Comparison of IGLV2-14 light chain sequences of patients with AL amyloidosis or multiple myeloma.
Berghaus N, Schreiner S, Poos AM, Raab MS, Goldschmidt H, Mai EK, Salwender HJ, Bernhard H, Thurner L, Müller-Tidow C, Weinhold N, Hegenbart U, Schönland SO, Huhn S.
FEBS J. doi: 10.1111/febs.16805, online before print (2023)

Antibodies gone bad - the molecular mechanism of light chain amyloidosis.
Absmeier, R.M., Rottenaicher, GJ, Svilenov HL, Kazman P, Buchner J.
FEBS Journal 290, 1398-1419, doi: 10.1111/febs.16390 (2023)  

A constant domain mutation in a patient-derived antibody light chain reveals principles of AL amyloidosis.
Rottenaicher GJ, Absmeier RM, Meier L, Zacharias M, Buchner J.
Commun Biol 6, 209, doi: 10.1038/s42003-023-04574-y (2023)

Identification of AL proteins from 10 λ-AL amyloidosis patients by mass spectrometry extracted from abdominal fat and heart tissue.
Baur J, Berghaus N, Schreiner S, Hegenbart U, Schönland SO, Wiese S,  Huhn S, Haupt Ch.
Amyloid, 30, 27-37, doi 10.1080/13506129.2022.2095618 (2023)

Mechanistic insight into the aggregation pathway of an immunoglobulin light chain protein.
Pradhan T, Sarkar R, Schwierz N, Zacharias M, Reif B.
PREPRINT (Version 1) available at Research Square, doi.org/10.21203/rs.3.rs-1812502/v1 (26 July 2022)

Concurrent light chain amyloidosis and proximal tubulopathy: Insights into different aggregation behavior-A case report.
Feurstein S, Zoller J, Schwab C, Schreiner S, Mundt H, Breitkreutz I, Schneider B, Beimler J, Zeier M, Waldherr R, Gröschel S, Müller-Tidow C, Schönland SO, Hegenbart U.
EJHaem, 8;1377-1380, doi: 10.1002/jha2.555 (2022)

Analysis of the complete lambda light chain germline usage in patients with AL amyloidosis and dominant heart or kidney involvement.
Berghaus N, Schreiner S, Granzow M, Müller-Tidow C, Hegenbart U, Schönland SO, Huhn S.
PLoS One 17, doi: 10.1371/journal.pone.0264407 (2022)

Cryo-EM demonstrates the in vitro proliferation of an ex vivo amyloid fibril morphology by seeding.
Heerde T, Rennegarbe M, Biedermann A, Savran D, Pfeiffer PB, Hitzenberger M, Baur J, Puscalau-Girtu I, Zacharias M, Schwierz N, Haupt C, Schmidt M, Fändrich M.
Nat Commun 13, 85, doi: 10.1038/s41467-021-27688-5 (2022)  

Lysozyme amyloidosis-a report on a large German cohort and the characterisation of a novel amyloidogenic lysozyme gene variant.
Anker S, Hinderhofer K, Baur J, Haupt C, Röcken C, Beimler J, Zeier M, Weiler M, Wühl E, Kimmich C, Schönland SO, Hegenbart U.
Amyloid 29, 245-254. doi: 10.1080/13506129.2022.2072198 (2022)

Seroconversion Rates After the Second COVID-19 Vaccination in Patients with Systemic Light Chain (AL) amyloidosis.
Liebers N, Schönland SO, Speer C, Edelmann D, Schnitzler P, Kräusslich HG, Mueller-Tidow C, Hegenbart U, Dietrich S.
Hemasphere, 6, e688, doi: 10.1097/HS9.0000000000000688 (2022)

Quantitative proteome profiling provides evidence of an activation of the complement cascade in ATTR amyloidosis. Treitz C, Gottwald J, Gericke E, Urban P, Meliß RR, Axmann HD, Siebert F, Becker K, Tholey A, Röcken C.
Amyloid. 29, 102-109. doi: 10.1080/13506129.2021.2015316 (2022)

Cryo-EM structure of an ATTRwt amyloid fibril from systemic non-hereditary transthyretin amyloidosis.
Steinebrei M, Gottwald J, Baur J, Röcken C, Hegenbart U, Schönland SO, Schmidt M.
Nat Commun. 13, 6398. doi: 10.1038/s41467-022-33591-4 (2022)

Light Chain Restriction in Proximal Tubules-Implications for Light Chain Proximal Tubulopathy.
Büttner-Herold M, Krieglstein N, Chuva T , Minuth K, Pfister F, Daniel Ch, Klewer M, Büttner A, Ferrazzi F, Bertz S, Amann K.
Front Med 9, 723758, doi: 10.3389/fmed.2022.723758 (2022)

Molecular mechanism of amyloidogenic mutations in hypervariable regions of antibody light chains.
Rottenaicher GJ, Weber B, Rührnößl F, Kazman P,  Absmeier RM, Hitzenberger M, Zacharias M and Buchner J.
J Biol Chem 296, 100334, doi: 10.1016/j.jbc.2021.100334 (2021)

Treatment in AL Amyloidosis: Moving towards Individualized and Clone-Directed Therapy.
Hegenbart U, Raab MS, Schönland SO.
Hemato 2, 739-747, doi: 10.3390/hemato2040050 (2021)

The AL Amyloid Fibril: Looking for a Link between Fibril Formation and Structure.
Haupt C.
Hemato 2, 505-514, doi: 10.3390/hemato2030032 (2021)

Daratumumab, lenalidomide, and dexamethasone in systemic light-chain amyloidosis: High efficacy, relevant toxicity and main adverse effect of gain 1q21.
Kimmich CR, Terzer T, Benner A, Hansen T, Carpinteiro A, Dittrich T, Veelken K, Jauch A, Huhn S, Basset M, Goldschmidt H, Müller-Tidow C, Schönland SO, Hegenbart U.
Am J Hematol 96, E253-E257, doi: 10.1002/ajh.26191 (2021)

Protease resistance of ex vivo amyloid fibrils implies the proteolytic selection of disease-associated fibril morphologies.
Schönfelder J, Pfeiffer PB, Pradhan T, Bijzet J, Hazenberg BPC, Schönland SO, Hegenbart U, Reif B, Haupt C, Fändrich M.
Amyloid 28, 243-251, doi: 10.1080/13506129.2021.1960501 (2021)

Role of mutations and post-translational modifications in systemic AL amyloidosis studied by cryo-EM.
Radamaker L, Karimi-Farsijani S, Andreotti G, Baur J, Neumann M, Schreiner S, Berghaus N, Motika R, Haupt C, Walther P, Schmidt V, Huhn S, Hegenbart U, Schönland SO, Wiese S, Read C, Schmidt M, Fändrich M.
Nat Commun 12, 6434, doi: 10.1038/s41467-021-26553-9 (2021)

Complement 9 in amyloid deposits.
Lux A, Gottwald J, Behrens HM, Daniel C, Amann K, Röcken C.
Amyloid, 28, 199-208. doi: 10.1080/13506129.2021.1932799 (2021)

The amyloid proteome: a systematic review and proposal of a protein classification system.
Gottwald J, Röcken Ch.
Crit Rev Biochem Mol Biol 56, No 4, doi: 10.1080/10409238.2021.1937926 (2021) 

Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis.
Radamaker L, Baur J, Huhn S, Haupt CH, Hegenbart U, Schönland S, Bansal A, Schmidt M, Fändrich M.
Nat Commun 12, 875, doi: 10.1038/s41467-021-21126-2 (2021)

Lenalidomide and dexamethasone in relapsed/refractory immunoglobulin light chain (AL) amyloidosis: results from a large cohort of patients with long follow-up.
Basset M, Kimmich CR, Schreck N, Krzykalla J, Dittrich T, Veelken K, Goldschmidt H, Seckinger A, Hose D, Jauch A, Müller-Tidow C, Benner A, Hegenbart U, Schönland SO.
Br J Haematol 195, 230-243, doi: 10.1111/bjh.17685 (2021)

AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils.
Bansal A, Schmidt M, Rennegarbe M, Haupt Ch, Liberta F, Stecher S, Puscalau-Girtu I, Biedermann A, Fändrich M.
Nat Commun 12, 1013, doi: 10.1038/s41467-021-21129-z (2021)

Methods to study the structure of misfolded protein states in systemic amyloidosis.
Fändrich M, Schmidt M.
Biochem Soc Trans 49, 977-985, doi: 10.1042/BST20201022 (2021)

Negatively Charged Peptide Nanofibrils from Immunoglobulin Light Chain Sequester Viral Particles but Lack Cell-Binding and Viral Transduction-Enhancing Properties.
Schütz D, Read C, Groß R, Röcker A, Rode S, Annamalai K, Fändrich M, Münch J.
ACS Omega 6, 7731-7738, doi: 10.1021/acsomega.1c00068 (2021)  

Dissection of the amyloid formation pathway in AL amyloidosis.
Kazman P, Absmeier RM, Engelhardt H, Buchner J. 
Nat Commun 12, 6516, doi: 10.1038/s41467-021-26845-0 (2021)  

Protease resistance of ex vivo amyloid fibrils implies the proteolytic selection of disease-associated fibril morphologies.
Schönfelder J, Pfeiffer PB, Pradhan T, Bijzet J, Hazenberg BPC, Schönland SO, Hegenbart U, Reif B, Haupt C, Fändrich M.
Amyloid 28, 243-251, doi: 10.1080/13506129.2021.1960501 (2021)

MALDI mass spectrometry imaging unravels organ and amyloid-type specific peptide signatures in pulmonary and gastrointestinal amyloidosis.
Schürmann J, Gottwald J, Rottenaicher G, Tholey A, Röcken C.
Proteomics Clin Appl 15, e2000079, doi: 10.1002/prca.202000079 (2021)

Seeded fibrils of the germline variant of human λ-III immunoglobulin light chain FOR005 have a similar core as patient fibrils with reduced stability.
Pradhan T, Annamalai K, Sarkar R, Huhn S, Hegenbart U, Schönland S, Fändrich M, Reif B.
J Biol Chem 295 (52), 18474-18484, doi: 10.1074/jbc.RA120.016006 (2020)

Domain interactions determine the amyloidogenicity of antibody light chain mutants.
Weber B, Hora M, Kazman P, Pradhan T, Rührnößl F, Reif B, Buchner J.
J Mol Biol 432 (23), 6187-6199, doi: 10.1016/j.jmb.2020.10.005 (2020) 

Solid state NMR assignments of a human λ-III immunoglobulin light chain amyloid fibril.
Pradhan T, Annamalai K, Sarkar R, Hegenbart U, Schönland S, Fändrich M, Reif B.
Biomol NMR Assign, 15, 9-16, doi: 10.1007/s12104-020-09975-2 (2020)

Half a century of amyloids: past, present and future.
Ke PC, Zhou R, Serpell LC, Riek R, Knowles TPJ, Lashuel HA, Gazit E, Hamley IW, Davis TP, Fändrich M, Otzen DE, Chapman MR, Dobson CM, Eisenberg DS, Mezzenga R.
Chem Soc Rev 49, 5473-5509, doi: 10.1039/c9cs00199a (2020)

Fatal amyloid formation in a patient's antibody light chain is caused by a single point mutation.
Kazman P,  Vielberg MT, Pulido Cendales MD, Hunziger L, Weber B, Hegenbart U, Zacharias M, Köhler, R, Schönland S, Groll M, Buchner J.
Elife 9, e52300, doi: 10.7554/eLife.52300 (2020)

Unraveling the complexity of amyloid polymorphism using gold nanoparticles and cryo-EM.
Cendrowska U, Silva PJ, Ait-Bouziad N, Müller M, Zekiye PG, Vieweg S, Chiki A, Radamaker L, Kumar ST, Fändrich M, Tavanti F, Menziani MC, Alexander-Katz A, Stellacci F, Lashuel HA.
Proc Natl Acad Sci U S A, 117, 6866-6874, doi: 10.1073/pnas.1916176117 (2020)

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Older publications:

Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis.
Radamaker L, Lin Y-H, Annamalai K, Huhn S, Hegenbart U, Schönland SO, Fritz G, Schmidt M, Fändrich M.
Nature Communications 10, 1103 (2019)

Physical basis of amyloid fibril polymorphism.
Close W, Neumann M, Schmidt A, Hora M, Annamalai K, Schmidt M, Reif B, Schmidt V, Grigorieff N, Fändrich M.
Nature Communications 9, 699 (2018)

Lenalidomide/Melphalan/Dexamethasone in newly diagnosed patients with AL Amyloidosis: results of a prospective phase 2 study with long-term follow-up.
Hegenbart U, Bochtler T, Benner A, Becker N, Kimmich C, Kristen AV, Beimler J, Hund E, Zorn M, Freiberger A, Gawlik M, Goldschmidt H, Hose D, Jauch A, Ho AD, Schönland SO.
Haematologica 102, 1424-1431 (2017)

Common fibril structures imply systemically conserved protein misfolding pathways in vivo.
Annamalai K, Liberta F, Vielberg M-T, Close W, Lilie H, Gührs K-H, Schierhorn A, Koehler R, Schmidt A, Haupt C, Hegenbart U, Schönland SO, Schmidt M, Groll M, Fändrich M.
Angew Chem Int Ed 56, 7510-7514 (2017)

Genome-wide association study of immunoglobulin light chain amyloidosis in three patient cohorts: comparison with myeloma.
da Silva Filho MI, Försti A, Weinhold N, Meziane I, Campo C, Huhn S, Nickel J, Hoffmann P, Nothen MM, Jockel KH, Landi S, Mitchell JS, Johnson D, Morgan GJ, Houlston R, Goldschmidt H, Jauch A, Milani P, Merlini G, Rowcieno D, Hawkins P, Hegenbart U, Palladini G, Wechalekar A, Schönland SO, Hemminki K.
Leukemia 31, 1735-1742 (2017)

Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains.
Hora M, Carballo-Pacheco M, Weber B, Morris VK, Wittkopf A, Buchner J, Strodel B, Reif B.
Sci Rep 7, 41515 (2017)

A Stable Mutant Predisposes Antibody Domains to Amyloid Formation through Specific Non-Native Interactions.
Nokwe CN, Hora M, Zacharias M, Yagi H, Peschek J, Reif B, Goto Y, Buchner J.
Mol Biol 428, 1315-1332 (2016)

Cardiac amloid load: a prognostic and predictive biomarker at diagnosis prior to chemotherapy in AL amyloidosis.
Kristen AV, Brokbals E, Siepen F, Bauer R, Hein S, Aurich M, Riffel J, Behrens HM, Krüger S, Schirmacher P, Katus HA, Röcken C.
J Am Coll Cardiol 68, 13-24 (2016)

Polymorphism of Amyloid Fibrils In Vivo.
Annamalai K, Gührs KH, Koehler R, Schmidt M, Michel H, Loos C, Gaffney PM, Sigurdson CJ, Hegenbart U, Schönland SO, Fändrich M.
Angew Chem Int Ed 55, 4822-5 (2016)

Renal AA-amyloidosis in intravenous drug users - a role for HIV-infection?
Jung O, Haack HS, Buettner M, Betz C, Stephan C, Gruetzmacher P, Amann K, Bickel M.
BMC Nephrol 13, 151 (2012).

Immunohistochemistry in the classification of systemic forms of amyloidosis: a systematic investigation of 117 patients.
Schönland SO, Hegenbart U, Bochtler T, Mangatter A, Hansberg O, Ho AD, Lohse P, Röcken C.
Blood 119, 488-93 (2012)