6. Appendix
6.1. Literature
Abramson, S., Hoffstein, S.T., and Weissmann, G. (1982). Superoxide anion generation by human neutrophils exposed to monosodium urate. effect of protein adsorption and complement activation. Arthritis Rheum. 25, 174–180.
An, L.L., Mehta, P., Xu, L., Turman, S., Reimer, T., Naiman, B., Connor, J., Sanjuan, M., Kolbeck, R., and Fung, M. (2014). Complement C5a potentiates uric acid crystal-induced IL-1β production. Eur. J. Immunol. 44, 3669–3679.
Arredouani, M.S., Palecanda, A., Koziel, H., Huang, Y.-C., Imrich, A., Sulahian, T.H., Ning, Y.Y., Yang, Z., Pikkarainen, T., Sankala, M., et al. (2005). MARCO Is the Major Binding Receptor for Unopsonized Particles and Bacteria on Human Alveolar Macrophages. J. Immunol.
175, 6058–6064.
Barabé, F., Gilbert, C., Liao, N., Bourgoin, S.G., and Naccache, P.H. (1998). Crystal-induced neutrophil activation VI. Involvement of FcγRIIIB (CD16) and CD11b in response to inflammatory microcrystals. FASEB J. 12, 209–220.
Bencardino, J.T., and Hassankhani, A. (2003). Calcium pyrophosphate dihydrate crystal deposition disease. Semin. Musculoskelet. Radiol. 7, 175–185.
Bianchetti, M.G., Roduit, C., and Oetliker, O.H. (1991). Acyclovir-induced renal failure: course and risk factors. Pediatr. Nephrol. 5, 238–239.
Brand, K., Eisele, T., Kreusel, U., Page, M., Page, S., Haas, M., Gerling, A., Kaltschmidt, C., Neumann, F.-J., Mackman, N., et al. (1997). Dysregulation of Monocytic Nuclear Factor-κB by Oxidized Low-Density Lipoprotein. Arterioscler. Thromb. Vasc. Biol. 17, 1901–1909.
Brown, M.S., and Goldstein, J.L. (1984). How LDL receptors influence cholesterol and atherosclerosis. Sci. Am. 251, 58–66.
Broz, P., and Dixit, V.M. (2016). Inflammasomes: Mechanism of assembly, regulation and signalling. Nat. Rev. Immunol. 16, 407–420.
Byers, P.H., Ward, P.A., Kellermeyer, R.W., and Naff, G.B. (1973). Complement as a mediator of inflammation in acute gouty arthritis. II. Biological activities generated from complement by the interaction of serum complement and sodium urate crystals. J. Lab. Clin. Med. 81, 761–769.
Coronado, L.M., Nadovich, C.T., and Spadafora, C. (2014). Malarial hemozoin: From target to tool. Biochim. Biophys. Acta - Gen. Subj. 1840, 2032–2041.
Dalbeth, N., Merriman, T.R., and Stamp, L.K. (2016). Gout. Lancet 388, 2039–2052.
Duewell, P., Kono, H., Rayner, K.J., Sirois, C.M., Vladimer, G., Bauernfeind, F.G., Abela, G.S., Franchi, L., Nũez, G., Schnurr, M., et al. (2010). NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals. Nature 464, 1357–1361.
Elshourbagy, N.A., Li, X., Terrett, J., VanHorn, S., Gross, M.S., Adamou, J.E., Anderson, K.M., Webb, C.L., and Lysko, P.G. (2000). Molecular characterization of a human scavenger receptor, human MARCO. Eur. J. Biochem. 267, 919–926.
27 Flajnik, M.F. (2018). A cold-blooded view of adaptive immunity. Nat. Rev. Immunol. 18, 438– 453.
Franklin, B.S., Mangan, M.S., and Latz, E. (2016). Crystal Formation in Inflammation. Annu.
Rev. Immunol. 34, 173–202.
Hardison, S.E., and Brown, G.D. (2012). C-type lectin receptors orchestrate antifungal immunity.
Nat. Immunol. 13, 817–822.
Hari, A., Zhang, Y., Tu, Z., Detampel, P., Stenner, M., Ganguly, A., and Shi, Y. (2014).
Activation of NLRP3 inflammasome by crystalline structures via cell surface contact. Sci. Rep. 4, 7281.
Hernanz-Falcón, P., Joffre, O., Williams, D.L., and Reis e Sousa, C. (2009). Internalization of Dectin-1 terminates induction of inflammatory responses. Eur. J. Immunol. 39, 507–513.
Hnizdo, E., and Vallyathan, V. (2003). Chronic obstructive pulmonary disease due to occupational exposure to silica dust: A review of epidemiological and pathological evidence.
Occup. Environ. Med. 60, 237–243.
Honarpisheh, M., Foresto-Neto, O., Desai, J., Steiger, S., Gómez, L.A., Popper, B., Boor, P., Anders, H.J., and Mulay, S.R. (2017). Phagocytosis of environmental or metabolic crystalline particles induces cytotoxicity by triggering necroptosis across a broad range of particle size and shape. Sci. Rep. 7, 15523.
Hornung, V., Bauernfeind, F., Halle, A., Samstad, E.O., Kono, H., Rock, K.L., Fitzgerald, K.A., and Latz, E. (2008). Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat. Immunol. 9, 847–856.
Hui, M., Carr, A., Cameron, S., Davenport, G., Doherty, M., Forrester, H., Jenkins, W., Jordan, K.M., Mallen, C.D., McDonald, T.M., et al. (2017). The British Society For Rheumatology guideline for the management of gout. Rheumatol. (United Kingdom) 56, e1–e20.
Inouye, H., Fraser, P.E., and Kirschner, D.A. (1993). Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction. Biophys. J.
64, 502–519.
Kayagaki, N., Stowe, I.B., Lee, B.L., O’Rourke, K., Anderson, K., Warming, S., Cuellar, T., Haley, B., Roose-Girma, M., Phung, Q.T., et al. (2015). Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling. Nature 526, 666–671.
Kiyotake, R., Oh-Hora, M., Ishikawa, E., Miyamoto, T., Ishibashi, T., and Yamasaki, S. (2015).
Human Mincle Binds to Cholesterol Crystals and Triggers Innate Immune Responses. J. Biol.
Chem. 290, 25322–25332.
Kushiyama, A., Nakatsu, Y., Matsunaga, Y., Yamamotoya, T., Mori, K., Ueda, K., Inoue, Y., Sakoda, H., Fujishiro, M., Ono, H., et al. (2016). Role of uric acid metabolism-related inflammation in the pathogenesis of metabolic syndrome components such as atherosclerosis and nonalcoholic steatohepatitis. Mediators Inflamm. 2016, 8603164.
Landis, R.C., Yagnik, D.R., Florey, O., Philippidis, P., Emons, V., Mason, J.C., and Haskard, D.O. (2002). Safe disposal of inflammatory monosodium urate monohydrate crystals by differentiated macrophages. Arthritis Rheum. 46, 3026–3033.
Lee, J.H., Yang, J.A., Shin, K., Lee, G.H., Lee, W.W., Lee, E.Y., Song, Y.W., Lee, E.B., and Park, J.K. (2017). Elderly patients exhibit stronger inflammatory responses during gout attacks. J.
Korean Med. Sci. 32, 1967–1973.
Li, K., Neumann, K., Duhan, V., Namineni, S., Hansen, A.L., Wartewig, T., Kurgyis, Z., Holm, C.K., Heikenwalder, M., Lang, K.S., et al. (2019). The uric acid crystal receptor Clec12A potentiates type I interferon responses. Proc. Natl. Acad. Sci. U. S. A. 116, 18544–18549.
Li, Y., Cao, X., Liu, Y., Zhao, Y., and Herrmann, M. (2018). Neutrophil extracellular traps formation and aggregation orchestrate induction and resolution of sterile crystal-mediated inflammation. Front. Immunol. 9, 1559.
Martinon, F., Burns, K., and Tschopp, J. (2002). The Inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-β. Mol. Cell 10, 417–426.
Martinon, F., Pétrilli, V., Mayor, A., Tardivel, A., and Tschopp, J. (2006). Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 440, 237–241.
Martinon, F., Mayor, A., and Tschopp, J. (2009). The inflammasomes: Guardians of the body.
Annu. Rev. Immunol. 27, 229–265.
Mbikay, M., Mayne, J., and Chrétien, M. (2020). The enigma of soluble LDLR: Could inflammation be the key? Lipids Health Dis. 19, 17.
Merriman, T.R. Pathophysiology of gout. UpToDate database.
https://www.uptodate.com/contents/pathophysiology-of-gout [accessed August 04, 2020].
Mitroulis, I., Kambas, K., Chrysanthopoulou, A., Skendros, P., Apostolidou, E., Kourtzelis, I., Drosos, G.I., Boumpas, D.T., and Ritis, K. (2011). Neutrophil extracellular trap formation is associated with IL-1β and autophagy-related signaling in gout. PLoS One 6, e29318.
Von Moltke, J., Trinidad, N.J., Moayeri, M., Kintzer, A.F., Wang, S.B., Van Rooijen, N., Brown, C.R., Krantz, B.A., Leppla, S.H., Gronert, K., et al. (2012). Rapid induction of inflammatory lipid mediators by the inflammasome in vivo. Nature 490, 107–111.
Mu, L., Tu, Z., Miao, L., Ruan, H., Kang, N., Hei, Y., Chen, J., Wei, W., Gong, F., Wang, B., et al. (2018). A phosphatidylinositol 4,5-bisphosphate redistribution-based sensing mechanism initiates a phagocytosis programing. Nat. Commun. 9, 4259.
Mulay, S.R., and Anders, H.-J. (2016). Crystallopathies. N. Engl. J. Med. 374, 2465–2476.
Mulay, S.R., Desai, J., Kumar, S. V., Eberhard, J.N., Thomasova, D., Romoli, S., Grigorescu, M., Kulkarni, O.P., Popper, B., Vielhauer, V., et al. (2016). Cytotoxicity of crystals involves RIPK3-MLKL-mediated necroptosis. Nat. Commun. 7, 10274.
Mulay, S.R., Steiger, S., Shi, C., and Anders, H.J. (2020). A guide to crystal-related and nano- or microparticle-related tissue responses. FEBS J. 287, 818–832.
Muñoz, L.E., Boeltz, S., Bilyy, R., Schauer, C., Mahajan, A., Widulin, N., Grüneboom, A., Herrmann, I., Boada, E., Rauh, M., et al. (2019). Neutrophil Extracellular Traps Initiate Gallstone Formation. Immunity 51, 443–450.e4.
Naff, G.B., and Byers, P.H. (1973). Complement as a mediator of inflammation in acute gouty arthritis. I. Studies on the reaction between human serum complement and sodium urate crystals.
J. Lab. Clin. Med. 81, 747–760.
Neumann, K., Castiñeiras-Vilariño, M., Höckendorf, U., Hannesschläger, N., Lemeer, S., Kupka, D., Meyermann, S., Lech, M., Anders, H.J., Kuster, B., et al. (2014). Clec12a is an inhibitory receptor for uric acid crystals that regulates inflammation in response to cell death. Immunity 40, 389–399.
29 Neyen, C., Plüddemann, A., Roversi, P., Thomas, B., Cai, L., Van Der Westhuyzen, D.R., Sim, R.B., and Gordon, S. (2009). Macrophage scavenger receptor a mediates adhesion to apolipoproteins A-I and E. Biochemistry 48, 11858–11871.
Ng, G., Sharma, K., Ward, S.M., Desrosiers, M.D., Stephens, L.A., Schoel, W.M., Li, T., Lowell, C.A., Ling, C.C., Amrein, M.W., et al. (2008). Receptor-Independent, Direct Membrane Binding Leads to Cell-Surface Lipid Sorting and Syk Kinase Activation in Dendritic Cells. Immunity 29, 807–818.
Ng, P.M.L., Le Saux, A., Lee, C.M., Tan, N.S., Lu, J., Thiel, S., Ho, B., and Ding, J.L. (2007). C-reactive protein collaborates with plasma lectins to boost immune response against bacteria.
EMBO J. 26, 3431–3440.
Noris, M., and Remuzzi, G. (2013). Overview of complement activation and regulation. Semin.
Nephrol. 33, 479–492.
Pétrilli, V., Papin, S., Dostert, C., Mayor, A., Martinon, F., and Tschopp, J. (2007). Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration. Cell Death Differ. 14, 1583–1589.
Piedrahita, J.A., Zhang, S.H., Hagaman, J.R., Oliver, P.M., and Maeda, N. (1992). Generation of mice carrying a mutant apolipoprotein E gene inactivated by gene targeting in embryonic stem cells. Proc. Natl. Acad. Sci. U. S. A. 89, 4471–4475.
Poloni, L.N., and Ward, M.D. (2014). The materials science of pathological crystals. Chem.
Mater. 26, 477–495.
Portincasa, P., Moschetta, A., and Palasciano, G. (2006). Cholesterol gallstone disease. Lancet 368, 230–239.
Raulf, M.K., Johannssen, T., Matthiesen, S., Neumann, K., Hachenberg, S., Mayer-Lambertz, S., Steinbeis, F., Hegermann, J., Seeberger, P.H., Baumgärtner, W., et al. (2019). The C-type Lectin Receptor CLEC12A Recognizes Plasmodial Hemozoin and Contributes to Cerebral Malaria Development. Cell Rep. 28, 30–38.e5.
Reis, E.S., Mastellos, D.C., Hajishengallis, G., and Lambris, J.D. (2019). New insights into the immune functions of complement. Nat. Rev. Immunol. 19, 503–516.
Richette, P., and Bardin, T. (2010). Gout. Lancet 375, 318–328.
Ricklin, D., Reis, E.S., and Lambris, J.D. (2016). Complement in disease: a defence system turning offensive. Nat. Rev. Nephrol. 12, 383–401.
Rosas, M., Liddiard, K., Kimberg, M., Faro-Trindade, I., McDonald, J.U., Williams, D.L., Brown, G.D., and Taylor, P.R. (2008). The Induction of Inflammation by Dectin-1 In Vivo Is Dependent on Myeloid Cell Programming and the Progression of Phagocytosis. J. Immunol. 181, 3549–3557.
Rosenthal, A.K. Clinical manifestations and diagnosis of calcium pyrophosphate crystal deposition (CPPD) disease. UpToDate database. https://www.uptodate.com/contents/clinical-manifestations-and-diagnosis-of-calcium-pyrophosphate-crystal-deposition-cppd-disease.
[accessed August 04, 2020]
Schorn, C., Janko, C., Latzko, M., Chaurio, R., Schett, G., and Herrmann, M. (2012).
Monosodium urate crystals induce extracellular DNA traps in neutrophils, eosinophils, and basophils but not in mononuclear cells. Front. Immunol. 3, 277.
Scott, P., Ma, H., Viriyakosol, S., Terkeltaub, R., and Liu-Bryan, R. (2006). Engagement of CD14 Mediates the Inflammatory Potential of Monosodium Urate Crystals. J. Immunol. 177, 6370–
6378.
Shi, J., Zhao, Y., Wang, K., Shi, X., Wang, Y., Huang, H., Zhuang, Y., Cai, T., Wang, F., and Shao, F. (2015). Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death.
Nature 526, 660–665.
Shi, Y., Evans, J.E., and Rock, K.L. (2003). Molecular identification of a danger signal that alerts the immune system to dying cells. Nature 425, 516–521.
Sonnenberg, G.F., and Hepworth, M.R. (2019). Functional interactions between innate lymphoid cells and adaptive immunity. Nat. Rev. Immunol. 19, 599–613.
Spillantini, M.G., Schmidt, M.L., Lee, V.M.Y., Trojanowski, J.Q., Jakes, R., and Goedert, M.
(1997). α-synuclein in Lewy bodies [8]. Nature 388, 839–840.
Stewart, C.R., Stuart, L.M., Wilkinson, K., Van Gils, J.M., Deng, J., Halle, A., Rayner, K.J., Boyer, L., Zhong, R., Frazier, W.A., et al. (2010). CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer. Nat. Immunol. 11, 155–161.
Struglics, A., Okroj, M., Swärd, P., Frobell, R., Saxne, T., Lohmander, L.S., and Blom, A.M.
(2016). The complement system is activated in synovial fluid from subjects with knee injury and from patients with osteoarthritis. Arthritis Res. Ther. 18, 223.
Suresh, M. V., Singh, S.K., Ferguson, D.A., and Agrawal, A. (2006). Role of the Property of C-Reactive Protein to Activate the Classical Pathway of Complement in Protecting Mice from Pneumococcal Infection. J. Immunol. 176, 4369–4374.
Tausche, A.K., Jansen, T.L., Schröder, H.E., Bornstein, S.R., Aringer, M., and Müller-Ladner, U.
(2009). Gicht - Aktuelle Aspekte in Diagnostik und Therapie. Dtsch. Arztebl. 106, 549–555.
Terkeltaub, R., Tenner, A.J., Kozin, F., and Ginsberg, M.H. (1983). Plasma Protein Binding by Monosodium Urate Crystals. Arthritis Rheum. 26, 775–783.
Terkeltaub, R., Curtiss, L.K., Tenner, A.J., and Ginsberg, M.H. (1984). Lipoproteins containing apoprotein B are a major regulator of neutrophil responses to monosodium urate crystals. J. Clin.
Invest. 73, 1719–1730.
Terkeltaub, R., Martin, J., Curtiss, L.K., and Ginsberg, M.H. (1986). Apolipoprotein B mediates the capacity of low density lipoprotein to suppress neutrophil stimulation by particulates. J. Biol.
Chem. 261, 15662–15667.
Terkeltaub, R.A., Dyer, C.A., Martin, J., and Curtiss, L.K. (1991). Apolipoprotein (apo) E inhibits the capacity of monosodium urate crystals to stimulate neutrophils. Characterization of intraarticular apo E and demonstration of apo E binding to urate crystals in vivo. J. Clin. Invest.
87, 20–26.
Thakur, S.A., Beamer, C.A., Migliaccio, C.T., and Holian, A. (2009). Critical role of MARCO in crystalline silica-induced pulmonary inflammation. Toxicol. Sci. 108, 462–471.
Thefeld, W., Hoffmeister, H., Busch, E.W., Koller, P.U., and Vollmar, J. (1973). Normalwerte der Serumharnsäure in Abhängigkeit von Alter und Geschlecht mit einem neuen enzymatischen Harnsäurefarbtest. Dtsch. Medizinische Wochenschrift 98, 380–384.
31 Thomas, P.G., Dash, P., Aldridge, J.R., Ellebedy, A.H., Reynolds, C., Funk, A.J., Martin, W.J., Lamkanfi, M., Webby, R.J., Boyd, K.L., et al. (2009). The Intracellular Sensor NLRP3 Mediates Key Innate and Healing Responses to Influenza A Virus via the Regulation of Caspase-1.
Immunity 30, 566–575.
Udensi, U., and Tchounwou, P. (2017). Potassium homeostasis, oxidative stress, and human disease. Int. J. Clin. Exp. Physiol. 4, 111-122.
Uniprot database. MARCO_HUMAN (2020). https://www.uniprot.org/uniprot/Q9UEW3664 [accessed July 27, 2020].
Verschoor, A., Kemper, C., and Köhl, J. (2017). Complement Receptors. In eLS, John Wiley &
Sons, Ltd (Ed.), doi:10.1002/9780470015902.a0000512.pub3.
Zelensky, A.N., and Gready, J.E. (2005). The C-type lectin-like domain superfamily. FEBS J.
272, 6179–6217.
Zhang, W., Doherty, M., Bardin, T., Pascual, E., Barskova, V., Conaghan, P., Gerster, J., Jacobs, J., Leeb, B., Lioté, F., et al. (2006). EULAR evidence based recommendations for gout. Part II:
Management. Report of a task force of the EULAR Standing Committee for International Clinical Studies Including Therapeutics (ESCISIT). Ann. Rheum. Dis. 65, 1312–1324.
Ziegler-Heitbrock, H.W.L., and Ulevitch, R.J. (1993). CD14: Cell surface receptor and differentiation marker. Immunol. Today 14, 121–125.
6.2. Table of Figures
Figure 1. Biosynthesis of uric acid during purine degradation ... 4
Figure 2. Crystal-induced pathologies in human ... 5
Figure 3. Crystal-related outside-in signaling ... 7
Figure 4. Simplified, schematic overview of the complement cascade ... 11
Figure 5. Direct and indirect interaction between an immune cell and uric acid crystals ... 14
6.3. Abbreviations
°C degree Celsius
µg microgram
µl microliter
AF488 AlexaFluor 488
AIM2 absent in melanoma 2
Apo apolipoprotein
ASC apoptosis-associated speck-like protein containing a CARD
ATP adenosine triphosphate
BSA bovine serum albumin
C complement protein
ca. circa
CaCO3 calcium carbonate
CaOx calcium oxalate
CARD caspase activation and recruitment domain
Cas9 CRISPR-associated protein 9
CD cluster of differentiation
CDC complement-dependent cytotoxicity
Clec12A C-type lectin domain family 12 member A CLL-1 C-type lectin-like molecule 1
CLR C-type lectin receptor
COPD chronic obstructive pulmonary disease CPPD calcium pyrophosphate dihydrate
CRISPR clustered regularly interspaced short palindromic repeats
CRP C-reactive protein
crRNA CRISPR-RNA
DAMPs damage-associated molecular patterns
dl deciliter
DMEM Dulbecco’s Modified Eagle Medium
DNA deoxyribonucleic acid
33 E. coli Escherichia coli
e.g. for example; latin exempli gratia
EDTA ethylendiamintetraacetat
ELISA enzyme-linked immunosorbent assay et al. and others; latin et alli
FACS fluorescence-activated cell sorting, flow cytometry
FCS fetal calf serum
Fig. Figure
FSC forward scatter
g gram
GFP green fluorescent protein
GM-CSF granulocyte-macrophage colony-stimulating factor
gRNA guide RNA
h hour
h human
i.e. that is; latin id est
IgG immune globulin G
IgM immune globulin M
IL interleukin
kb kilo base
kDa kilo Dalton
KO knock-out
l liter
LC-MS liquid chromatography-mass spectrometry
LDL low-density lipoprotein
LDLR low-density lipoprotein receptor
LRR leucine-rich repeat
M molar (g/mol)
m murine
MAC membrane attack complex
MARCO macrophage receptor with collagenous structure
MASP MBL-associated serine proteases
MBL mannose-binding lectins
M-CSF macrophage colony-stimulating factor
mg milligram
MICL myeloid inhibitory C-type lectin-like receptor
min minute
ml mililiter
mol amount of substance
MSU monosodium urate
NACHT conserved domain containing: NAIP (NLP family apoptosis inhibitor protein), CIITA (C2TA or MHC class II transcription activator), HET-E (incompatibility locus protein from Podospora anserina) and TEP1 (TP1 or telomerase-associated protein)
NETs neutrophil extracellular traps
NF-B nuclear factor B
NLRP inflam. NACHT, LRR, and PYD domains–containing protein 3 inflammasome NOD nucleotide-binding oligomerization domain
NSAIDs nonsteroidal anti-inflammatory drug PAGE polyacrylamide gel electrophoresis PAMPs pathogen-associated molecular patterns PBMC peripheral blood mononuclear cell
PBS phosphate buffered saline
PC-agarose phosphorylcholine coupled to agarose
PCR polymerase chain reaction
PRR pattern recognition receptor
PYD pyrin domain
RLU relative light unit
RNA ribonucleic acid
ROS reactive oxygen species
rpm rounds per minute
RT room temperature (20°C)
S. aureus Staphylococcus aureus
35
SDS sodium dodecyl sulfate
SR scavenger receptor
SSC sideward scatter
Tab. Table
TiO2 titanium dioxide
TLR Toll-like receptors
TNF- tumor necrosis factor
vs. versus
WT wild type
xg multiple acceleration of gravity (9.81 m/s²)
6.4. List of own publications
Alberts, A., Klingberg, A., Wessig, A.K., Combes, C., Witte, T., Brand, K., Pich, A., and
Neumann, K. C-reactive protein (CRP) recognizes uric acid crystals and recruits proteases C1 and MASP1. Sci Rep 10, 6391 (2020). https://doi.org/10.1038/s41598-020-63318-8
Alberts, A., Klingberg, A., Hoffmeister, L., Wessig, A.K., Brand, K., Pich, A., and Neumann, K.
Binding of macrophage receptor MARCO, LDL, and LDL receptor (LDLR) to disease-associated crystalline structures. (submitted, in review)