of peptidase dysfunction |
| DDIT3 | Stress-induced transcription factor CHOP | Readout of cellular stress in TPP2 depletion studies |
How Is tripeptidyl-peptidase activity Regulated?
Tripeptidyl-peptidase activity is regulated at multiple levels, including transcription, subcellular localization and post-translational control. The transcription factor TFEB promotes lysosomal biogenesis and can increase expression of lysosomal enzymes such as TPP1, thereby indirectly regulating tripeptidyl-peptidase activity in the lysosome. In the cytosol and nucleus, TPP2 is subject to regulation through protein-protein interactions, including a serpinB2-TPP2 signaling axis that has been implicated in senescence. Loss of TPP2 causes calcium/lipid dyshomeostasis and autophagic degradation of CYP19A1, indicating that the activity is embedded in feedback loops that sense cellular stress and metabolic state. Autophagy pathways, including those controlled by mTOR and ATG proteins, can influence the delivery of substrates to lysosomal TPP1 and the turnover of TPP2-associated factors. Together, these mechanisms ensure that tripeptidyl-peptidase activity is tuned to the physiological state of the cell.
tripeptidyl-peptidase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| TPP1 | Lysosomal storage disorder with neurodegeneration (CLN2 disease) | TPP1 knockout neurons and patient-derived iPSCs |
| TPP2 | Presenile dementia and calcium/lipid dyshomeostasis in female mice | TPP2 knockout mouse models and neuronal cell lines |
| TPP1 | Malignant pancreatic cysts with increased enzyme activity | Pancreatic cancer cell lines and organoids |
| TPP2 | Senescence and aging-related signaling | SerpinB2/TPP2 perturbation in senescent fibroblasts |
| TPP1 | Peripheral nervous system function in spinal ganglia | Porcine or rodent dorsal root ganglia histochemistry |
Neurodegeneration and lysosomal storage disorders
TPP1 is the lysosomal enzyme responsible for a major fraction of tripeptidyl-peptidase activity in neurons, and its deficiency causes a severe neurodegenerative lysosomal storage disorder. In models of motoneuron degeneration, induction of autophagy via TFEB activation can enhance lysosomal function, highlighting the therapeutic potential of modulating this pathway. TPP2 depletion in female mice causes presenile dementia through calcium/lipid dyshomeostasis-induced autophagic degradation of CYP19A1, expanding the neurological relevance of tripeptidyl-peptidase activity beyond the lysosome. These findings establish GO:0008240 as a central node in neurodegenerative disease mechanisms.
Cancer and pancreatic disease
The lysosomal aminopeptidase TPP1 displays increased activity in malignant pancreatic cysts, suggesting that tripeptidyl-peptidase activity may be altered in neoplastic lesions of the pancreas. This observation raises the possibility that TPP1 activity could serve as a functional biomarker or contribute to tumor biology, although the underlying mechanisms require further study. Because TPP1 is a lysosomal enzyme, its increased activity in cysts may reflect changes in lysosomal content or secretory pathways in malignant cells. Research using CRISPR models can help determine whether increased TPP1 activity is causal or a consequence of disease.
Senescence and aging-related phenotypes
A serpinB2-TPP2 signaling axis has been described during senescence, linking tripeptidyl-peptidase activity to aging-related cellular programs. TPP2 depletion in mice causes presenile dementia, indicating that loss of this activity accelerates age-related neurological decline in a sex-dependent manner. These studies suggest that TPP2, and by extension GO:0008240, participates in the regulation of senescence and organismal aging. Understanding how TPP2 activity is controlled during aging may reveal new targets for interventions aimed at preserving neuronal function.
Peripheral nervous system and tissue-specific roles
Histochemical studies have detected TPP1 activity in porcine lumbar spinal ganglia, demonstrating that tripeptidyl-peptidase activity is present in peripheral sensory neurons. This tissue-specific distribution suggests roles in neuropeptide processing or protein turnover in the peripheral nervous system. Comparative studies across species and tissues can reveal conserved and specialized functions of GO:0008240. Such work provides a foundation for understanding how systemic loss of tripeptidyl-peptidase activity affects different neuronal populations.
From tripeptidyl-peptidase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of TPP1 cause lysosomal dysfunction and neurodegeneration? | TPP1 knockout in human iPSC-derived neurons |
| Does TPP2 depletion alter calcium/lipid homeostasis and autophagy? | TPP2 knockout mouse and neuronal cell lines |
| Is increased TPP1 activity causal in pancreatic cysts? | TPP1 overexpression in pancreatic organoids |
| How does a disease-associated point mutation affect TPP1 activity? | CRISPR point-mutation knock-in in cell lines |
| Can tagged TPP1 be used to track lysosomal localization? | Knock-in of fluorescent or epitope tags at the endogenous locus |
| Does TPP2 regulate senescence through serpinB2? | TPP2 knockout and serpinB2 perturbation in senescent cells |
How to Study the tripeptidyl-peptidase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Fluorogenic tripeptide assay | Enzymatic release of tripeptide from substrate | Quantifying TPP1/TPP2 activity in lysates |
| Histochemistry | Spatial distribution of active enzyme in tissue sections | Mapping TPP1 activity in spinal ganglia |
| Immunofluorescence | Subcellular localization of TPP1 or TPP2 | Confirming lysosomal vs cytosolic localization |
| Western blot | Protein abundance and processing of TPP1/TPP2 | Validating knockout or overexpression models |
| RNA-seq | Transcriptional changes after perturbation | Identifying pathways downstream of TPP2 loss |
| Proteomics | Protein abundance and interaction networks | Discovering substrates and partners of TPP1/TPP2 |
| Autophagy flux assay | LC3 turnover and SQSTM1 degradation | Linking tripeptidyl-peptidase activity to autophagy |
| CRISPR screening | Genes required for activity or resistance phenotypes | Identifying modifiers of TPP1/TPP2 function |
Enzymatic activity assays
Tripeptidyl-peptidase activity can be measured using fluorogenic or chromogenic tripeptide substrates that release a detectable product upon cleavage. These assays are used to quantify activity in tissue lysates, cell extracts and body fluids, and have been applied to malignant pancreatic cysts and spinal ganglia. Activity assays are essential for validating the functional impact of CRISPR-generated mutations in TPP1 or TPP2.
Histochemistry and imaging
Histochemical detection of TPP1 activity allows spatial mapping of the enzyme in tissues such as porcine lumbar spinal ganglia. Immunofluorescence and live-cell imaging with tagged enzymes can reveal subcellular localization, for example lysosomal versus cytosolic distribution. These methods complement biochemical assays by providing cellular and tissue context for GO:0008240.
Omics and proteomics
Proteomics and transcriptomics can identify substrates, interaction partners and downstream pathways affected by changes in tripeptidyl-peptidase activity. For example, TPP2 depletion has been linked to autophagic degradation of CYP19A1 and to calcium/lipid dyshomeostasis, which can be monitored by omics approaches. Combining CRISPR perturbation with RNA-seq or proteomics enables unbiased discovery of pathways dependent on GO:0008240.
Autophagy and lysosomal function assays
Because TPP1 and TPP2 intersect with autophagy and lysosomal pathways, standard autophagy flux assays (LC3 turnover, SQSTM1 degradation) are useful readouts. TFEB activation and lysosomal biogenesis can be assessed by imaging and reporter assays in models of motoneuron degeneration. These functional assays help connect tripeptidyl-peptidase activity to cellular quality control.
How CRISPR Can Be Used to Study GO:0008240 tripeptidyl-peptidase activity
Knockout
CRISPR knockout of TPP1 or TPP2 is used to eliminate tripeptidyl-peptidase activity and study the consequences in disease-relevant cell types. TPP2 knockout mice display presenile dementia and calcium/lipid dyshomeostasis, demonstrating the power of complete loss-of-function models. TPP1 knockout in neurons recapitulates key features of lysosomal storage disorders and can be used to test rescue strategies.
Point Mutation
CRISPR point-mutation knock-in allows introduction of disease-associated missense variants into the endogenous TPP1 or TPP2 locus. Such models are essential to distinguish loss-of-function, gain-of-function and hypomorphic alleles, and to measure their impact on enzymatic activity. Point-mutation models also help validate variant pathogenicity in a native genomic context.
Knock-in
Knock-in of fluorescent or epitope tags at the TPP1 or TPP2 locus enables real-time tracking of protein localization and turnover without overexpression artifacts. Tagged knock-in models can be combined with live-cell imaging to study lysosomal targeting of TPP1 or nuclear localization of TPP2. These models are valuable for dissecting the subcellular compartments where GO:0008240 operates.
Overexpression
CRISPR-mediated overexpression or cDNA-based overexpression of TPP1 or TPP2 is used to test gain-of-function phenotypes, such as increased activity in malignant pancreatic cysts. Overexpression models can reveal whether elevated tripeptidyl-peptidase activity is sufficient to drive cellular transformation or metabolic changes. They also provide a system to study substrate processing when enzyme levels are limiting.
How EDITGENE Supports tripeptidyl-peptidase activity Research
Researchers studying tripeptidyl-peptidase activity-related genes often need to determine whether a candidate gene is causally involved in a disease phenotype or whether it merely correlates with it. This requires precise genetic models that can eliminate, modify or tag the endogenous gene in relevant cell types. EDITGENE provides a suite of CRISPR-based services designed to support such studies, from knockout and point-mutation models to knock-in reporters and overexpression systems, as well as library screening and bioinformatics support.
Contact EDITGENE today to design your custom CRISPR model for tripeptidyl-peptidase activity research.
Frequently Asked Questions About tripeptidyl-peptidase activity
What is tripeptidyl-peptidase activity?
Tripeptidyl-peptidase activity (GO:0008240) is a molecular function that catalyzes the release of an N-terminal tripeptide from a polypeptide, acting as an exopeptidase.
What genes are involved in tripeptidyl-peptidase activity?
The main human genes are TPP1, which encodes a lysosomal enzyme, and TPP2, which encodes a cytosolic/nuclear multi-purpose peptidase.
What diseases are linked to tripeptidyl-peptidase activity?
TPP1 deficiency causes a neurodegenerative lysosomal storage disorder, while TPP2 depletion has been linked to presenile dementia and senescence in model systems.
Where does tripeptidyl-peptidase activity occur in the cell?
TPP1 acts in the lysosome, whereas TPP2 is predominantly cytosolic and nuclear, so the activity occurs in multiple compartments.
How is tripeptidyl-peptidase activity measured?
It is commonly measured using fluorogenic or chromogenic tripeptide substrates in tissue lysates or cell extracts, and by histochemistry in tissue sections.
Is tripeptidyl-peptidase activity involved in cancer?
Increased TPP1 activity has been observed in malignant pancreatic cysts, suggesting a possible role in pancreatic disease.
What is the difference between TPP1 and TPP2?
TPP1 is a lysosomal serine exopeptidase, while TPP2 is a large cytosolic/nuclear peptidase that also has endopeptidase activity.
Can CRISPR be used to study tripeptidyl-peptidase activity?
Yes, CRISPR knockout, point-mutation, knock-in and overexpression models are widely used to dissect the functions of TPP1 and TPP2.
What pathways regulate tripeptidyl-peptidase activity?
TFEB-mediated lysosomal biogenesis, autophagy pathways and a serpinB2-TPP2 signaling axis have been implicated in its regulation.
Why is tripeptidyl-peptidase activity important for neurodegeneration research?
Because loss of TPP1 or TPP2 causes severe neurological phenotypes in humans and mice, making this activity central to neurodegenerative disease mechanisms.
Conclusion
Tripeptidyl-peptidase activity (GO:0008240) is a well-defined molecular function carried out by enzymes such as TPP1 and TPP2, with critical roles in lysosomal catabolism, cytosolic proteolysis and cellular stress responses. Its dysfunction is directly linked to neurodegenerative disease, senescence and altered pancreatic biology, making it a high-value target for mechanistic and translational research. By combining precise CRISPR models with biochemical and omics readouts, researchers can determine how tripeptidyl-peptidase activity contributes to health and disease, and whether modulating it can produce therapeutic benefit. EDITGENE supports these efforts with customized knockout, point-mutation, knock-in, overexpression and screening services tailored to TPP1, TPP2 and related pathways.
References
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- 3. Rusmini P et al.. 2019. Trehalose induces autophagy via lysosomal-mediated TFEB activation in models of motoneuron degeneration.. Autophagy 15(4):631-651 PMID: 30335591
- 4. Vodenicharov AP et al.. 2021. Tripeptidyl peptidase I activity in porcine lumbar spinal ganglia - a histochemical study.. Pol J Vet Sci 24(3):409-414 PMID: 34730302
- 5. Ivry SL et al.. 2019. The lysosomal aminopeptidase tripeptidyl peptidase 1 displays increased activity in malignant pancreatic cysts.. Biol Chem 400(12):1629-1638 PMID: 31256057
- 6. Tomkinson B et al.. 2005. Tripeptidyl-peptidase II: a multi-purpose peptidase.. Int J Biochem Cell Biol 37(10):1933-7 PMID: 16125107
- 7. Eklund S et al.. 2012. Characterization of the endopeptidase activity of tripeptidyl-peptidase II.. Biochem Biophys Res Commun 424(3):503-7 PMID: 22771804
- 8. Liao CL et al.. 2022. Unveiling a novel serpinB2-tripeptidyl peptidase II signaling axis during senescence.. J Cell Sci 135(10) PMID: 35466366
