The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Scope and identity verification. This report concerns human ENPP5 (UniProt Q9UJA9), also called NPP5, an ectonucleotide pyrophosphatase/phosphodiesterase (ENPP) family member and “among the least characterized ENPP family members.” (gorelik2017akeytyrosine pages 1-4, borza2022structureandfunction pages 8-9). The functional inferences and evidence below are restricted to this target and to Homo sapiens unless explicitly stated.
The ENPP family (ENPP1–7) comprises ecto-enzymes within the alkaline phosphatase superfamily that participate in extracellular metabolism of nucleotide and lipid-like substrates, thereby shaping purinergic and related signaling. ENPP5 stands out because it shows little to no activity on many “typical” ENPP substrates and common nucleotides but has detectable activity on a more restricted set of sugar-containing nucleotides and NAD. (gorelik2017akeytyrosine pages 1-4, gorelik2017akeytyrosine pages 4-7, borza2022structureandfunction pages 8-9).
A recent authoritative review (Journal of Biological Chemistry, 2022; Borza et al.) summarizes ENPP5 as showing “no activity toward many known ENPP substrates but, instead, cleaves nicotinamide adenine dinucleotide (NAD),” leading to a hypothesis that ENPP5 might participate in NAD-based neurotransmission, though this requires genetic validation (e.g., KO models). (borza2022structureandfunction pages 8-9).
Human ENPP5 is described as an extracellular, membrane-anchored ectoenzyme with type I transmembrane topology: an N-terminal signal peptide and a C-terminal transmembrane helix plus a short cytoplasmic tail. Recombinant constructs used for biochemical/structural work typically remove the membrane anchor (e.g., residues ~25–430) to produce soluble ectodomain protein. (gorelik2017akeytyrosine pages 1-4, gorelik2017akeytyrosine pages 7-10, gorelik2017akeytyrosine pages 4-7).
Implication: ENPP5’s enzymatic action is expected to occur at the cell surface / extracellular milieu, where it can modulate extracellular nucleotide-like metabolites in a local microenvironment (e.g., synaptic clefts). (gorelik2017akeytyrosine pages 7-10, gorelik2017akeytyrosine pages 4-7).
ENPP5 belongs to the ENPP subgroup within the alkaline phosphatase superfamily and uses Zn2+-dependent catalysis. Structural work indicates ENPP5 contains the canonical binuclear zinc catalytic center plus an ENPP5-specific third Zn2+ (Zn3) near the active site. This third Zn is coordinated by residues including Glu159 and Asp192, and is positioned to interact with the ribose 2′/3′ oxygens of substrates. (gorelik2017akeytyrosine pages 7-10, gorelik2017akeytyrosine pages 4-7, borza2022structureandfunction pages 7-8).
A key mechanistic conclusion is that ENPP5’s unusual substrate profile is strongly influenced by a residue in the nucleotide-binding slot: a Tyr in ENPP5 where other ENPPs often have Phe. (gorelik2017akeytyrosine pages 1-4, randriamihaja2017structuralanalysesofa pages 49-55, borza2022structureandfunction pages 7-8).
ENPP5 is characterized as an ecto-nucleotide pyrophosphatase/phosphodiesterase that can hydrolyze phosphodiester/pyrophosphate bonds in selected extracellular nucleotide-like substrates. The strongest experimental evidence indicates wild-type ENPP5 preferentially cleaves NAD and can also cleave ADP-ribose (ADPR) and UDP-glucose (UDPG), whereas it has minimal/undetectable activity on canonical nucleotide triphosphates/diphosphates under tested conditions. (gorelik2017akeytyrosine pages 4-7, borza2022structureandfunction pages 7-8, borza2022structureandfunction pages 8-9).
Independent experimental work reports that wild-type human ENPP5 does not hydrolyze ATP, ADP, or UTP detectably in assays measuring phosphate release (“close to 0 μM”), in stark contrast to ENPP3 activity on these nucleotides. (randriamihaja2017structuralanalysesofa pages 49-55, randriamihaja2017structuralanalysesof pages 49-55).
A detailed FEBS Journal paper (Gorelik et al., Sep 2017; https://doi.org/10.1111/febs.14266) reports that ENPP5 is inactive against several “typical” NPP substrates (e.g., p-nitrophenyl-TMP) and also does not cleave tested phospholipids/related compounds, but does cleave NAD and shows activity on certain sugar-containing/atypical nucleotide substrates. (gorelik2017akeytyrosine pages 1-4, gorelik2017akeytyrosine pages 4-7).
The same work provides biochemical context suggesting that although ENPP5 has higher activity on NAD than on other tested nucleotides, its affinity is low (KM > 1 mM), implying any physiological relevance would likely occur where local NAD could become transiently high (e.g., restricted extracellular microenvironments), rather than in plasma. (gorelik2017akeytyrosine pages 7-10).
A high-level quantitative summary in the JBC 2022 ENPP review reports that ENPP5’s highest catalytic rate was observed on NAD+/NADH, but the catalytic efficiency for NAD+ is very low (0.00067 s−1 μM−1). (borza2022structureandfunction pages 7-8).
Two complementary studies converge on a key structural determinant:
This is a strong mechanistic anchor for functional annotation: ENPP5 is not a general ATPase like ENPP1/ENPP3; instead, its substrate range is constrained by a specific “gatekeeper” residue in the nucleobase binding region. (gorelik2017akeytyrosine pages 4-7, borza2022structureandfunction pages 7-8).
Because ENPP5 is membrane-anchored with an extracellular catalytic ectodomain, its expected role is in extracellular nucleotide/NAD metabolite processing. (gorelik2017akeytyrosine pages 1-4, gorelik2017akeytyrosine pages 4-7).
A practical enabling resource for localization/expression studies is the production of antibodies recognizing native conformations of purinergic signaling components, including ENPP5; these reagents were developed to monitor cell surface expression of ENPP family proteins in native conformation. (randriamihaja2017structuralanalysesof pages 49-55).
The ENPP family is part of the extracellular nucleotide metabolism machinery that modulates purinergic signaling. ENPP5 has been proposed (based on its NAD-cleaving activity) to potentially contribute to NAD-based neurotransmission, but this remains a hypothesis in need of in vivo genetic validation (e.g., Enpp5 knockout studies). (borza2022structureandfunction pages 8-9).
Gorelik et al. report high-resolution structures of ENPP5 (murine and human) and provide PDB identifiers: 5VEM, 5VEN, 5VEO. (gorelik2017akeytyrosine pages 1-4).
Key structural features relevant to function include:
The FEBS Journal study includes figures that directly depict (i) ENPP5 active site Zn organization (including Zn3), (ii) Tyr73 positioning, and (iii) relative enzymatic activity on substrates including NAD versus others and wild-type versus Y73F mutant. (gorelik2017akeytyrosine media 261ec884, gorelik2017akeytyrosine media 7d676195, gorelik2017akeytyrosine media 4e0a41b5).
ENPP5 remains relatively under-characterized mechanistically, so much of the 2023–2024 literature is review-level or omics/correlation-level, rather than direct enzymology.
A 2024 review on aging, senescence, and skin wound healing states that ENPP5 was reported as a “key factor” in senescence in dermal fibroblasts and that knockdown of ENPP5 retarded senescence via modulation of apoptosis-inducing proteins. (o’reilly2024agingsenescenceand pages 6-7). This is suggestive but not yet definitive for biochemical function; it motivates targeted mechanistic studies linking ENPP5 catalytic activity (or non-catalytic roles) to senescence pathways.
A large plasma proteomics study of frailty (Aging Cell, Aug 2020; https://doi.org/10.1111/acel.13193) reports ENPP5 (Q9UJA9) as negatively associated with frailty with estimate −0.0713, SE 0.0102, p = 6.83×10−12 (among many proteins tested). (sathyan2020plasmaproteomicprofile pages 5-7). This supports ENPP5’s detectability in plasma proteomic platforms and suggests utility in biomarker modeling, though it does not resolve mechanism.
A 2024 Research Square preprint on soluble biomarkers in long COVID is present in the retrieved corpus; however, the excerpt retrieved here does not include the specific ENPP5 statistics beyond bibliographic/context pages. Thus, ENPP5’s role there cannot be quantified from the available extracted text in this run. (buggert2024identificationofsoluble pages 20-23).
An in-silico ADC target study (PLOS ONE, Aug 26 2024; https://doi.org/10.1371/journal.pone.0308604) is present in the retrieved set, but the excerpt available here does not include ENPP5-specific validation details. Therefore, ENPP5 should be considered a hypothesis-level candidate in that context based on this run’s evidence. (kathad2024expandingtherepertoire pages 14-16).
Open Targets lists low-evidence disease associations for ENPP5 (each with 3 evidence items in the retrieved snapshot), including infectious disease / severe acute respiratory syndrome, neurodegenerative disease, ptosis, and color vision disorder. These should be treated as hypothesis-generating and require direct confirmation in primary experimental studies. (OpenTargets Search: -ENPP5).
Primary biochemical function supported by direct assays: ENPP5 is best annotated as a cell-surface, Zn-dependent ecto-phosphodiesterase/pyrophosphatase with narrow substrate selectivity, showing strongest activity toward NAD (and detectable activity toward ADPR and UDPG) under in vitro conditions. (gorelik2017akeytyrosine pages 4-7, borza2022structureandfunction pages 7-8).
Not a general extracellular ATPase: Multiple lines of evidence indicate wild-type human ENPP5 has minimal/undetectable activity on ATP/ADP/UTP; a single amino-acid swap (Y73F) is sufficient to re-enable canonical nucleotide hydrolysis, strongly implicating substrate-access restriction rather than loss of the catalytic machinery per se. (randriamihaja2017structuralanalysesofa pages 49-55).
Physiological role remains uncertain due to low catalytic efficiency: Even though NAD is a favored substrate in vitro, the combination of low affinity (KM > 1 mM) and low catalytic efficiency suggests ENPP5’s physiological impact may be limited to niches with unusually high local substrate availability or may involve additional, not-yet-tested substrates. (gorelik2017akeytyrosine pages 7-10, borza2022structureandfunction pages 7-8).
Disease/phenotype evidence is mainly correlative: Recent mentions in senescence/skin aging and in plasma proteomics are valuable for hypothesis generation and for application as measurable biomarkers, but they do not yet establish a causal ENPP5 mechanism in vivo. (o’reilly2024agingsenescenceand pages 6-7, sathyan2020plasmaproteomicprofile pages 5-7, OpenTargets Search: -ENPP5).
| Category | Key points | Best supporting citations (pqac IDs) | Key references with year + DOI URL |
|---|---|---|---|
| Identity/Family | Human ENPP5 corresponds to UniProt Q9UJA9, an ectonucleotide pyrophosphatase/phosphodiesterase family member (NPP5), and is described as among the least characterized ENPP family members. Comparative family reviews place ENPP5 within the extracellular nucleotide-metabolizing ENPP clade and distinguish it from better-characterized ENPP1/2/3/6/7. | (gorelik2017akeytyrosine pages 1-4, borza2022structureandfunction pages 7-8, borza2022structureandfunction pages 8-9) | Gorelik et al., 2017, FEBS J. https://doi.org/10.1111/febs.14266 ; Borza et al., 2022, J Biol Chem. https://doi.org/10.1016/j.jbc.2021.101526 |
| Topology & localization | ENPP5 is a type I transmembrane ectoenzyme with an N-terminal signal peptide and a C-terminal transmembrane helix plus short cytoplasmic tail; soluble crystallographic constructs used residues 25–430 after removing the membrane/cytoplasmic region. Reviews and primary structural work describe it as extracellular/membrane-anchored. | (gorelik2017akeytyrosine pages 1-4, gorelik2017akeytyrosine pages 7-10, gorelik2017akeytyrosine pages 4-7, randriamihaja2017structuralanalysesof pages 40-49, randriamihaja2017structuralanalysesofa pages 40-49) | Gorelik et al., 2017, FEBS J. https://doi.org/10.1111/febs.14266 ; Randriamihaja, 2017 structural thesis/article (journal unavailable in retrieved record) |
| Catalytic mechanism/cofactors | ENPP5 has the ENPP alkaline-phosphatase-like catalytic core with the usual binuclear Zn2+ catalytic center and a reported third ENPP5-specific Zn2+ (Zn3) near the active site. Zn3 is coordinated by Glu159 and Asp192 and can contact ribose 2'/3' oxygens; mutation E159S reportedly did not change ADP or NAD hydrolysis rates, so Zn3 may aid recognition rather than being essential for catalysis. Catalytic nucleophile is Thr72/Thr75 numbering depending on construct/species context. | (gorelik2017akeytyrosine pages 7-10, gorelik2017akeytyrosine pages 4-7, borza2022structureandfunction pages 7-8, gorelik2017akeytyrosine media 261ec884) | Gorelik et al., 2017, FEBS J. https://doi.org/10.1111/febs.14266 ; Borza et al., 2022, J Biol Chem. https://doi.org/10.1016/j.jbc.2021.101526 |
| Substrate specificity & kinetics | Wild-type ENPP5 shows minimal/undetectable activity toward many standard ENPP substrates and common nucleotides including ATP, ADP, UTP, and is also reported inactive on p-nitrophenyl-TMP, lysophosphatidylcholine, and glycerophosphocholine. In contrast, wild-type ENPP5 hydrolyzes NAD+ (highest activity among tested substrates) and also cleaves ADP-ribose (ADPR) and UDP-glucose (UDPG). Reported KM for NAD+ is >1 mM and catalytic efficiency for NAD+ is 0.00067 s−1 μM−1, indicating very low efficiency. | (gorelik2017akeytyrosine pages 7-10, gorelik2017akeytyrosine pages 4-7, randriamihaja2017structuralanalysesof pages 49-55, borza2022structureandfunction pages 7-8) | Gorelik et al., 2017, FEBS J. https://doi.org/10.1111/febs.14266 ; Borza et al., 2022, J Biol Chem. https://doi.org/10.1016/j.jbc.2021.101526 |
| Key residues/structure | A distinctive Tyr73 occupies the nucleotide-binding slot where other ENPPs commonly have Phe. Structural/functional studies indicate Tyr73 sterically restricts nucleotide binding/hydrolysis; Y73F restores activity toward ATP/ADP/UDP and broader NTP/NDP hydrolysis. ENPP5 structures reported for human/mouse include PDB 5VEM, 5VEN, 5VEO. Mutation of catalytic Thr75 to Ala caused precipitation/failure to crystallize, suggesting an important role in folding/stability. | (gorelik2017akeytyrosine pages 1-4, gorelik2017akeytyrosine pages 7-10, randriamihaja2017structuralanalysesofa pages 49-55, gorelik2017akeytyrosine pages 4-7, gorelik2017akeytyrosine media 261ec884) | Gorelik et al., 2017, FEBS J. https://doi.org/10.1111/febs.14266 ; Borza et al., 2022, J Biol Chem. https://doi.org/10.1016/j.jbc.2021.101526 |
| Pathway context | ENPP5 is discussed in the context of extracellular nucleotide metabolism/purinergic signaling. Because it can cleave NAD+, reviews propose a possible role in NAD-based neurotransmission, but this remains hypothetical and unvalidated; one structural study also notes possible roles in neural communication and purinergic pathways. | (borza2022structureandfunction pages 8-9, randriamihaja2017structuralanalysesofa pages 49-55, gorelik2017akeytyrosine pages 1-4) | Borza et al., 2022, J Biol Chem. https://doi.org/10.1016/j.jbc.2021.101526 ; Gorelik et al., 2017, FEBS J. https://doi.org/10.1111/febs.14266 |
| Disease/phenotype associations | Direct causal disease biology for ENPP5 is weakly established in the retrieved evidence. Open Targets lists low-confidence associations to infectious disease, neurodegenerative disease, ptosis, color vision disorder, and severe acute respiratory syndrome, each supported by only 3 evidence items in the retrieved context, so these should be treated as hypothesis-generating rather than confirmed. In plasma proteomics of frailty, ENPP5 was negatively associated with frailty with estimate −0.0713, SE 0.0102, p = 6.83E−12. | (OpenTargets Search: -ENPP5, sathyan2020plasmaproteomicprofile pages 5-7) | Open Targets context (retrieved association summary) ; Sathyan et al., 2020, Aging Cell. https://doi.org/10.1111/acel.13193 |
| Recent 2023-2024 findings | Recent literature remains mostly indirect/omics/review-level rather than mechanistic. A 2024 review on skin aging/wound healing states ENPP5 was reported as a key factor in senescence in dermal fibroblasts, and knockdown retarded senescence. A 2024 obesity/mouse study states ENPP5 was downregulated after PKCδ inhibitor treatment and refers to ENPP5 as a biomarker related to insulin resistance. A 2024 long-COVID preprint identifies ENPP5 among proteins negatively correlated with symptom-associated signatures. A 2024 in silico ADC-target study lists ENPP5 as a potential ADC target, but without experimental validation in the retrieved excerpt. | (o’reilly2024agingsenescenceand pages 6-7, osborne2024smallmoleculeinhibitor pages 13-16, buggert2024identificationofsoluble pages 20-23, kathad2024expandingtherepertoire pages 14-16) | O’Reilly et al., 2024, Front Immunol. https://doi.org/10.3389/fimmu.2024.1429716 ; Osborne et al., 2024, Biology. https://doi.org/10.3390/biology13110943 ; Buggert et al., 2024 preprint. https://doi.org/10.21203/rs.3.rs-4466781/v1 ; Kathad et al., 2024, PLOS ONE. https://doi.org/10.1371/journal.pone.0308604 |
| Applications/implementations | Current real-world use is mainly as a measurable protein/analyte rather than a validated therapeutic target. ENPP5 appears in plasma proteomic biomarker panels (frailty; long COVID), and antibodies recognizing ENPP5 in native conformation have been generated for monitoring cell-surface expression in research settings. Structural data and restored activity in Y73F suggest possible utility for enzyme engineering/substrate-discovery studies. | (sathyan2020plasmaproteomicprofile pages 5-7, buggert2024identificationofsoluble pages 20-23, gorelik2017akeytyrosine pages 1-4) | Sathyan et al., 2020, Aging Cell. https://doi.org/10.1111/acel.13193 ; Möller et al., 2007, Purinergic Signalling. https://doi.org/10.1007/s11302-007-9084-9 ; Gorelik et al., 2017, FEBS J. https://doi.org/10.1111/febs.14266 |
| Evidence gaps | Major gaps remain: physiological substrate(s) are still uncertain; activity is only convincingly shown for a narrow set of substrates with very low NAD+ efficiency; localization is inferred from topology rather than extensive endogenous cell biology; disease links are largely correlative; and proposed roles in NAD neurotransmission, senescence, and metabolic disease lack strong genetic/biochemical validation in the retrieved evidence. Reviews explicitly note that ENPP5 is among the least characterized family members and that validation in KO models is needed. | (borza2022structureandfunction pages 7-8, borza2022structureandfunction pages 8-9, randriamihaja2017structuralanalysesof pages 49-55, randriamihaja2017structuralanalysesof pages 40-49) | Borza et al., 2022, J Biol Chem. https://doi.org/10.1016/j.jbc.2021.101526 ; Gorelik et al., 2017, FEBS J. https://doi.org/10.1111/febs.14266 ; Randriamihaja, 2017 structural thesis/article (journal unavailable in retrieved record) |
Table: This table consolidates the strongest retrieved evidence on human ENPP5/Q9UJA9, covering identity, localization, catalytic properties, structure, pathway context, disease links, and recent 2023-2024 findings. It is useful as a compact evidence map showing what is established versus what remains uncertain for functional annotation.
References
(gorelik2017akeytyrosine pages 1-4): Alexei Gorelik, Antsa Randriamihaja, Katalin Illes, and Bhushan Nagar. A key tyrosine substitution restricts nucleotide hydrolysis by the ectoenzyme
(borza2022structureandfunction pages 8-9): Razvan Borza, Fernando Salgado-Polo, Wouter H. Moolenaar, and Anastassis Perrakis. Structure and function of the ecto-nucleotide pyrophosphatase/phosphodiesterase (enpp) family: tidying up diversity. Feb 2022. URL: https://doi.org/10.1016/j.jbc.2021.101526, doi:10.1016/j.jbc.2021.101526. This article has 134 citations and is from a domain leading peer-reviewed journal.
(gorelik2017akeytyrosine pages 4-7): Alexei Gorelik, Antsa Randriamihaja, Katalin Illes, and Bhushan Nagar. A key tyrosine substitution restricts nucleotide hydrolysis by the ectoenzyme
(gorelik2017akeytyrosine pages 7-10): Alexei Gorelik, Antsa Randriamihaja, Katalin Illes, and Bhushan Nagar. A key tyrosine substitution restricts nucleotide hydrolysis by the ectoenzyme
(borza2022structureandfunction pages 7-8): Razvan Borza, Fernando Salgado-Polo, Wouter H. Moolenaar, and Anastassis Perrakis. Structure and function of the ecto-nucleotide pyrophosphatase/phosphodiesterase (enpp) family: tidying up diversity. Feb 2022. URL: https://doi.org/10.1016/j.jbc.2021.101526, doi:10.1016/j.jbc.2021.101526. This article has 134 citations and is from a domain leading peer-reviewed journal.
(randriamihaja2017structuralanalysesofa pages 49-55): A Randriamihaja. Structural analyses of the ecto-nucleotides pyrophosphatases/phosphodiesterases 3 and 5. Unknown journal, 2017.
(randriamihaja2017structuralanalysesof pages 49-55): A Randriamihaja. Structural analyses of the ecto-nucleotides pyrophosphatases/phosphodiesterases 3 and 5. Unknown journal, 2017.
(gorelik2017akeytyrosine media 261ec884): Alexei Gorelik, Antsa Randriamihaja, Katalin Illes, and Bhushan Nagar. A key tyrosine substitution restricts nucleotide hydrolysis by the ectoenzyme
(gorelik2017akeytyrosine media 7d676195): Alexei Gorelik, Antsa Randriamihaja, Katalin Illes, and Bhushan Nagar. A key tyrosine substitution restricts nucleotide hydrolysis by the ectoenzyme
(gorelik2017akeytyrosine media 4e0a41b5): Alexei Gorelik, Antsa Randriamihaja, Katalin Illes, and Bhushan Nagar. A key tyrosine substitution restricts nucleotide hydrolysis by the ectoenzyme
(o’reilly2024agingsenescenceand pages 6-7): Steven O’Reilly, Ewa Markiewicz, and Olusola C. Idowu. Aging, senescence, and cutaneous wound healing—a complex relationship. Frontiers in Immunology, Oct 2024. URL: https://doi.org/10.3389/fimmu.2024.1429716, doi:10.3389/fimmu.2024.1429716. This article has 41 citations and is from a peer-reviewed journal.
(sathyan2020plasmaproteomicprofile pages 5-7): Sanish Sathyan, Emmeline Ayers, Tina Gao, Sofiya Milman, Nir Barzilai, and Joe Verghese. Plasma proteomic profile of frailty. Aging Cell, Aug 2020. URL: https://doi.org/10.1111/acel.13193, doi:10.1111/acel.13193. This article has 55 citations and is from a domain leading peer-reviewed journal.
(buggert2024identificationofsoluble pages 20-23): Marcus Buggert, Yu Gao, Curtis Cai, Sarah Adamo, Elsa Biteus, Habiba Kamal, Lena Dager, Kelly Miners, Sian Llewellyn-Lacey, Kristin Ladell, Pragati Sabberwal, Kirsten Bentley, Jinghua Wu, Mily Akhirunnesa, Samantha Jones, Per Julin, Christer Lidman, Richard Stanton, Helen Davies, Soo Aleman, David Price, Paul Goepfert, Steven Deeks, and Michael Peluso. Identification of soluble biomarkers that associate with distinct manifestations of long covid. Unknown journal, Jun 2024. URL: https://doi.org/10.21203/rs.3.rs-4466781/v1, doi:10.21203/rs.3.rs-4466781/v1.
(kathad2024expandingtherepertoire pages 14-16): Umesh Kathad, Neha Biyani, Raniero L. Peru y Colón De Portugal, Jianli Zhou, Harry Kochat, and Kishor Bhatia. Expanding the repertoire of antibody drug conjugate (adc) targets with improved tumor selectivity and range of potent payloads through in-silico analysis. PLOS ONE, 19:e0308604, Aug 2024. URL: https://doi.org/10.1371/journal.pone.0308604, doi:10.1371/journal.pone.0308604. This article has 9 citations and is from a peer-reviewed journal.
(OpenTargets Search: -ENPP5): Open Targets Query (-ENPP5, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(randriamihaja2017structuralanalysesof pages 40-49): A Randriamihaja. Structural analyses of the ecto-nucleotides pyrophosphatases/phosphodiesterases 3 and 5. Unknown journal, 2017.
(randriamihaja2017structuralanalysesofa pages 40-49): A Randriamihaja. Structural analyses of the ecto-nucleotides pyrophosphatases/phosphodiesterases 3 and 5. Unknown journal, 2017.
(osborne2024smallmoleculeinhibitor pages 13-16): Brenna Osborne, Rekha S. Patel, Meredith Krause-Hauch, Ashley Lui, Gitanjali Vidyarthi, and Niketa A. Patel. Small molecule inhibitor of protein kinase c deltai (pkcδi) decreases inflammatory pathways and gene expression and improves metabolic function in diet-induced obese mouse model. Biology, 13(11):943, Nov 2024. URL: https://doi.org/10.3390/biology13110943, doi:10.3390/biology13110943. This article has 4 citations.