Publications – Landau Group (Visiting)

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Sla2 is a core interaction hub for clathrin light chain and the Pan1/End3/Sla1 complex.

Draper-Barr G, Defelipe LA, Ruiz-Carrillo D, Gustavsson E, Landau M, García-Alai M

Structure (London, England : 1993), 2025

doi:10.1016/j.str.2025.04.013.

Resilience and Charge-Dependent Fibrillation of functional amyloid: Interactions of Pseudomonas Biofilm-Associated FapB and FapC Amyloids.

Golan N, Parizat A, Tabachnikov O, Barnea E, Olsen WP, Otzen DE, Landau M

The Journal of biological chemistry, 2025

doi:10.1016/j.jbc.2024.108096.

Digestive fate of milk and egg-derived amyloids: attenuated digestive proteolysis and impact on the trajectory of the gut microbiota.

Refael G, Engelberg Y, Romano A, Amiram G, Barnea E, Shani Levi C,Turjeman S, Landau M, Koren O, Lesmes U

Food hydrocolloids, 2024

doi:10.1016/j.foodhyd.2024.109820.

Staphylococcus aureus functional amyloids catalyze degradation of β-lactam antibiotics.

Arad E, Pedersen KB, Malka O, Mambram Kunnath S, Golan N, Aibinder P, Schiøtt B, Rapaport H, Landau M, Jelinek R

Nature communications, 2023

doi:10.1038/s41467-023-43624-1.

What can AlphaFold do for antimicrobial amyloids?

Ragonis-Bachar P, Axel G, Blau S, Ben-Tal N, Kolodny R, Landau M

Proteins, 2023

doi:10.1002/prot.26618.

Differential fibril morphologies and thermostability determine functional roles of Staphylococcus aureus PSMα1 and PSMα3.

Rayan B, Barnea E, Khokhlov A, Upcher A, Landau M

Frontiers in molecular biosciences, 2023

doi:10.3389/fmolb.2023.1184785.

Designed inhibitors to reduce amyloid virulence and cytotoxicity and combat neurodegenerative and infectious diseases.

Indig RY, Landau M

Current opinion in chemical biology, 2023

doi:10.1016/j.cbpa.2023.102318.

Beyond One-Trick Ponies: The Multifunctional Marvels of Microbial Functional Amyloids.

Landau M

Microorganisms, 2023

doi:10.3390/microorganisms11051201.

Natural antimicrobial peptides self-assemble as α/β chameleon amyloids.

Ragonis-Bachar P, Rayan B, Barnea E, Engelberg Y, Upcher A, Landau M

Biomacromolecules, 2022

doi:10.1021/acs.biomac.2c00582.

The Cryo-EM structures of two amphibian antimicrobial cross-β amyloid fibrils.

Bücker R, Seuring C, Cazey C, Veith K, García-Alai M, Grünewald K, Landau M

Nature communications, 2022

doi:10.1038/s41467-022-32039-z.

Structure and conservation of amyloid spines from the Candida albicans Als5 adhesin

Golan N, Schwartz-Perov S, Landau M, Lipke PN

Frontiers in molecular biosciences, 2022

doi:10.3389/fmolb.2022.926959.

Structural mimicry in microbial and antimicrobial amyloids.

Golan N, Engelberg Y, Landau M

Annual review of biochemistry, 2022

doi:10.1146/annurev-biochem-032620-105157.

Rare by natural selection: disulfide-bonded supramolecular antimicrobial peptides.

Engelberg Y, Ragonis-Bachar P, Landau M

Biomacromolecules, 2022

doi:10.1021/acs.biomac.1c01353.

Structural and functional insights into the biofilm-associated BceF tyrosine kinase domain from Burkholderia cepacia.

Mayer M, Matiuhin Y, Nawatha M, Tabachnikov O, Fish I, Schutz N, Dvir H, Landau M

Biomolecules, 2021

doi:10.3390/biom11081196.

Integrative structural biology in the era of accurate structure prediction.

Masarati G, Landau M, Ben-Tal N, Lupas A, Kosloff M, Kosinski J

Journal of molecular biology, 2021

doi:10.1016/j.jmb.2021.167127.

Inhibition of Staphylococcus aureus biofilm-forming functional amyloid by molecular tweezers.

Malishev R, Salinas N, Gibson J, Eden AB, Mieres-Perez J, Ruiz-Blanco YB, Malka O, Kolusheva S, Klärner FG, Schrader T, Sanchez-Garcia E, Wang C, Landau M, Bitan G, Jelinek R

Cell chemical biology, 2021

doi:10.1016/j.chembiol.2021.03.013.

Functional and pathological amyloid structures in the eyes of 2020 cryo-EM.

Ragonis-Bachar P, Landau M

Current opinion in structural biology, 2021

doi:10.1016/j.sbi.2021.01.006.

The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid.

Salinas N, Tayeb-Fligelman E, Sammito MD, Bloch D, Jelinek R, Noy D, Usón I, Landau M

Proceedings of the National Academy of Sciences of the United States of America, 2021

doi:10.1073/pnas.2014442118.

The Human LL-37(17-29) antimicrobial peptide reveals a functional supramolecular structure.

Engelberg Y, Landau M

Nature communications, 2020

doi:10.1038/s41467-020-17736-x.

Staphylococcus aureus PSMα3 cross-α fibril polymorphism and determinants of cytotoxicity.

Tayeb-Fligelman E, Salinas N, Tabachnikov O, Landau M

Structure (London, England : 1993), 2020

doi:10.1016/j.str.2019.12.006.

Structural insights into curli CsgA Cross-β fibril architecture inspire repurposing of anti-amyloid compounds as anti-biofilm agents.

Perov S, Lidor O, Salinas N, Golan N, Tayeb-Fligelman E, Deshmukh M, Willbold D, Landau M

PLoS pathogens, 2019

doi:10.1371/journal.ppat.1007978.

Identification of two principal amyloid-driving segments in variable domains of Ig light chains in systemic light-chain amyloidosis.

Brumshtein B, Esswein SR, Sawaya MR, Rosenberg G, Ly AT, Landau M, Eisenberg DS

The Journal of biological chemistry, 2019

doi:10.1074/jbc.RA118.004142.

Mimicking cross-α amyloids.

Landau M

Nature chemical biology, 2018

doi:10.1038/s41589-018-0118-0.

Extreme amyloid polymorphism in Staphylococcus aureus virulent PSMα peptides.

Salinas N, Colletier JP, Moshe A, Landau M

Nature communications, 2018

doi:10.1038/s41467-018-05490-0.

Reciprocal interactions between membrane bilayers and S. aureus PSMα3 cross-α amyloid fibrils account for species-specific cytotoxicity.

Malishev R, Tayeb-Fligelman E, David S, Meijler MM, Landau M, Jelinek R

Journal of molecular biology, 2018

doi:10.1016/j.jmb.2018.03.022.

X-Ray structural study of amyloid-like fibrils of Tau peptides bound to small-molecule ligands.

Tayeb-Fligelman E, Landau M

Methods in molecular biology (Clifton, N.J.), 2017

doi:10.1007/978-1-4939-6598-4_5.

Getting in charge of β-synuclein fibrillation.

Landau M

The Journal of biological chemistry, 2017

doi:10.1074/jbc.H117.780528.

A Small molecule inhibitor of Bruton's tyrosine kinase involved in B-Cell signaling.

Ratzon E, Bloch I, Nicola M, Cohen E, Ruimi N, Dotan N, Landau M, Gal M

ACS omega, 2017

doi:10.1021/acsomega.7b00576.

The cytotoxic Staphylococcus aureus PSMα3 reveals a cross-α amyloid-like fibril

Tayeb-Fligelman E, Tabachnikov O, Moshe A, Goldshmidt-Tran O, Sawaya MR, Coquelle N, Colletier JP, Landau M

Science (New York, N.Y.), 2017

doi:10.1126/science.aaf4901.

Congenital dilated cardiomyopathy caused by biallelic mutations in Filamin C.

Reinstein E, Gutierrez-Fernandez A, Tzur S, Bormans C, Marcu S, Tayeb-Fligelman E, Vinkler C, Raas-Rothschild A, Irge D, Landau M, Shohat M, Puente XS, Behar DM, Lopez-Otın C

European journal of human genetics : EJHG, 2017

doi:10.1038/ejhg.2016.110.

Preparation of crystalline samples of amyloid fibrils and oligomers.

Moshe A, Landau M, Eisenberg D

Methods in molecular biology (Clifton, N.J.), 2016

doi:10.1007/978-1-4939-2978-8_13.

Sodium-proton (Na(+)/H(+)) antiporters: properties and roles in health and disease.

Padan E, Landau M

Metal ions in life sciences, 2016

doi:10.1007/978-3-319-21756-7_12.

The GPSM2/LGN GoLoco motifs are essential for hearing.

Bhonker Y, Abu-Rayyan A, Ushakov K, Amir-Zilberstein L, Shivatzki S, Yizhar-Barnea O, Elkan-Miller T, Tayeb-Fligelman E, Kim SM, Landau M, Kanaan M, Chen P, Matsuzaki F, Sprinzak D, Avraham KB

Mammalian genome : official journal of the International Mammalian Genome Society, 2016

doi:10.1007/s00335-015-9614-7.

Mutations in TAX1BP3 cause dilated cardiomyopathy with septo-optic dysplasia.

Reinstein E, Orvin K, Tayeb-Fligelman E, Stiebel-Kalish H, Tzur S, Pimienta AL, Bazak L, Bengal T, Cohen L, Gaton DD, Bormans C, Landau M, Kornowski R, Shohat M, Behar DM

Human mutation, 2015

doi:10.1002/humu.22759.

Formation of amyloid fibers by monomeric light chain variable domains.

Brumshtein B, Esswein SR, Landau M, Ryan CM, Whitelegge JP, Phillips ML, Cascio D, Sawaya MR, Eisenberg DS

The Journal of biological chemistry, 2014

doi:10.1074/jbc.M114.585638.

Functional evaluation of autism-associated mutations in NHE9.

Kondapalli KC, Hack A, Schushan M, Landau M, Ben-Tal N, Rao R

Nature communications, 2013

doi:10.1038/ncomms3510.

Lipid bilayers significantly modulate cross-fibrillation of two distinct amyloidogenic peptides.

Gal N, Morag A, Kolusheva S, Winter R, Landau M, Jelinek R

Journal of the American Chemical Society, 2013

doi:10.1021/ja4070427.

Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta.

Jiang L, Liu C, Leibly D, Landau M, Zhao M, Hughes MP, Eisenberg DS

eLife, 2013

doi:10.7554/eLife.00857.

Compound heterozygosity of HLA-DRB301:01 and HLA-DRB401:01 as a potential predictor of fetal neonatal alloimmune thrombocytopenia.

Loewenthal R, Rosenberg N, Kalt R, Dardik R, Landau M, Yahalom V, Avishai O, Frenkel O, Gazit E, Steinberg DM, Lipitz S, Salomon O

Transfusion, 2013

doi:10.1111/j.1537-2995.2012.03734.x.

Atomic view of a toxic amyloid small oligomer.

Laganowsky A, Liu C, Sawaya MR, Whitelegge JP, Park J, Zhao M, Pensalfini A, Soriaga AB, Landau M, Teng PK, Cascio D, Glabe C, Eisenberg D

Science (New York, N.Y.), 2012

doi:10.1126/science.1213151.

Molecular basis for amyloid-beta polymorphism.

Colletier JP, Laganowsky A, Landau M, Zhao M, Soriaga AB, Goldschmidt L, Flot D, Cascio D, Sawaya MR, Eisenberg D

Proceedings of the National Academy of Sciences of the United States of America, 2011

doi:10.1073/pnas.1112600108.

Towards a pharmacophore for amyloid.

Landau M, Sawaya MR, Faull KF, Laganowsky A, Jiang L, Sievers SA, Liu J, Barrio JR, Eisenberg D

PLoS biology, 2011

doi:10.1371/journal.pbio.1001080.

Two conflicting NHE1 model structures: compatibility with experimental data and implications for the transport mechanism.

Schushan M, Landau M, Padan E, Ben-Tal N

The Journal of biological chemistry, 2011

doi:10.1074/jbc.L110.159202.

Molecular insight into human platelet antigens: structural and evolutionary conservation analyses offer new perspective to immunogenic disorders.

Landau M, Rosenberg N

Transfusion, 2011

doi:10.1111/j.1537-2995.2010.02862.x.

A unique interaction between alphaIIb and beta3 in the head region is essential for outside-in signaling-related functions of alphaIIbbeta3 integrin.

Hauschner H, Landau M, Seligsohn U, Rosenberg N

Blood, 2010

doi:10.1182/blood-2009-10-251066.

Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function.

Laganowsky A, Benesch JL, Landau M, Ding L, Sawaya MR, Cascio D, Huang Q, Robinson CV, Horwitz J, Eisenberg D

Protein science : a publication of the Protein Society, 2010

doi:10.1002/pro.380.

Molecular mechanisms for protein-encoded inheritance.

Wiltzius JJ, Landau M, Nelson R, Sawaya MR, Apostol MI, Goldschmidt L, Soriaga AB, Cascio D, Rajashankar K, Eisenberg D

Nature structural & molecular biology, 2009

doi:10.1038/nsmb.1643.

Three residues at the interface of factor XI (FXI) monomers augment covalent dimerization of FXI.

Zucker M, Zivelin A, Landau M, Rosenberg N, Seligsohn U

Journal of thrombosis and haemostasis : JTH, 2009

doi:10.1111/j.1538-7836.2009.03353.x.

Specific cysteines in beta3 are involved in disulfide bond exchange-dependent and -independent activation of alphaIIbbeta3.

Mor-Cohen R, Rosenberg N, Landau M, Lahav J, Seligsohn U

The Journal of biological chemistry, 2008

doi:10.1074/jbc.M802399200.

Dynamic equilibrium between multiple active and inactive conformations explains regulation and oncogenic mutations in ErbB receptors.

Landau M, Ben-Tal N

Biochimica et biophysica acta, 2008

doi:10.1016/j.bbcan.2007.08.001.

A novel factor XI missense mutation (Val371Ile) in the activation loop is responsible for a case of mild type II factor XI deficiency.

Bozzao C, Rimoldi V, Asselta R, Landau M, Ghiotto R, Tenchini ML, De Cristofaro R, Castaman G, Duga S

The FEBS journal, 2007

doi:10.1111/j.1742-4658.2007.06134.x.

Disulfide bond disruption by a beta 3-Cys549Arg mutation in six Jordanian families with Glanzmann thrombasthenia causes diminished production of constitutively active alpha IIb beta 3.

Mor-Cohen R, Rosenberg N, Peretz H, Landau M, Coller BS, Awidi A, Seligsohn U

Thrombosis and haemostasis, 2007

doi:10.1160/TH07-04-0248.

Model structure of the Na+/H+ exchanger 1 (NHE1): functional and clinical implications.

Landau M, Herz K, Padan E, Ben-Tal N

The Journal of biological chemistry, 2007

doi:10.1074/jbc.M705460200.

Characterization of seven novel mutations causing factor XI deficiency.

Zucker M, Zivelin A, Landau M, Salomon O, Kenet G, Bauduer F, Samama M, Conard J, Denninger MH, Hani AS, Berruyer M, Feinstein D, Seligsohn U

Haematologica, 2007

doi:10.3324/haematol.11526.

Trp207Gly in platelet glycoprotein Ibalpha is a novel mutation that disrupts the connection between the leucine-rich repeat domain and the disulfide loop structure and causes Bernard-Soulier syndrome.

Rosenberg N, Lalezari S, Landau M, Shenkman B, Seligsohn U, Izraeli S

Journal of thrombosis and haemostasis : JTH, 2007

doi:10.1111/j.1538-7836.2007.02298.x.

Molecular diversity of Glanzmann thrombasthenia in southern India: new insights into mRNA splicing and structure-function correlations of alphaIIbbeta3 integrin (ITGA2B, ITGB3).

Peretz H, Rosenberg N, Landau M, Usher S, Nelson EJ, Mor-Cohen R, French DL, Mitchell BW, Nair SC, Chandy M, Coller BS, Srivastava A, Seligsohn U

Human mutation, 2006

doi:10.1002/humu.20304.

A 13-bp deletion in alpha(IIb) gene is a founder mutation that predominates in Palestinian-Arab patients with Glanzmann thrombasthenia.

Rosenberg N, Hauschner H, Peretz H, Mor-Cohen R, Landau M, Shenkman B, Kenet G, Coller BS, Awidi AA, Seligsohn U

Journal of thrombosis and haemostasis : JTH, 2005

doi:10.1111/j.1538-7836.2005.01618.x.

Of four mutations in the factor VII gene in Tunisian patients, one novel mutation (Ser339Phe) in three unrelated families abrogates factor X activation.

Fromovich-Amit Y, Zivelin A, Rosenberg N, Landau M, Rosa JP, Seligsohn U

Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis, 2005

doi:10.1097/01.mbc.0000172696.62363.8c.

ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures.

Landau M, Mayrose I, Rosenberg Y, Glaser F, Martz E, Pupko T, Ben-Tal N

Nucleic acids research, 2005

doi:10.1093/nar/gki370.

Single point mutations in the zinc finger motifs of the human immunodeficiency virus type 1 nucleocapsid alter RNA binding specificities of the gag protein and enhance packaging and infectivity.

Mark-Danieli M, Laham N, Kenan-Eichler M, Castiel A, Melamed D, Landau M, Bouvier NM, Evans MJ, Bacharach E

Journal of virology, 2005

doi:10.1128/JVI.79.12.7756-7767.2005.

A putative mechanism for downregulation of the catalytic activity of the EGF receptor via direct contact between its kinase and C-terminal domains.

Landau M, Fleishman SJ, Ben-Tal N

Structure (London, England : 1993), 2004

doi:10.1016/j.str.2004.10.006.

Characterization of mutations causing factor VII deficiency in 61 unrelated Israeli patients.

Fromovich-Amit Y, Zivelin A, Rosenberg N, Tamary H, Landau M, Seligsohn U

Journal of thrombosis and haemostasis : JTH, 2004

doi:10.1111/j.1538-7836.2004.00921.x.

Severe factor XI deficiency caused by a Gly555 to Glu mutation (factor XI-Glu555): a cross-reactive material positive variant defective in factor IX activation.

Zivelin A, Ogawa T, Bulvik S, Landau M, Toomey JR, Lane J, Seligsohn U, Gailani D

Journal of thrombosis and haemostasis : JTH, 2004

doi:10.1111/j.1538-7836.2004.00882.x.

Seven novel mutations in the factor XIII A-subunit gene causing hereditary factor XIII deficiency in 10 unrelated families.

Vysokovsky A, Saxena R, Landau M, Zivelin A, Eskaraev R, Rosenberg N, Seligsohn U, Inbal A

Journal of thrombosis and haemostasis : JTH, 2004

doi:10.1111/j.1538-7836.2004.00908.x.

Evolution of p53 in hypoxia-stressed Spalax mimics human tumor mutation.

Ashur-Fabian O, Avivi A, Trakhtenbrot L, Adamsky K, Cohen M, Kajakaro G, Joel A, Amariglio N, Nevo E, Rechavi G

Proceedings of the National Academy of Sciences of the United States of America, 2004

doi:10.1073/pnas.0404998101.

A novel Phe171Cys mutation in integrin alpha causes Glanzmann thrombasthenia by abrogating alphabeta complex formation.

Rosenberg N, Landau M, Luboshitz J, Rechavi G, Seligsohn U

Journal of thrombosis and haemostasis : JTH, 2004

doi:10.1111/j.1538-7836.2004.00758.x.