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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Identity verification passed. The target is unambiguously human ZDHHC23 (zinc finger DHHC-type palmitoyltransferase 23; DHHC-23; UniProt Q8IYP9), not a similarly named protein from another organism. Independent structural work explicitly identifies Q8IYP9 as human palmitoyltransferase ZDHHC23. Its DHHC cysteine-rich domain, predicted multi-pass membrane topology, and zinc-binding architecture agree with assignment to the DHHC protein S-acyltransferase family (durr2023metal3dageneral pages 6-7, allagioti2025analysisandfunctional pages 33-37).
The best-supported primary function is membrane-associated protein S-acyltransferase activity: transfer of a long-chain fatty acyl group from fatty acyl-CoA to a substrate cysteine, forming a reversible thioester. ZDHHC23 shows a marked biochemical preference for C18:0/stearoyl donor relative to C14:0 and C16:0 probes, although this was measured principally through enzyme autoacylation and should not be interpreted as absolute donor exclusivity (anwar2023refiningsacylationstructure pages 2-3, greaves2017molecularbasisof pages 6-6).
The strongest substrate/pathway evidence supports:
ZDHHC23 is therefore best understood as a predominantly Golgi/trans-Golgi or perinuclear endomembrane enzyme whose physiological effects depend on which substrate encounters it in a particular cellular context. Evidence for nuclear colocalization with PHF2 in HCC cells suggests either context-dependent distribution or trafficking, but the protein’s endogenous localization remains incompletely mapped across human tissues (jeong2023palmitoylationdrivenphf2ubiquitination pages 2-3, duncan2019sacylationcontrolsfunctional pages 4-5).
The supplied identity—ZDHHC23, Homo sapiens, UniProt Q8IYP9—matches the literature. A 2023 structural-informatics study specifically analyzed “human palmitoyltransferase ZDHHC23 (UniProt Q8IYP9),” independently confirming accession, organism, and functional family (durr2023metal3dageneral pages 6-7).
ZDHHC proteins are integral membrane S-acyltransferases named for the conserved Asp–His–His–Cys (DHHC) motif. Their catalytic region lies on the cytosolic face of the membrane, allowing access to cytosolic domains of membrane proteins and soluble proteins recruited to membranes. ZDHHC23 is unusual within the family in being predicted to have six transmembrane helices, with its catalytic region between the fourth and fifth helices, rather than the canonical four-pass arrangement with the DHHC domain between TM2 and TM3 (allagioti2025analysisandfunctional pages 33-37). This agrees with the supplied InterPro/Pfam assignments—Palmitoyltrfase_DHHC, PFA4/ZDH16/20/ERF2-like, and PF01529—and does not indicate symbol ambiguity.
The “zinc finger” designation primarily describes structural metal coordination rather than a conventional DNA-binding zinc finger. Metal3D analysis of the high-confidence AlphaFold2 Q8IYP9 model predicted two zinc sites with probabilities above 0.99 and positional deviations of 0.75 Å and 0.48 Å from reference placements. Homology-based AlphaFill could not place these metals because the closest structural template, PDB 6BMS, shared only 24% sequence identity, below its 25% threshold (durr2023metal3dageneral pages 6-7). These predictions strengthen the structural annotation but do not constitute an experimental ZDHHC23 structure.
The family-level reaction is:
fatty acyl-CoA + protein cysteine → CoA + protein-S-acyl thioester.
Current mechanistic understanding supports a two-step, ping-pong cycle. First, fatty acyl-CoA acylates the conserved DHHC cysteine, forming a transient enzyme–acyl intermediate. Second, the acyl group is transferred to a cysteine in the protein substrate; water can alternatively hydrolyze the intermediate. The membrane-embedded helices form a hydrophobic cavity that helps select acyl-chain length, while the cytosolic DHHC region performs acyl transfer (malgapo2021substraterecruitmentby pages 3-4, anwar2023refiningsacylationstructure pages 2-3).
For ZDHHC23 specifically, click-chemistry analysis in HA-ZDHHC-expressing HEK293T cells compared C14:0, C16:0, and C18:0 fatty-acid azides. ZDHHC23 displayed a strong preference for the longest tested chain, C18:0, whereas several other family members preferred C14/C16 or lacked a clear preference. The experiment involved 4-hour labeling at 37 °C and at least six replicates in the additional-enzyme analysis (greaves2017molecularbasisof pages 6-6). Because the principal readout was ZDHHC23 autoacylation, it establishes donor engagement more directly than it establishes the exact fatty acid transferred to every physiological protein substrate. Thus, “stearoyl-preferring protein S-acyltransferase” is more precise than treating ZDHHC23 as exclusively a palmitoyl/C16 enzyme.
Protein-substrate specificity is only partly understood. Authoritative reviews emphasize that proximity in a shared membrane compartment, transient recruitment, accessory proteins, transmembrane-domain recognition, and motifs outside the catalytic core may all contribute. Consequently, co-expression, colocalization, or a change after knockdown alone is insufficient for definitive substrate assignment; site mutants, catalytic dependence, biochemical acylation assays, and endogenous genetics provide stronger evidence (anwar2023refiningsacylationstructure pages 3-5, mesquita2024mechanismsandfunctions pages 1-5).
The following table separates demonstrated catalytic substrates from regulatory associations and exploratory candidates.
| Substrate/pathway | Modified site or molecular event | Model and key evidence | Functional consequence | Evidence strength and key citation/date/DOI URL |
|---|---|---|---|---|
| KCNMA1/BK α channel | S-acylation of Cys53, Cys54 and Cys56 in the intracellular S0–S1 loop; ZDHHC22 provides overlapping activity | HEK293 siRNA/overexpression, [³H]palmitate incorporation and trafficking assays; Zdhhc23-knockout mouse vascular smooth-muscle cells showed ~60% lower BK S-acylation and ~40% lower sustained BK current | Promotes trans-Golgi-network exit and surface delivery in recombinant cells; in β1-expressing vascular muscle, principally supports α–β1 functional coupling and BK current without changing the ~12% surface pool | Strong: mapped cysteines, enzyme perturbation and genetic knockout physiology. Tian et al., 18 Apr 2012, DOI; Duncan et al., 2 Aug 2019, DOI (duncan2019sacylationcontrolsfunctional pages 4-5, tian2012distinctacylprotein pages 2-3, duncan2019sacylationcontrolsfunctional pages 13-16) |
| PHF2–SREBP1c lipid-metabolism pathway | ZDHHC23-dependent PHF2 S-palmitoylation at Cys23, followed by PHF2 ubiquitination and proteasomal degradation | Human HepG2/Hep3B HCC cells; screen of all 23 ZDHHCs, siRNA/overexpression, ABE and LC–MS, WT-versus-C23A PHF2, binding and palmitoyl-CoA labeling; PHF2 and ZDHHC23 colocalized in nuclei | Loss of the PHF2 E3-ligase function stabilizes SREBP1c, increasing lipogenic programs, lipid accumulation and spheroid growth; supports a palmitic-acid–PHF2–SREBP1c feedback loop | Strong cellular/mechanistic; clinical association observational: Jeong et al., 12 Oct 2023, DOI (jeong2023palmitoylationdrivenphf2ubiquitination pages 2-3, jeong2023palmitoylationdrivenphf2ubiquitination pages 1-2, jeong2023palmitoylationdrivenphf2ubiquitination pages 3-4, jeong2023palmitoylationdrivenphf2ubiquitination pages 10-11) |
| GFAP–STAT3 inflammatory pain pathway | ZDHHC23-dependent GFAP palmitoylation at Cys291 | MA-C mouse astrocytes and C57BL/6 S-180 sciatic-nerve cancer-pain model; ABE, co-IP, ZDHHC23 siRNA, 2-bromopalmitate and GFAP-C291A; a competing GFAP peptide was tested in cells and mice | Enhances astrocyte activation, branching, CXCL10/IL-6/GM-CSF release and STAT3 phosphorylation; peptide interference reduced pain signaling and morphine tolerance in the rodent model | Moderate-to-strong preclinical: site mutation and enzyme knockdown support causality, but no human validation. Fan et al., Nov 2024, DOI (fan2024gfappalmitoylcationmediated pages 1-1, fan2024gfappalmitoylcationmediated pages 7-8, fan2024gfappalmitoylcationmediated pages 3-3, fan2024gfappalmitoylcationmediated pages 6-7, fan2024gfappalmitoylcationmediated pages 8-9) |
| BMI1–RNF144A / glioma-stem-cell plasticity | ZDHHC23 recruits/interacts with RNF144A and BMI1, increasing BMI1 polyubiquitination and reducing BMI1 abundance; BMI1 palmitoylation was not demonstrated | Human proneural and mesenchymal glioma stem cells, patient GBM tissue, co-IP/LC–MS and ZDHHC23 depletion/overexpression; ZDHHC23 was enriched in proneural/CD133⁺ leading-edge cells | Helps regulate proneural–mesenchymal state transitions and survival under tumor-microenvironment stress through BMI1 abundance | Moderate: direct protein-network and perturbation evidence, but the event is ubiquitination regulation—not an established ZDHHC23-catalyzed S-acylation reaction. Chen et al., 28 Jan 2019, DOI (chen2019dhhcproteinfamily pages 6-9, chen2019dhhcproteinfamily pages 11-14, chen2019dhhcproteinfamily pages 9-11) |
| Exploratory neuroblastoma interactome | No validated substrate; candidate associations with proteasome/ERAD, ARP2/3, transport and RNA-binding networks; phosphorylation detected at ZDHHC23 Ser206, Ser232 and Ser252 | Exogenous HA–mCherry-ZDHHC23 immunoprecipitation/LC–MS in SK-N-AS cells at 21% versus 1% O₂; 262 candidate interactors, ~45–50% sequence coverage; endogenous antibodies/IP and tumour PRM failed validation | Hypothesized links to cytoskeletal organization, adhesion, senescence and oxygen-dependent signaling; Golgi localization was suggested but ER localization was not excluded | Exploratory/low: tagged-protein discovery study with no validated endogenous substrate or interaction. Oswald, Jan 2023, doctoral thesis, DOI (oswald2023aproteomicsinvestigation pages 158-163, oswald2023aproteomicsinvestigation pages 100-106, oswald2023aproteomicsinvestigation pages 177-180, oswald2023aproteomicsinvestigation pages 96-100, oswald2023aproteomicsinvestigation pages 134-141, oswald2023aproteomicsinvestigation pages 167-170) |
Table: Evidence-calibrated summary of established and proposed mammalian ZDHHC23 substrates, pathways and functional consequences. It distinguishes demonstrated S-acylation reactions from non-catalytic protein-network effects and exploratory proteomics.
The earliest precise substrate evidence concerns the pore-forming α-subunit of the large-conductance Ca²⁺/voltage-activated K⁺ channel, encoded by KCNMA1. Tian et al. identified ZDHHC22 and ZDHHC23 as enzymes modifying Cys53, Cys54, and Cys56 in the intracellular S0–S1 loop. In HEK293 assays, ZDHHC23 overexpression increased surface expression of an S0–S1 reporter to 144 ± 5.3% of control. Tagged ZDHHC23 localized mainly to Golgi/TGN compartments, with reported correlations of R=0.71 ± 0.01 with GM130 and R=0.38 ± 0.02 with TGN38 (n=15). Loss of S-acylation delayed BK-channel exit from the trans-Golgi network (tian2012distinctacylprotein pages 2-3, tian2012distinctacylprotein pages 1-2).
Genetic evidence subsequently established physiological relevance. In vascular smooth-muscle cells from Zdhhc23-null mice, endogenous BK α-subunit S-acylation fell by approximately 60%, consistent with residual activity from ZDHHC22. Sustained BK current was approximately 40% lower, yet channel surface abundance was unchanged: 12.6 ± 0.6% in wild type, 12.4 ± 0.5% in knockout, and 11.7 ± 0.6% after 2-bromopalmitate treatment (p=0.485). Thus, in β1-containing vascular smooth muscle, ZDHHC23-dependent acylation principally governs functional α–β1 coupling rather than simply the number of channels at the surface (duncan2019sacylationcontrolsfunctional pages 4-5). The effects of α-subunit acylation and β1 expression on half-maximal activation voltage were both highly significant—F(1,129)=34.28 and F(2,129)=49.24, respectively; p<0.0001, n≥14 (duncan2019sacylationcontrolsfunctional pages 13-16).
This is the strongest evidence that ZDHHC23 has a normal physiological role: it combines mapped substrate cysteines, biochemical assays, trafficking data, genetic knockout, and native electrophysiology.
A major 2023 development was identification of PHF2 Cys23 as a ZDHHC23 substrate in human HepG2 and Hep3B hepatocellular-carcinoma cells. Palmitic-acid exposure increased palmitoyl-CoA and PHF2 S-acylation; 2-bromopalmitate at 50 μM blocked the response. LC–MS and acyl-biotin exchange mapped the site to Cys23, and PHF2-C23A resisted both acylation and palmitic-acid-induced loss (jeong2023palmitoylationdrivenphf2ubiquitination pages 1-2, jeong2023palmitoylationdrivenphf2ubiquitination pages 3-4).
A screen of all 23 human ZDHHCs found five knockdown hits—ZDHHC4, ZDHHC5, ZDHHC11, ZDHHC17, and ZDHHC23—but endogenous experiments identified ZDHHC23 as the predominant enzyme in HepG2 cells. Wild-type PHF2, but not C23A, bound ZDHHC23; time-resolved palmitoyl-CoA labeling and colocalization further supported a direct enzyme–substrate relationship. Molecular modeling placed palmitoyl-CoA approximately 5 Å from PHF2 Cys23 (jeong2023palmitoylationdrivenphf2ubiquitination pages 2-3, jeong2023palmitoylationdrivenphf2ubiquitination pages 3-4).
Functionally, acylation promoted PHF2 ubiquitination and proteasomal degradation. PHF2 was reported to act as an E3 ligase that destabilizes SREBP1c, so PHF2 loss increased SREBP1c, lipogenic genes, lipid accumulation, and spheroid growth. The authors proposed a positive-feedback loop: SREBP1c increases fatty-acid production, including palmitate; palmitate drives ZDHHC23-dependent PHF2 loss; reduced PHF2 further stabilizes SREBP1c. In human datasets, ZDHHC23 expression correlated positively with HCC stage/grade and SREBP1c-associated programs and inversely with PHF2, although the retrieved report did not provide correlation coefficients or clinical sample sizes (jeong2023palmitoylationdrivenphf2ubiquitination pages 10-11).
This is strong mechanistic evidence in human cancer cells, but evidence that inhibiting ZDHHC23 would safely treat patients remains absent. The study’s dietary-palmitate implication is hypothesis-generating, not a clinical dietary guideline.
Fan et al. (November 2024) studied a C57BL/6 mouse model in which S-180 sarcoma cells were inoculated around the sciatic nerve, together with MA-C mouse astrocytes and L4–L6 dorsal-horn tissue. Tumor growth and nerve invasion were accompanied by increased spinal ZDHHC23, GFAP S-acylation, astrocyte activation, and pain behavior (fan2024gfappalmitoylcationmediated pages 1-1, fan2024gfappalmitoylcationmediated pages 3-3).
A 23-ZDHHC screen initially implicated ZDHHC5, ZDHHC12, ZDHHC21, and ZDHHC23, but siRNA experiments identified ZDHHC23 as the functionally important enzyme. Mutation GFAP C291A, ZDHHC23 knockdown, or 48-hour 2-bromopalmitate treatment reduced GFAP acylation and suppressed astrocyte activation, process/branch changes, cytokine release, and STAT3 phosphorylation. The measured inflammatory mediators included IL-6, CXCL10, and GM-CSF; the proposed circuit is GFAP S-acylation → astrocyte activation → IL-6/JAK2/STAT3 signaling → further astrocyte proliferation and central sensitization (fan2024gfappalmitoylcationmediated pages 7-8, fan2024gfappalmitoylcationmediated pages 6-7).
A competitive GFAP peptide was tested at 25 μg/mL in vitro and 50 μg per injection twice daily in vivo. It reduced pain-associated signaling and attenuated morphine tolerance in mice (fan2024gfappalmitoylcationmediated pages 8-9, fan2024gfappalmitoylcationmediated pages 5-6). This is a promising substrate-directed proof of concept, but it is wholly preclinical; the authors explicitly call for human translational work. It also does not prove that inhibiting ZDHHC23 systemically would be safe or selective.
In human glioma stem cells, ZDHHC23 was preferentially associated with the proneural state and found mainly at the tumor leading edge, where it co-expressed with CD133 and OLIG2. ZDHHC23 depletion shifted proneural cells toward mesenchymal markers; overexpression in mesenchymal cells promoted the reverse transition and reduced survival under stress (chen2019dhhcproteinfamily pages 6-9).
Mechanistically, ZDHHC23 interacted with RNF144A and recruited RNF144A to BMI1, increasing BMI1 polyubiquitination and reducing BMI1 abundance. ZDHHC23 depletion reduced BMI1 polyubiquitination, whereas ZDHHC23 overexpression reduced BMI1 protein. More than 60% of ZDHHC18/ZDHHC23-associated proteins were subtype-specific, with 31 shared targets (chen2019dhhcproteinfamily pages 9-11).
The crucial annotation caveat is that these experiments established a protein-complex/ubiquitination mechanism. They did not map a BMI1 S-acylated cysteine or directly demonstrate ZDHHC23-catalyzed BMI1 palmitoylation. BMI1 should therefore be listed as a ZDHHC23-regulated pathway component or interactor, not a high-confidence enzymatic substrate (chen2019dhhcproteinfamily pages 11-14, chen2019dhhcproteinfamily pages 9-11).
The convergent localization model is cytosolic-face activity on Golgi/trans-Golgi and related perinuclear endomembranes. In the BK-channel study, overexpressed ZDHHC23 colocalized strongly with Golgi marker GM130 and more modestly with TGN38; BK channels lacking the relevant S-acylation were retained or delayed in the TGN. Native mouse vascular smooth-muscle staining was perinuclear/intracellular and consistent with Golgi/ER localization (duncan2019sacylationcontrolsfunctional pages 4-5, tian2012distinctacylprotein pages 2-3).
The 2023 PHF2 study reported ZDHHC23 in both cytoplasm and nucleus in human liver tissue and nuclear colocalization with PHF2 in HCC cells (jeong2023palmitoylationdrivenphf2ubiquitination pages 2-3). This is unusual for a multi-pass membrane enzyme and should be interpreted cautiously: possibilities include nuclear-envelope/contiguous ER membranes, antibody or resolution limitations, or genuine context-dependent localization. Biochemical membrane-fractionation and endogenous super-resolution studies would be needed to distinguish these possibilities.
Exploratory neuroblastoma imaging suggested oxygen-independent Golgi localization but could not exclude ER localization. Endogenous antibody validation was problematic: expected ZDHHC23 is approximately 45 kDa, but candidate antibodies generated inconsistent 34-, 55-, 72-, 95-, or >250-kDa signals, and endogenous IP–MS detected no ZDHHC23 peptides (oswald2023aproteomicsinvestigation pages 100-106, oswald2023aproteomicsinvestigation pages 177-180, oswald2023aproteomicsinvestigation pages 96-100). This methodological warning is important when interpreting database-derived tissue-localization claims.
There is no established clinical application, approved ZDHHC23-selective drug, validated companion diagnostic, or human interventional trial identified in the searched literature. Current implementations are research or preclinical:
Broad inhibitors such as 2-bromopalmitate are unsuitable as target-validation endpoints by themselves because they affect multiple lipid-metabolic and S-acylation processes. The 2024 GFAP study explicitly notes poor selectivity of commonly used inhibitors, and modern reviews stress the difficulty of selectively targeting the highly conserved DHHC catalytic core (fan2024gfappalmitoylcationmediated pages 9-9, anwar2023refiningsacylationstructure pages 3-5).
ZDHHC23 is a Golgi/perinuclear, multi-pass protein S-acyltransferase with preference for C18:0 acyl donors. It catalyzes cysteine S-acylation of selected proteins, thereby regulating secretory-pathway trafficking, ion-channel function, protein stability/ubiquitination, lipid-metabolic signaling, and—under pathological conditions—astrocyte inflammatory signaling.
ZDHHC23/Q8IYP9 is correctly identified as a human DHHC-family protein S-acyltransferase, with the strongest localization evidence placing it in Golgi/TGN or perinuclear endomembranes and biochemical evidence indicating preference for C18:0 fatty-acyl donors. The most rigorous functional evidence is the ZDHHC23–KCNMA1 axis in BK-channel trafficking and β1 coupling. Recent work expands its role to PHF2 degradation and SREBP1c-dependent lipid reprogramming in human HCC cells and to GFAP-dependent astrocyte inflammation and pain in mice. ZDHHC23 also regulates BMI1 ubiquitination through RNF144A in glioma stem cells, but this should not be annotated as proven BMI1 palmitoylation. Overall, ZDHHC23 is a mechanistically credible but still incompletely characterized enzyme and an early-stage preclinical target, not yet a clinically implemented biomarker or therapeutic target.
References
(durr2023metal3dageneral pages 6-7): Simon L. Dürr, Andrea Levy, and Ursula Rothlisberger. Metal3d: a general deep learning framework for accurate metal ion location prediction in proteins. Nature Communications, May 2023. URL: https://doi.org/10.1038/s41467-023-37870-6, doi:10.1038/s41467-023-37870-6. This article has 103 citations and is from a highest quality peer-reviewed journal.
(allagioti2025analysisandfunctional pages 33-37): D Allagioti. Analysis and functional characterisation of the zdhhc9/gcp16 protein complex. Unknown journal, 2025.
(anwar2023refiningsacylationstructure pages 2-3): Muhammad U. Anwar and F. Gisou van der Goot. Refining s-acylation: structure, regulation, dynamics, and therapeutic implications. The Journal of Cell Biology, Sep 2023. URL: https://doi.org/10.1083/jcb.202307103, doi:10.1083/jcb.202307103. This article has 39 citations.
(greaves2017molecularbasisof pages 6-6): Jennifer Greaves, Kevin R. Munro, Stuart C. Davidson, Matthieu Riviere, Justyna Wojno, Terry K. Smith, Nicholas C. O. Tomkinson, and Luke H. Chamberlain. Molecular basis of fatty acid selectivity in the zdhhc family of s-acyltransferases revealed by click chemistry. Proceedings of the National Academy of Sciences, 114:E1365-E1374, Feb 2017. URL: https://doi.org/10.1073/pnas.1612254114, doi:10.1073/pnas.1612254114. This article has 196 citations and is from a highest quality peer-reviewed journal.
(jeong2023palmitoylationdrivenphf2ubiquitination pages 2-3): Do-Won Jeong, Jong-Wan Park, Kyeong Seog Kim, Jiyoung Kim, June Huh, Jieun Seo, Ye Lee Kim, Joo-Youn Cho, Kwang-Woong Lee, Junji Fukuda, and Yang-Sook Chun. Palmitoylation-driven phf2 ubiquitination remodels lipid metabolism through the srebp1c axis in hepatocellular carcinoma. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-42170-0, doi:10.1038/s41467-023-42170-0. This article has 98 citations and is from a highest quality peer-reviewed journal.
(chen2019dhhcproteinfamily pages 9-11): Xueran Chen, Lei Hu, Haoran Yang, Huihui Ma, Kaiqin Ye, Chenggang Zhao, Zhiyang Zhao, Haiming Dai, Hongzhi Wang, and Zhiyou Fang. Dhhc protein family targets different subsets of glioma stem cells in specific niches. Journal of Experimental & Clinical Cancer Research : CR, Jan 2019. URL: https://doi.org/10.1186/s13046-019-1033-2, doi:10.1186/s13046-019-1033-2. This article has 64 citations.
(duncan2019sacylationcontrolsfunctional pages 4-5): Peter J. Duncan, Danlei Bi, Heather McClafferty, Lie Chen, Lijun Tian, and Michael J. Shipston. S-acylation controls functional coupling of bk channel pore-forming α-subunits and β1-subunits. Aug 2019. URL: https://doi.org/10.1074/jbc.ra119.009065, doi:10.1074/jbc.ra119.009065. This article has 18 citations and is from a domain leading peer-reviewed journal.
(tian2012distinctacylprotein pages 2-3): Lijun Tian, Heather McClafferty, Hans-Guenther Knaus, Peter Ruth, and Michael J. Shipston. Distinct acyl protein transferases and thioesterases control surface expression of calcium-activated potassium channels. Apr 2012. URL: https://doi.org/10.1074/jbc.m111.335547, doi:10.1074/jbc.m111.335547. This article has 160 citations and is from a domain leading peer-reviewed journal.
(fan2024gfappalmitoylcationmediated pages 7-8): Xiaoqing Fan, Siyu Zhang, Suling Sun, Wenxu Bi, Shuyang Li, Wei Wang, Xueran Chen, and Zhiyou Fang. Gfap palmitoylcation mediated by zdhhc23 in spinal astrocytes contributes to the development of neuropathic pain. Nov 2024. URL: https://doi.org/10.1136/rapm-2023-104980, doi:10.1136/rapm-2023-104980. This article has 12 citations and is from a domain leading peer-reviewed journal.
(malgapo2021substraterecruitmentby pages 3-4): Martin Ian P. Malgapo and Maurine E. Linder. Substrate recruitment by zdhhc protein acyltransferases. Open Biology, Apr 2021. URL: https://doi.org/10.1098/rsob.210026, doi:10.1098/rsob.210026. This article has 120 citations and is from a peer-reviewed journal.
(anwar2023refiningsacylationstructure pages 3-5): Muhammad U. Anwar and F. Gisou van der Goot. Refining s-acylation: structure, regulation, dynamics, and therapeutic implications. The Journal of Cell Biology, Sep 2023. URL: https://doi.org/10.1083/jcb.202307103, doi:10.1083/jcb.202307103. This article has 39 citations.
(mesquita2024mechanismsandfunctions pages 1-5): Francisco S. Mesquita, Laurence Abrami, Maurine E. Linder, Shernaz X. Bamji, Bryan C. Dickinson, and F. Gisou van der Goot. Mechanisms and functions of protein s-acylation. Nature reviews. Molecular cell biology, 25:488-509, Feb 2024. URL: https://doi.org/10.1038/s41580-024-00700-8, doi:10.1038/s41580-024-00700-8. This article has 238 citations.
(duncan2019sacylationcontrolsfunctional pages 13-16): Peter J. Duncan, Danlei Bi, Heather McClafferty, Lie Chen, Lijun Tian, and Michael J. Shipston. S-acylation controls functional coupling of bk channel pore-forming α-subunits and β1-subunits. Aug 2019. URL: https://doi.org/10.1074/jbc.ra119.009065, doi:10.1074/jbc.ra119.009065. This article has 18 citations and is from a domain leading peer-reviewed journal.
(jeong2023palmitoylationdrivenphf2ubiquitination pages 1-2): Do-Won Jeong, Jong-Wan Park, Kyeong Seog Kim, Jiyoung Kim, June Huh, Jieun Seo, Ye Lee Kim, Joo-Youn Cho, Kwang-Woong Lee, Junji Fukuda, and Yang-Sook Chun. Palmitoylation-driven phf2 ubiquitination remodels lipid metabolism through the srebp1c axis in hepatocellular carcinoma. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-42170-0, doi:10.1038/s41467-023-42170-0. This article has 98 citations and is from a highest quality peer-reviewed journal.
(jeong2023palmitoylationdrivenphf2ubiquitination pages 3-4): Do-Won Jeong, Jong-Wan Park, Kyeong Seog Kim, Jiyoung Kim, June Huh, Jieun Seo, Ye Lee Kim, Joo-Youn Cho, Kwang-Woong Lee, Junji Fukuda, and Yang-Sook Chun. Palmitoylation-driven phf2 ubiquitination remodels lipid metabolism through the srebp1c axis in hepatocellular carcinoma. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-42170-0, doi:10.1038/s41467-023-42170-0. This article has 98 citations and is from a highest quality peer-reviewed journal.
(jeong2023palmitoylationdrivenphf2ubiquitination pages 10-11): Do-Won Jeong, Jong-Wan Park, Kyeong Seog Kim, Jiyoung Kim, June Huh, Jieun Seo, Ye Lee Kim, Joo-Youn Cho, Kwang-Woong Lee, Junji Fukuda, and Yang-Sook Chun. Palmitoylation-driven phf2 ubiquitination remodels lipid metabolism through the srebp1c axis in hepatocellular carcinoma. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-42170-0, doi:10.1038/s41467-023-42170-0. This article has 98 citations and is from a highest quality peer-reviewed journal.
(fan2024gfappalmitoylcationmediated pages 1-1): Xiaoqing Fan, Siyu Zhang, Suling Sun, Wenxu Bi, Shuyang Li, Wei Wang, Xueran Chen, and Zhiyou Fang. Gfap palmitoylcation mediated by zdhhc23 in spinal astrocytes contributes to the development of neuropathic pain. Nov 2024. URL: https://doi.org/10.1136/rapm-2023-104980, doi:10.1136/rapm-2023-104980. This article has 12 citations and is from a domain leading peer-reviewed journal.
(fan2024gfappalmitoylcationmediated pages 3-3): Xiaoqing Fan, Siyu Zhang, Suling Sun, Wenxu Bi, Shuyang Li, Wei Wang, Xueran Chen, and Zhiyou Fang. Gfap palmitoylcation mediated by zdhhc23 in spinal astrocytes contributes to the development of neuropathic pain. Nov 2024. URL: https://doi.org/10.1136/rapm-2023-104980, doi:10.1136/rapm-2023-104980. This article has 12 citations and is from a domain leading peer-reviewed journal.
(fan2024gfappalmitoylcationmediated pages 6-7): Xiaoqing Fan, Siyu Zhang, Suling Sun, Wenxu Bi, Shuyang Li, Wei Wang, Xueran Chen, and Zhiyou Fang. Gfap palmitoylcation mediated by zdhhc23 in spinal astrocytes contributes to the development of neuropathic pain. Nov 2024. URL: https://doi.org/10.1136/rapm-2023-104980, doi:10.1136/rapm-2023-104980. This article has 12 citations and is from a domain leading peer-reviewed journal.
(fan2024gfappalmitoylcationmediated pages 8-9): Xiaoqing Fan, Siyu Zhang, Suling Sun, Wenxu Bi, Shuyang Li, Wei Wang, Xueran Chen, and Zhiyou Fang. Gfap palmitoylcation mediated by zdhhc23 in spinal astrocytes contributes to the development of neuropathic pain. Nov 2024. URL: https://doi.org/10.1136/rapm-2023-104980, doi:10.1136/rapm-2023-104980. This article has 12 citations and is from a domain leading peer-reviewed journal.
(chen2019dhhcproteinfamily pages 6-9): Xueran Chen, Lei Hu, Haoran Yang, Huihui Ma, Kaiqin Ye, Chenggang Zhao, Zhiyang Zhao, Haiming Dai, Hongzhi Wang, and Zhiyou Fang. Dhhc protein family targets different subsets of glioma stem cells in specific niches. Journal of Experimental & Clinical Cancer Research : CR, Jan 2019. URL: https://doi.org/10.1186/s13046-019-1033-2, doi:10.1186/s13046-019-1033-2. This article has 64 citations.
(chen2019dhhcproteinfamily pages 11-14): Xueran Chen, Lei Hu, Haoran Yang, Huihui Ma, Kaiqin Ye, Chenggang Zhao, Zhiyang Zhao, Haiming Dai, Hongzhi Wang, and Zhiyou Fang. Dhhc protein family targets different subsets of glioma stem cells in specific niches. Journal of Experimental & Clinical Cancer Research : CR, Jan 2019. URL: https://doi.org/10.1186/s13046-019-1033-2, doi:10.1186/s13046-019-1033-2. This article has 64 citations.
(oswald2023aproteomicsinvestigation pages 158-163): Sally Oswald. A proteomics investigation into the role of zdhhc23 and mroh6 in neuroblastoma. Text, Jan 2023. URL: https://doi.org/10.17638/03169651, doi:10.17638/03169651. This article has 0 citations and is from a peer-reviewed journal.
(oswald2023aproteomicsinvestigation pages 100-106): Sally Oswald. A proteomics investigation into the role of zdhhc23 and mroh6 in neuroblastoma. Text, Jan 2023. URL: https://doi.org/10.17638/03169651, doi:10.17638/03169651. This article has 0 citations and is from a peer-reviewed journal.
(oswald2023aproteomicsinvestigation pages 177-180): Sally Oswald. A proteomics investigation into the role of zdhhc23 and mroh6 in neuroblastoma. Text, Jan 2023. URL: https://doi.org/10.17638/03169651, doi:10.17638/03169651. This article has 0 citations and is from a peer-reviewed journal.
(oswald2023aproteomicsinvestigation pages 96-100): Sally Oswald. A proteomics investigation into the role of zdhhc23 and mroh6 in neuroblastoma. Text, Jan 2023. URL: https://doi.org/10.17638/03169651, doi:10.17638/03169651. This article has 0 citations and is from a peer-reviewed journal.
(oswald2023aproteomicsinvestigation pages 134-141): Sally Oswald. A proteomics investigation into the role of zdhhc23 and mroh6 in neuroblastoma. Text, Jan 2023. URL: https://doi.org/10.17638/03169651, doi:10.17638/03169651. This article has 0 citations and is from a peer-reviewed journal.
(oswald2023aproteomicsinvestigation pages 167-170): Sally Oswald. A proteomics investigation into the role of zdhhc23 and mroh6 in neuroblastoma. Text, Jan 2023. URL: https://doi.org/10.17638/03169651, doi:10.17638/03169651. This article has 0 citations and is from a peer-reviewed journal.
(tian2012distinctacylprotein pages 1-2): Lijun Tian, Heather McClafferty, Hans-Guenther Knaus, Peter Ruth, and Michael J. Shipston. Distinct acyl protein transferases and thioesterases control surface expression of calcium-activated potassium channels. Apr 2012. URL: https://doi.org/10.1074/jbc.m111.335547, doi:10.1074/jbc.m111.335547. This article has 160 citations and is from a domain leading peer-reviewed journal.
(fan2024gfappalmitoylcationmediated pages 5-6): Xiaoqing Fan, Siyu Zhang, Suling Sun, Wenxu Bi, Shuyang Li, Wei Wang, Xueran Chen, and Zhiyou Fang. Gfap palmitoylcation mediated by zdhhc23 in spinal astrocytes contributes to the development of neuropathic pain. Nov 2024. URL: https://doi.org/10.1136/rapm-2023-104980, doi:10.1136/rapm-2023-104980. This article has 12 citations and is from a domain leading peer-reviewed journal.
(tang2024researchprogresson pages 8-10): Beiyan Tang, Wei Kang, Qiang Dong, Zhenwei Qin, Lei Duan, Xianjun Zhao, Guoqiang Yuan, and Yawen Pan. Research progress on s-palmitoylation modification mediated by the zdhhc family in glioblastoma. Frontiers in Cell and Developmental Biology, Nov 2024. URL: https://doi.org/10.3389/fcell.2024.1413708, doi:10.3389/fcell.2024.1413708. This article has 14 citations.
(fan2024gfappalmitoylcationmediated pages 9-9): Xiaoqing Fan, Siyu Zhang, Suling Sun, Wenxu Bi, Shuyang Li, Wei Wang, Xueran Chen, and Zhiyou Fang. Gfap palmitoylcation mediated by zdhhc23 in spinal astrocytes contributes to the development of neuropathic pain. Nov 2024. URL: https://doi.org/10.1136/rapm-2023-104980, doi:10.1136/rapm-2023-104980. This article has 12 citations and is from a domain leading peer-reviewed journal.