Abstract
Lipids perform a wide range of functions inside the cell, ranging from structural building block of membranes and energy storage to cell signaling. The mode of action of many signaling lipids has remained elusive due to their low abundance, high lipophilicity, and inherent instability. Various chemical biology approaches, such as photoaffinity or activity-based protein profiling methods, have been employed to shed light on the biological role of lipids and the lipid–protein interaction profile. In this review, we will summarize the recent developments in the field of chemical probes to study lipid biology, especially in immunology, and indicate potential avenues for future research.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsReferences
Abe M, Nakano M, Kosaka A, Miyoshi H (2015) Syntheses of photoreactive cardiolipins for a photoaffinity labeling study. Tetrahedron Lett 56:2258–2261. https://doi.org/10.1016/j.tetlet.2015.03.056
Ahn K, Smith SE, Liimatta MB et al (2011) Mechanistic and pharmacological characterization of PF-04457845: a highly potent and selective fatty acid amide hydrolase inhibitor that reduces inflammatory and noninflammatory pain. J Pharmacol Exp Ther 338:114–124. https://doi.org/10.1124/jpet.111.180257
Arrowsmith CH, Audia JE, Austin C et al (2015) The promise and peril of chemical probes. Nat Chem Biol 11:536–541
Aureli M, Prioni S, Mauri L et al (2010) Photoactivable sphingosine as a tool to study membrane microenvironments in cultured cells. J Lipid Res 51:798–808. https://doi.org/10.1194/jlr.M001974
Baggelaar MP, Janssen FJ, van Esbroeck ACM et al (2013) Development of an activity-based probe and in silico design reveal highly selective inhibitors for diacylglycerol lipase-α in brain. Angew Chemie Int Ed 52:12081–12085. https://doi.org/10.1002/anie.201306295
Baggelaar MP, Van Esbroeck ACM, Van Rooden EJ et al (2017) Chemical proteomics maps brain region specific activity of endocannabinoid hydrolases. ACS Chem Biol 12:852–861. https://doi.org/10.1021/acschembio.6b01052
Bandyopadhyay S, Bong D (2011) Synthesis of trifunctional phosphatidylserine probes for identification of lipid-binding proteins. European J Org Chem 751–758. https://doi.org/10.1002/ejoc.201001264
Basu S, Dittel BN (2011) Unraveling the complexities of cannabinoid receptor 2 (CB2) immune regulation in health and disease. Immunol Res 51:26–38. https://doi.org/10.1007/s12026-011-8210-5
Bernstein PS, Choi S-Y, Ho Y-C, Rando RR (1995) Photoaffinity labeling of retinoic acid-binding proteins. Biochemistry 92:654–658
Bockelmann S, Mina JGM, Korneev S, et al (2018) A search for ceramide binding proteins using bifunctional lipid analogs yields CERT-related protein StarD7. J Lipid Res. https://doi.org/10.1194/jlr.m082354 (jlr.M082354)
Budelier MM, Cheng WWL, Bergdoll L et al (2017) Photoaffinity labeling with cholesterol analogues precisely maps a cholesterol-binding site in voltage-dependent anion channel-1. J Biol Chem 292:9294–9304. https://doi.org/10.1074/jbc.M116.773069
Bush JT, Walport LJ, McGouran JF et al (2013) The Ugi four-component reaction enables expedient synthesis and comparison of photoaffinity probes. Chem Sci 4:4115. https://doi.org/10.1039/c3sc51708j
Byrd KM, Arieno MD, Kennelly ME et al (2015) Design and synthesis of a crosslinker for studying intracellular steroid trafficking pathways. Bioorganic Med Chem 23:3843–3851. https://doi.org/10.1016/j.bmc.2015.03.053
Cabral GA, Griffin-Thomas L (2009) Emerging role of the cannabinoid receptor CB2 in immune regulation: therapeutic prospects for neuroinflammation. Expert Rev Mol Med 11:e3. https://doi.org/10.1017/S1462399409000957
Cai X, Conley SM, Naash MI (2009) RPE65: Role in the visual cycle, human retinal disease, and gene therapy. Ophthalmic Genet 30:57–62
Carlberg C (1999) Lipid soluble vitamins in gene regulation. In: BioFactors, IOS Press, Oxford, pp 91–97
Chang JW, Moellering RE, Cravatt BF (2012) An activity-based imaging probe for the integral membrane hydrolase KIAA1363. Angew Chemie Int Ed 51:966–970. https://doi.org/10.1002/anie.201107236
Chen G, Radominska-Pandya A (2000) Direct photoaffinity labeling of cellular retinoic acid-binding protein I (CRABP-I) with all-trans-retinoic acid: identification of amino acids in the ligand binding site. Biochemistry 39:12568–12574. https://doi.org/10.1021/bi000321n
Chen Y, Falck JR, Manthati VL et al (2011) 20-Iodo-14,15-epoxyeicosa-8(Z)-enoyl-3-azidophenylsulfonamide: photoaffinity labeling of a 14,15-epoxyeicosatrienoic acid receptor. Biochemistry 50:3840–3848. https://doi.org/10.1021/bi102070w
Chen W, Dong J, Plate L et al (2016) Arylfluorosulfates inactivate intracellular lipid binding protein(s) through chemoselective SuFEx reaction with a binding site Tyr residue. J Am Chem Soc 138:7353–7364. https://doi.org/10.1021/jacs.6b02960
Chiurchiù V, Battistini L, Maccarrone M (2015) Endocannabinoid signalling in innate and adaptive immunity. Immunology 144:352–364. https://doi.org/10.1111/imm.12441
Chiurchiù V, van der Stelt M, Centonze D, Maccarrone M (2018) The endocannabinoid system and its therapeutic exploitation in multiple sclerosis: clues for other neuroinflammatory diseases. Prog Neurobiol 160:82–100. https://doi.org/10.1016/j.pneurobio.2017.10.007
Cravatt BF, Wright AT, Kozarich JW (2008) Activity-based protein profiling: from enzyme chemistry to proteomic chemistry. Annu Rev Biochem 77:383–414. https://doi.org/10.1146/annurev.biochem.75.101304.124125
Cunningham M, Gilkeson G (2011) Estrogen receptors in immunity and autoimmunity. Clin Rev Allergy Immunol 40:66–73. https://doi.org/10.1007/s12016-010-8203-5
Eleftheriadis N, Thee SA, Zwinderman MRH et al (2016) Activity-based probes for 15-lipoxygenase-1. Angew Chemie Int Ed 55:12300–12305. https://doi.org/10.1002/anie.201606876
Fahy E, Subramaniam S, Murphy RC et al (2009) Update of the LIPID MAPS comprehensive classification system for lipids. J Lipid Res 50(Suppl):S9–S14. https://doi.org/10.1194/jlr.R800095-JLR200
Fahy E, Cotter D, Sud M, Subramaniam S (2011) Lipid classification, structures and tools. Biochim Biophys Acta 1811:637–647. https://doi.org/10.1016/j.bbalip.2011.06.009
Furman D (2015) Sexual dimorphism in immunity: improving our understanding of vaccine immune responses in men. Expert Rev Vaccines 14:461–471
Gaebler A, Milan R, Straub L et al (2013) Alkyne lipids as substrates for click chemistry-based in vitro enzymatic assays. J Lipid Res 54:2282–2290. https://doi.org/10.1194/jlr.D038653
Gaebler A, Penno A, Kuerschner L, Thiele C (2016) A highly sensitive protocol for microscopy of alkyne lipids and fluorescently tagged or immunostained proteins. J Lipid Res 57:1934–1947. https://doi.org/10.1194/jlr.D070565
Gu X, Huang Y, Levison BS et al (2016) Identification of critical paraoxonase 1 residues involved in high density lipoprotein interaction. J Biol Chem 291:1890–1904. https://doi.org/10.1074/jbc.M115.678334
Gubbens J, Ruijter E, de Fays LEV et al (2009) Photocrosslinking and click chemistry enable the specific detection of proteins interacting with phospholipids at the membrane interface. Chem Biol 16:3–14. https://doi.org/10.1016/j.chembiol.2008.11.009
Guo H, Xu J, Hao P et al (2017) Competitive affinity-based proteome profiling and imaging to reveal potential cellular targets of betulinic acid. Chem Commun 53:9620–9623. https://doi.org/10.1039/C7CC04190J
Haberkant P, Schmitt O, Contreras F-X et al (2008) Protein-sphingolipid interactions within cellular membranes. J Lipid Res 49:251–262. https://doi.org/10.1194/jlr.D700023-JLR200
Haberkant P, Raijmakers R, Wildwater M et al (2013) In vivo profiling and visualization of cellular protein-lipid interactions using bifunctional fatty acids. Angew Chemie Int Ed 52:4033–4038. https://doi.org/10.1002/anie.201210178
Haberkant P, Stein F, Höglinger D et al (2016) Bifunctional sphingosine for cell-based analysis of protein-sphingolipid interactions. ACS Chem Biol 11:222–230. https://doi.org/10.1021/acschembio.5b00810
Hein JE, Fokin VV (2010) Copper-catalyzed azide-alkyne cycloaddition (CuAAC) and beyond: new reactivity of copper(I) acetylides. Chem Soc Rev 39:1302–1315
Herner A, Marjanovic J, Lewandowski TM et al (2016) 2-Aryl-5-carboxytetrazole as a new photoaffinity label for drug target identification. J Am Chem Soc 138:14609–14615. https://doi.org/10.1021/jacs.6b06645
Hofmann K, Thiele C, Schött H-F et al (2014) A novel alkyne cholesterol to trace cellular cholesterol metabolism and localization. J Lipid Res 55:583–591. https://doi.org/10.1194/jlr.D044727
Höglinger D, Nadler A, Haberkant P et al (2017) Trifunctional lipid probes for comprehensive studies of single lipid species in living cells. Proc Natl Acad Sci 114:1566–1571. https://doi.org/10.1073/pnas.1611096114
Homo-Delarche F, Fitzpatrick F, Christeff N et al (1991) Sex steroids, glucocorticoids, stress and autoimmunity. J Steroid Biochem Mol Biol 40:619–637. https://doi.org/10.1016/0960-0760(91)90285-D
Hsu KL, Tsuboi K, Adibekian A et al (2012) DAGLβ inhibition perturbs a lipid network involved in macrophage inflammatory responses. Nat Chem Biol. https://doi.org/10.1038/nchembio.1105
Hulce JJ, Cognetta AB, Niphakis MJ et al (2013) Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells. Nat Methods 10:259–264. https://doi.org/10.1038/nmeth.2368
Jahng WJ, David C, Nesnas N et al (2003a) A cleavable affinity biotinylating agent reveals a retinoid binding role for RPE65. Biochemistry 42:6159–6168. https://doi.org/10.1021/bi034002i
Jahng WJ, Xue L, Rando RR (2003b) Lecithin retinol acyltransferase is a founder member of a novel family of enzymes. Biochemistry 42:12805–12812. https://doi.org/10.1021/bi035370p
Kallemeijn WW, Li KY, Witte MD et al (2012) Novel activity-based probes for broad-spectrum profiling of retaining β-exoglucosidases in situ and in vivo. Angew Chemie Int Ed 51:12529–12533. https://doi.org/10.1002/anie.201207771
Kleiner P, Heydenreuter W, Stahl M et al (2017) A whole proteome inventory of background photocrosslinker binding. Angew Chemie Int Ed 56:1396–1401. https://doi.org/10.1002/anie.201605993
Lai JJ, Lai KP, Zeng W et al (2012) Androgen receptor influences on body defense system via modulation of innate and adaptive immune systems: lessons from conditional AR knockout mice. Am J Pathol 181:1504–1512
Lee KSS, Henriksen NM, Ng CJ et al (2017) Probing the orientation of inhibitor and epoxy-eicosatrienoic acid binding in the active site of soluble epoxide hydrolase. Arch Biochem Biophys 613:1–11. https://doi.org/10.1016/j.abb.2016.10.017
Lentz CS, Sheldon JR, Crawford LA et al (2018) Identification of a S. aureus virulence factor by activity-based protein profiling (ABPP) article. Nat Chem Biol 14:609–617. https://doi.org/10.1038/s41589-018-0060-1
Li Z, Hao P, Li L et al (2013) Design and synthesis of minimalist terminal alkyne-containing diazirine photo-crosslinkers and their incorporation into kinase inhibitors for cell- and tissue-based proteome profiling. Angew Chemie Int Ed 52:8551–8556. https://doi.org/10.1002/anie.201300683
Liu Y, Patricelli MP, Cravatt BF (1999) Activity-based protein profiling: the serine hydrolases. Proc Natl Acad Sci 96:14694–14699. https://doi.org/10.1073/pnas.96.26.14694
Liu X, Dong T, Zhou Y et al (2016) Exploring the binding proteins of glycolipids with bifunctional chemical probes. Angew Chemie Int Ed 55:14330–14334. https://doi.org/10.1002/anie.201608827
Long JZ, Cravatt BF (2011) The metabolic serine hydrolases and their functions in mammalian physiology and disease. Chem Rev 111:6022–6063
Lum KM, Sato Y, Beyer BA et al (2017) Mapping protein targets of bioactive small molecules using lipid-based chemical proteomics. ACS Chem Biol 12:2671–2681. https://doi.org/10.1021/acschembio.7b00581
Marshall-Gradisnik S, Green R, Brenu E, Weatherby R (2009) Anabolic androgenic steroids effects on the immune system: a review. Open Life Sci 4:19–33. https://doi.org/10.2478/s11535-008-0058-x
Mellacheruvu D, Wright Z, Couzens AL et al (2013) The CRAPome: a contaminant repository for affinity purification-mass spectrometry data. Nat Methods 10:730–736. https://doi.org/10.1038/nmeth.2557
Mora JR, Iwata M, Von Andrian UH (2008) Vitamin effects on the immune system. Nat Rev Immunol 8:685–698. https://doi.org/10.1038/nri2378.Vitamin
Moriguchi S (1998) The role of vitamin E in T-cell differentiation and the decrease of cellular immunity with aging. BioFactors 7:77–86. https://doi.org/10.1002/biof.5520070111
Moriguchi S, Kaneyasu M (2003) Role of Vitamin E in immune system. Ser Rev JClin Biochem 34:97–109
Nadler A, Reither G, Feng S et al (2013) The fatty acid composition of diacylglycerols determines local signaling patterns. Angew Chemie Int Ed 52:6330–6334. https://doi.org/10.1002/anie.201301716
Nesnas N, Rando RR, Nakanishi K (2002) Synthesis of biotinylated retinoids for cross-linking and isolation of retinol binding proteins. Tetrahedron 58:6577–6584. https://doi.org/10.1016/S0040-4020(02)00667-1
Niphakis MJ, Lum KM, Cognetta AB et al (2015) A global map of lipid-binding proteins and their ligandability in cells. Cell 161:1668–1680. https://doi.org/10.1016/j.cell.2015.05.045
Norman AW, Mizwicki MT, Norman DPG (2004) Steroid-hormone rapid actions, membrane receptors and a conformational ensemble model. Nat Rev Drug Discov. https://doi.org/10.1038/nrd1283
Ogasawara D, Deng H, Viader A et al (2016) Rapid and profound rewiring of brain lipid signaling networks by acute diacylglycerol lipase inhibition. Proc Natl Acad Sci 113:26–33. https://doi.org/10.1073/pnas.1522364112
Ogawa N, Sugiyama T, Morita M et al (2017) Total synthesis of resolvin D5. J Org Chem 82:2032–2039. https://doi.org/10.1021/acs.joc.6b02870
Ouairy CMJ, Ferraz MJ, Boot RG et al (2015) Development of an acid ceramidase activity-based probe. Chem Commun 51:6161–6163. https://doi.org/10.1039/C5CC00356C
Ourailidou ME, van der Meer J-Y, Baas B-J et al (2014) Aqueous oxidative heck reaction as a protein-labeling strategy. ChemBioChem 15:209–212. https://doi.org/10.1002/cbic.201300714
Pacher P, Mechoulam R (2011) Is lipid signaling through cannabinoid 2 receptors part of a protective system? Prog Lipid Res 50:193–211. https://doi.org/10.1016/j.plipres.2011.01.001
Pandey R, Mousawy K, Nagarkatti M, Nagarkatti P (2009) Endocannabinoids and immune regulation. Pharmacol Res 60:85–92. https://doi.org/10.1016/j.phrs.2009.03.019
Peng T, Hang HC (2015) Bifunctional fatty acid chemical reporter for analyzing S-palmitoylated membrane protein-protein interactions in mammalian cells. J Am Chem Soc 137:556–559. https://doi.org/10.1021/ja502109n
Peng T, Yuan X, Hang HC (2014) Turning the spotlight on protein-lipid interactions in cells. Curr Opin Chem Biol 21:144–153. https://doi.org/10.1016/j.cbpa.2014.07.015
Petracca R, Romeo E, Baggelaar MP et al (2017) Novel activity-based probes for N-acylethanolamine acid amidase. Chem Commun 53:11810–11813. https://doi.org/10.1039/C7CC06838G
Pike LJ (2003) Lipid rafts. J Lipid Res 44:655–667. https://doi.org/10.1194/jlr.R200021-JLR200
Ray R, Bouillon R, Van Baelen H, Holick MF (1991) Synthesis of 25-hydroxyvitamin D3 3β-3′-[N-(4-azido-2-nitrophenyl)amino]propyl ether, a second-generation photoaffinity analogue of 25-hydroxyvitamin D3: photoaffinity labeling of rat serum vitamin D binding protein. Biochemistry 30:4809–4813. https://doi.org/10.1021/bi00233a024
Robichaud PP, Poirier SJ, Boudreau LH et al (2016) On the cellular metabolism of the click chemistry probe 19-alkyne arachidonic acid. J Lipid Res 57:1821–1830. https://doi.org/10.1194/jlr.M067637
Rodriguez AR, Spur BW (2017) First total synthesis of pro-resolving and tissue-regenerative resolvin sulfido-conjugates. Tetrahedron Lett 58:1662–1668. https://doi.org/10.1016/J.TETLET.2017.03.041
Romeo E, Ponzano S, Armirotti A et al (2015) Activity-based probe for N-acylethanolamine acid amidase. ACS Chem Biol 10:2057–2064. https://doi.org/10.1021/acschembio.5b00197
Rowland MM, Bostic HE, Gong D et al (2011) Phosphatidylinositol 3,4,5-trisphosphate activity probes for the labeling and proteomic characterization of protein binding partners. Biochemistry 50:11143–11161. https://doi.org/10.1021/bi201636s
Sakurai K, Ozawa S, Yamada R et al (2014) Comparison of the reactivity of carbohydrate photoaffinity probes with different photoreactive groups. ChemBioChem 15:1399–1403. https://doi.org/10.1002/cbic.201402051
Serhan CN, Petasis NA (2011) Resolvins and protectins in inflammation resolution. Chem Rev 111:5922–5943. https://doi.org/10.1021/cr100396c
Shimazawa R, Sanda R, Mizoguchi H et al (1991) Fluorescent and photoaffinity labeling probes for retinoic acid receptors. Biochem Biophys Res Commun 179:259–265. https://doi.org/10.1016/0006-291X(91)91363-H
Simon GM, Cravatt BF (2010) Activity-based proteomics of enzyme superfamilies: serine hydrolases as a case study. J Biol Chem 285:11051–11055
Soethoudt M, Stolze SC, Westphal MV et al (2018) Selective photoaffinity probe that enables assessment of cannabinoid CB2Receptor expression and ligand engagement in human cells. J Am Chem Soc 140:6067–6075. https://doi.org/10.1021/jacs.7b11281
Soontjens CD, Rafter JJ, Gustafsson JÅ (1996) Ligands for orphan receptors? J Endocrinol 150:241–257
Swamy N, Addo J, Vskokovic MR, Ray R (2000a) Probing the vitamin D sterol-binding pocket of human vitamin D-binding protein with bromoacetate affinity labeling reagents containing the affinity probe at C-3, C-6, C-11, and C-19 positions of parent vitamin D sterols. Arch Biochem Biophys 373:471–478. https://doi.org/10.1006/ABBI.1999.1537
Swamy N, Xu W, Paz N et al (2000b) Molecular modeling, affinity labeling, and site-directed mutagenesis define the key points of interaction between the ligand-binding domain of the vitamin D nuclear receptor and 1α,25-dihydroxyvitamin D3. Biochemistry 39:12162–12171. https://doi.org/10.1021/bi0002131
Tate EW, Kalesh KA, Lanyon-Hogg T et al (2015) Global profiling of protein lipidation using chemical proteomic technologies. Curr Opin Chem Biol 24:48–57. https://doi.org/10.1016/j.cbpa.2014.10.016
Trigunaite A, Dimo J (2015) Suppressive effects of androgens on the immune system. Cell Immunol 294:87–94. https://doi.org/10.1016/J.CELLIMM.2015.02.004
Tully SE, Cravatt BF (2010) Activity-based probes that target functional subclasses of phospholipases in proteomes. J Am Chem Soc 132:3264–3265. https://doi.org/10.1021/ja1000505
Turcotte C, Blanchet MR, Laviolette M, Flamand N (2016) The CB2 receptor and its role as a regulator of inflammation. Cell Mol Life Sci 73:4449–4470
Ulivi V, Lenti M, Gentili C et al (2011) Anti-inflammatory activity of monogalactosyldiacylglycerol in human articular cartilage in vitro: Activation of an anti-inflammatory cyclooxygenase-2 (COX-2) pathway. Arthritis Res Ther 13:R92. https://doi.org/10.1186/ar3367
Van Esbroeck ACM, Janssen APA, Cognetta AB et al (2017) Activity-based protein profiling reveals off-target proteins of the FAAH inhibitor BIA 10-2474. Science (80–)356:1084–1087. https://doi.org/10.1126/science.aaf7497
van Rooden EJ, van Esbroeck ACM, Baggelaar MP et al (2018) Chemical proteomics analysis of endocannabinoid hydrolase activity in Niemann-Pick Type C mouse brain. Manuscr Submitt 12. https://doi.org/10.3389/fnins.2018.00440
Vane JR (1971) Inhibition of prostaglandin synthesis as a mechanism of action for aspirin-like drugs. Nat New Biol 231:232–235. https://doi.org/10.1038/newbio231232a0
Waldmann H, Ahmed SA, Khan D (2016) The immune System is a natural target for estrogen action: opposing effects of estrogen in two prototypical autoimmune diseases. Front Immunol 6:6353389–6353635. https://doi.org/10.3389/fimmu.2015.00635
Wang D, Du S, Cazenave-Gassiot A et al (2017) Global mapping of protein-lipid interactions by using modified choline-containing phospholipids metabolically synthesized in live cells. Angew Chemie Int Ed 56:5829–5833. https://doi.org/10.1002/anie.201702509
Weerapana E, Speers AE, Cravatt BF (2007) Tandem orthogonal proteolysis-activity-based protein profiling (TOP-ABPP)—a general method for mapping sites of probe modification in proteomes. Nat Protoc 2:1414–1425. https://doi.org/10.1038/nprot.2007.194
Weller MG (2016) Quality issues of research antibodies. Anal Chem Insights 2016:21–27. https://doi.org/10.4137/Aci.s31614
Wenk MR (2005) The emerging field of lipidomics. Nat Rev Drug Discov 4:594–610. https://doi.org/10.1038/nrd1776
Wenk MR (2010) Lipidomics: new tools and applications. Cell 143:888–895. https://doi.org/10.1016/j.cell.2010.11.033
Witte MD, Kallemeijn WW, Aten J et al (2010) Ultrasensitive in situ visualization of active glucocerebrosidase molecules. Nat Chem Biol 6:907–913. https://doi.org/10.1038/nchembio.466
Wright MH, Paape D, Storck EM et al (2015) Global analysis of protein N-myristoylation and exploration of N-myristoyltransferase as a drug target in the neglected human pathogen leishmania donovani. Chem Biol 22:342–354. https://doi.org/10.1016/j.chembiol.2015.01.003
Wright MH, Sieber SA (2016) Chemical proteomics approaches for identifying the cellular targets of natural products. Nat Prod Rep 33:681–708. https://doi.org/10.1039/C6NP00001K
Xia Y, Peng L (2013) Photoactivatable lipid probes for studying biomembranes by photoaffinity labeling. Chem Rev 113:7880–7929. https://doi.org/10.1021/cr300419p
Yang K, Han X (2016) Lipidomics: techniques, applications, and outcomes related to biomedical sciences. Trends Biochem Sci 41:954–969
Yeagle PL (2016) The membranes of cells. Academic Press
Zhang L, Zhang Y, Dong J et al (2012) Design and synthesis of novel photoaffinity probes for study of the target proteins of oleanolic acid. Bioorganic Med Chem Lett 22:1036–1039. https://doi.org/10.1016/j.bmcl.2011.11.123
Zhou H, Hylemon PB (2014) Bile acids are nutrient signaling hormones. Steroids 86:62–68
Zhuang S, Li Q, Cai L et al (2017) Chemoproteomic profiling of bile acid interacting proteins. ACS Cent Sci 3:501–509. https://doi.org/10.1021/acscentsci.7b00134
Zweerink S, Kallnik V, Ninck S et al (2017) Activity-based protein profiling as a robust method for enzyme identification and screening in extremophilic Archaea. Nat Commun 8:15352. https://doi.org/10.1038/ncomms15352
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Supplementary
Supplementary
List of proteins identified as promiscuous lipid-binding proteins. The count shows the amount of experiments in which the protein was identified as a probe target. Proteins colored red are the proteins flagged by the CRAPome database.
Rights and permissions
Copyright information
© 2018 Springer Nature Switzerland AG
About this chapter
Cite this chapter
Koenders, S.T.A., Gagestein, B., van der Stelt, M. (2018). Opportunities for Lipid-Based Probes in the Field of Immunology. In: Cravatt, B., Hsu, KL., Weerapana, E. (eds) Activity-Based Protein Profiling. Current Topics in Microbiology and Immunology, vol 420. Springer, Cham. https://doi.org/10.1007/82_2018_127
Download citation
DOI: https://doi.org/10.1007/82_2018_127
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-11142-7
Online ISBN: 978-3-030-11143-4
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)