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Recent Scientific Publications

Please follow the link (the DOI number) to the article at the journal homepage. Be aware that not all articles are open access.

2017

Mattsson, K., Johnson, E.V., Malmendal, A., Linse, S., Hansson, L.-A., and Cedervall, T.

Brain damage and behavioural disorders in fish induced by plastic nanoparticles delivered through the food chain.

Scientific Reports, 2017, 7: 11452, 10.1038/s41598-017-10813-0

 

Meisl, G., Rajah, L.,  Cohen, S.A.I.,  Pfammatter, M.,  Šarić, A.,  Hellstrand, E.,  Buell, A.K.,  Aguzzi, A.,  Linse, S.,  Vendruscolo, M.,  Dobson, C.M.,  and  Knowles, T.P.J.

Scaling behaviour and rate-determining steps in filamentous self-assembly.

Chem. Sci., 2017, 10.1039/C7SC01965C

 

Meisl, G., Yang, X., Dobson, C.M., Linse. S., and Knowles, T.P.J.

Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants

Chem. Sci., 2017, 8, 4352-4362, 10.1039/c7sc00215g

 

Khan, M.A.I., Respondek, M., Kjellström, S., Deep, S., Linse, S., and Akke, M.

Cu/Zn Superoxide Dismutase Forms Amyloid Fibrils under Near-Physiological Quiescent Conditions: The Roles of Disulfide Bonds and Effects of Denaturant

ACS Chemical Neuroscience, 2017, 10.1021/acschemneuro.7b00162

 

Chia, S., Flagmeier, P., Habchi, J, Lattanzi, V., Linse, S., Dobson, C.M., Knowles, T.P.J., and Vendruscolo, M.

Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates

PNAS, 2017, 114, 8005-8010, 10.1073/pnas.1700239114

 

Munke, A., Persson, J., Weiffert, T., De Genst, E., Meisl, G., Arosio, P., Carnerup, A., Dobson, C.M., Vendruscolo, M., Knowles, T.P.J., and Linse, S.

Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication

PNAS, 2017, 114, 6444-6449, 10.1073/pnas.1700407114

 

Linse, S.,

Monomer-dependent secondary nucleation in amyloid formation

Biophys Rev, 2017, 10.1007/s12551-017-0289-z

 

Aprile, F.A., Sormanni, P., Perni, M., Arosio, P., Linse, S., Knowles, T.P.J., Dobson, C.M., and Vendruscolo, M.

Selective targeting of primary and secondarynucleation pathways in Ab42 aggregation using arational antibody scanning method.

Sci. Adv. 2017; 3: e1700488 10.1126/sciadv.1700488

 

Gaspar, R., Meisl, G., Buell, A.K., Young, L., Kaminski, C.F., and Knowles, T.P.J.

Acceleration of α-synuclein aggregation

Amyloid-The Journal of Protein Folding Disorders Volume 24, 2017 - Issue sup1, 10.1080/13506129.2017.1292904

 

Donovan, K.J., Silvers, R., Linse, S., and Griffin, R.G.

A 3D MAS NMR experiment utilizing through-space 15N-15N correlations

J. Am. Chem. Soc., 2017, 10.1021/jacs.7b01159

 

Lundqvist, M., Augustsson, C., Lilja, M., Lundkvist, K., Dahlbäck, B., Linse, S., and Cedervall, T.

The nanoparticle protein corona formed in human blood or human blood fractions

PLOS One, 2017, 10.1371/journal.pone.0175871

 

2016

Habchi, J., Chia, S., Limbocker, R., Mannini, B., Ahn, M., Perni, M., Hansson, O., Arosio, P., Kumita, J.R., Kumar Challa, P., Cohen, S.I.A, Linse, S., Dobson, C.M., Knowles, T.P.J., and Vendruscolo, M.

Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer’s disease

PNAS,2016, 10.1073/pnas.1615613114

 

Padayachee, E.R., Zetterberg, H. , Portelius, E. , Borén, J., Molinuevo, J.L., Andreasen, N., Cukalevski, R., Linse, S., Blennow, K. and Andreasson, U. 

Cerebrospinal fluid-induced retardation of amyloid β aggregation correlates with Alzheimer's disease and the APOE ε4 allele

Brain Research, 2016, 1651, 11-16, 10.1016/j.brainres.2016.09.022

 

Sanagavarapu, K., Weiffert, T., Mhurchú, N.N., O’Connell, D., and Linse, S.

Calcium Binding and Disulfide Bonds Regulate the Stability of Secretagogin towards Thermal and Urea Denaturation

PLOSone, 2016, 10.1371/journal.pone.0165709

 

O'Malley, T.T.; Wittbold, W.M., Linse, S., and Walsh D.M.

The aggregation paths and products of Aβ42 dimers are distinct from Aβ42 monomer

Biochemistry, 2016, 10.1021/acs.biochem.6b00453

 

Šarić, A., Buell, A.K., Meisl, G., Michaels, T.C.T., Dobson, C.M., Linse, S., Knowles T.P.J., and Frenkel D.,

Physical determinants of the self-replication of protein fibrils

Nature Physics, 2016, 10.1038/nphys3828

 

Colvin, M.T., Silvers, R., Ni, Q.Z., Can, T.V., Sergeyev, I.V., Rosay, M., Donovan, K.J., Michael, B., Wall, J.S., Linse, S., and Griffin, R.G.,

Atomic Resolution Structure of Monomorphic AB42 Amyloid Fibrils

J. Am. Chem. Soc., 2016, 10.1021/jacs.6b05129

 

Herling, T.W., O’Connell, D.J., Bauer, M.C., Persson, J., Weininger, U., Knowles, T.P.J., and Linse, S.

A Microfluidic Platform for Real-Time Detection and Quantification of Protein-Ligand Interactions

Biophys J., 2016, 110(9), 1957-66, 10.1016/j.bpj.2016.03.038

 

Kakkar, V., Månsson, C., de Mattos, E.P., Bergink, S., van der Zwaag, M., van Waarde, M.A.W.H., Kloosterhuis, N.J., Melki, R., van Cruchten, R.T.P., Al-Karadaghi, S., Arosio, P., Dobson, C.M., Knowles, T.P.J., Bates, G.P., van Deursen, J.M., Linse, S., van de Sluis, B., Emanuelsson, C., and Kampinga, H.H.

The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model

Molecular Cell, 2016, 10.1016/j.molcel.2016.03.017

 

Arosioa, P., Cedervall, T.,  Knowles, T.P.J., Linse, S.

Analysis of the length distribution of amyloid fibrils by centrifugal sedimentation

Analytical Biochemistry, 2016, 10.1016/j.ab.2016.03.015

 

Arosio, P., Michaels, T.C.T., Linse, S., Månsson, C., Emanuelsson, C., Presto, J., Johansson, J., Vendruscolo, M., Dobson C.M., and Knowles, T.P.J.

Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation

Nature Communications 7, 2016, Article number: 10948, 10.1038/ncomms10948

 

Habchi, J., Arosio, P., Perni, M., Costa, A.R., Yagi-Utsumi, M., Joshi, P., Chia, S., Cohen, S.I.A., Müller, M.B.D., Linse, S., Nollen, E.A.A., Dobson, C.M., Knowles, T.P.J., and Vendruscolo, M.

An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer’s disease

Science Advances, 2016, Vol. 2, no. 2, e1501244, 10.1126/sciadv.1501244

 

Meisl, G., Yang, X., Frohm, B., Knowles T.P.J., and Linse, S.

Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide

Scientific Reports, 2016,  6, Article number: 18728, doi:10.1038/srep18728

 

Meisl, G., Kirkegaard, J.B., Arosio, P., Michaels, T.C.T., Vendruscolo, M., Dobson, C.M., Linse, S., and Knowles T.P.J.

Molecular mechanisms of protein aggregation from global fitting of kinetic models.

Nature Protocols, 2016, 11, 252–272, 10.1038/nprot.2016.010

 

Arosio, P., Müller, T., Rajah, L., Yates, E.V., Aprile, F.A., Zhang, Y., Cohen, S.I.A., White, D.A., Herling, T.W., De Genst, E.J., Linse, S., Vendruscolo, M., Dobson, C.M, and Knowles T.P.J.

Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions.

ACS Nano, 10.1021/acsnano.5b04713

 

2015

Dunning, C.J., McGauran, G., Willén, K., Gouras, G.K., O'Connell,D.J., and Linse, S.

A direct high affinity interaction between Aβ42 and GSK3α stimulates hyperphosphorylation of tau. A new molecular link in Alzheimer's disease?

ACS Chem. Neurosci., 10.1021/acschemneuro.5b00262

 

Szczepankiewics, O., Linse, B., Meisl, G., Thulin, E., Frohm, B., Frigerio, C.S., Colvin, T.M. Jacavone, A.C., Griffin, R.G., Knowles, T.P.J., Walsh, D.M., and Linse, S.

N-terminal extensions retard Abeta42 fibril formation but allow cross-seeding and co-aggregation with Abeta42.

J. Am. Chem. Soc., 2015, 137 (46), 14673-14685, 10.1021/jacs.5b07849

http://pubs.acs.org/doi/abs/10.1021%2Fjacs.5b07849

 

Yates, E., Muller, T., Rajah, L., De Genst, E., Arosio, P., Linse, S., Vendruscolo, M., Dobson, C., and Knowles, T.

Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity

Nature Chemistry, 2015, 7(10), 802-9, 10.1038/nchem.2344

 

Nasir, I., Fatih, W., Svensson, A., Radu, D., Linse, S., Cabaleiro Lago, C., and Lundqvist, M.

High Throughput Screening Method to Explore Protein Interactions with Nanoparticles.

PLoS ONE, 2015, 10(8), e0 136687, 10.1371/journal.pone.0136687

 

Nasir, I., Linse, S., and Cabaleiro-Lago, C.

Fluorescent Filter-Trap Assay for Amyloid Fibril Formation Kinetics in Complex Solutions.

ACS Chemical Neuroscience, 2015, 6(8), 1436-1444, 10.1021/acschemneuro.5b00104

 

Colvin, M.T., Silvers, R., Frohm, B., Su, Y., Linse, S. and Griffin, R.G.

High Resolution Structural Characterization of Aβ42 Amyloid Fibrils by Magic Angle Spining NMR

J. Am. Chem. Soc., 2015, 137, 7509-7518, 10.1021/jacs.5b03997

 

Herling, T.W., Arosio, P., Mueller, T., Linse, S., and Knowels, T.P.J.

A Microfluidic Platform for Quantitative Measurments of Effective Protein Charges and Single Ion Binding In Solution.

Physical Chemistry Chemical Physics, 2015, 17(18), 12161-12167, 10.1039/c5cp00746a

 

Arosio, P., Knowles, T.P.J., and Linse, S.

On the Lag Phase in Amyloid Fibril Formation.

Physical Chemistry Chemical Physics, 2015, 17(12), 7606-7618, 10.1039/c4cp05563b

 

Wallerstein, J., Weininger, U., Khan, M. A. I., Linse, S. and Akke, M.

Site-Specific Protonation Kinetics of Acidic Side Chains in Proteins Determined by Ph-Dependent Carboxyl (13)C Nmr Relaxation

J. Am. Chem. Soc., 2015, 137, 3093-101, 10.1021/ja513205s

 

Cohen, S. I. A., Arosio, P., Presto, J., Kurudenkandy, F. R., Biverstal, H., Dolfe, L., Dunning, C., Yang, X., Frohm, B., Vendruscolo, M., Johansson, J., Dobson, C. M., Fisahn, A., Knowles, T. P. J. and Linse, S.

A Molecular Chaperone Breaks the Catalytic Cycle That Generates Toxic Abeta Oligomers

Nat. Struct. Mol. Biol., 2015, 22, 207-13, 10.1038/nsmb.2971

 

Sondergaard, M. T., Sorensen, A. B., Skov, L. L., Kjaer-Sorensen, K., Bauer, M. C., Nyegaard, M., Linse, S., Oxvig, C. and Overgaard, M. T.

Calmodulin Mutations Causing Catecholaminergic Polymorphic Ventricular Tachycardia Confer Opposing Functional and Biophysical Molecular Changes

The FEBS journal, 2015, 282, 803-16, 10.1111/febs.13184

 

Singh, B., Al Jubair, T., Morgelin, M., Sundin, A., Linse, S., Nilsson, U. J. and Riesbeck, K.

Haemophilus Influenzae Surface Fibril (Hsf) Is a Unique Twisted Hairpin-Like Trimeric Autotransporter

International Journal of Medical Microbiology, 2015, 305, 27-37, 10.1016/j.ijmm.2014.10.004

 

Shimanovich, U., Efimov, I., Mason, T. O., Flagmeier, P., Buell, A. K., Gedanken, A., Linse, S., Akerfeldt, K. S., Dobson, C. M., Weitz, D. A. and Knowles, T. P. J.

Protein Microgels from Amyloid Fibril Networks

Acs Nano, 2015, 9, 43-51, 10.1021/nn504869d

 

Mattsson, K., Ekvall, M. T., Hansson, L.-A., Linse, S., Malmendal, A. and Cedervall, T.

Altered Behavior, Physiology, and Metabolism in Fish Exposed to Polystyrene Nanoparticles

Environmental Science & Technology, 2015, 49, 553-561, 10.1021/es5053655

 

Cukalevski, R., Yang, X., Meisl, G., Weininger, U., Bemfur, K., Frohm, B., Knowles, T.P.J., and Linse, S.

The A beta 40 and A beta 42 Peptides Self-assemble into Seperate Homomolecular Fibrils in Binary Mixtures but Cross-react During Primary Nucleation.

Chemical Science, 2015, 6(7), 4215-4233, 10.1039/c4sc02517b

 

Jonsson, T., Memon, A. A., Sundquist, K., Sundquist, J., Olsson, S., Nalla, A., Bauer, M. and Linse, S.

Digested Wheat Gluten Inhibits Binding between Leptin and Its Receptor

BMC Biochemistry, 2015, 16, 10.1186/s12858-015-0032-y

 

Grey, M., Dunning, C. J., Gaspar, R., Grey, C., Brundin, P., Sparr, E. and Linse, S.

Acceleration of Alpha-Synuclein Aggregation by Exosomes

Journal of Biological Chemistry, 2015, 290, 2969-2982, 10.1074/jbc.M114.585703

 

Frohm, B., DeNizio, J. E., Lee, D. S. M., Gentile, L., Olsson, U., Malm, J., Akerfeldt, K. S. and Linse, S.

A Peptide from Human Semenogelin I Self-Assembles into a Ph-Responsive Hydrogel

Soft Matter, 2015, 11, 414-421, 10.1039/c4sm01793e

 

2014

Vacha, R., Linse, S. and Lund, M.

Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides

Journal of the American Chemical Society, 2014, 136, 11776-11782, 10.1021/ja505502e

 

Sanfins, E., Augustsson, C., Dahlback, B., Linse, S. and Cedervall, T.

Size-Dependent Effects of Nanoparticles on Enzymes in the Blood Coagulation Cascade

Nano Letters, 2014, 14, 4736-4744, 10.1021/nl501863u

 

O'Malley, T. T., Oktaviani, N. A., Zhang, D., Lomakin, A., O'Nuallain, B., Linse, S., Benedek, G. B., Rowan, M. J., Mulder, F. A. A. and Walsh, D. M.

A Beta Dimers Differ from Monomers in Structural Propensity, Aggregation Paths and Population of Synaptotoxic Assemblies

Biochemical Journal, 2014, 461, 413-426, 10.1042/bj20140219

 

Meisl, G., Yang, X., Hellstrand, E., Frohm, B., Kirkegaard, J. B., Cohen, S. I. A., Dobson, C. M., Linse, S. and Knowles, T. P. J.

Differences in Nucleation Behavior Underlie the Contrasting Aggregation Kinetics of the a Beta 40 and a Beta 42 Peptides

Proceedings of the National Academy of Sciences of the United States of America, 2014, 111, 9384-9389, 10.1073/pnas.1401564111

 

Mansson, C., Arosio, P., Hussein, R., Kampinga, H. H., Hashem, R. M., Boelens, W. C., Dobson, C. M., Knowles, T. P. J., Linse, S. and Emanuelsson, C.

Interaction of the Molecular Chaperone Dnajb6 with Growing Arnyloid-Beta 42 (a Beta 42) Aggregates Leads to Sub-Stoichiometric Inhibition of Amyloid Formation

Journal of Biological Chemistry, 2014, 289, 31066-31076, 10.1074/jbc.M114.595124

 

Hermansson, E., Schultz, S., Crowther, D., Linse, S., Winblad, B., Westermark, G., Johansson, J. and Presto, J.

The Chaperone Domain Brichos Prevents Cns Toxicity of Amyloid-Beta Peptide in Drosophila Melanogaster

Disease Models & Mechanisms, 2014, 7, 659-665, 10.1242/dmm.014787

 

Dell'Orco, D., Lundqvist, M., Linse, S. and Cedervall, T.

Mathematical Modeling of the Protein Corona: Implications for Nanoparticulate Delivery Systems

Nanomedicine, 2014, 9, 851-858, 10.2217/nnm.14.39

 

Buell, A. K., Galvagnion, C., Gaspar, R., Sparr, E., Vendruscolo, M., Knowles, T. P. J., Linse, S. and Dobson, C. M.

Solution Conditions Determine the Relative Importance of Nucleation and Growth Processes in Alpha-Synuclein Aggregation

Proceedings of the National Academy of Sciences of the United States of America, 2014, 111, 7671-7676, 10.1073/pnas.1315346111

 

Assarsson, A., Linse, S. and Cabaleiro-Lago, C.

Effects of Polyamino Acids and Polyelectrolytes on Amyloid Beta Fibril Formation

Langmuir, 2014, 30, 8812-8818, 10.1021/la501414j

 

Assarsson, A., Hellstrand, E., Cabaleiro-Lago, C. and Linse, S.

Charge Dependent Retardation of Amyloid Beta Aggregation by Hydrophilic Proteins

Acs Chemical Neuroscience, 2014, 5, 266-274, 10.1021/cn400124r

 

Arosio, P., Cukalevski, R., Frohm, B., Knowles, T. P. J. and Linse, S.

Quantification of the Concentration of a Beta 42 Propagons During the Lag Phase by an Amyloid Chain Reaction Assay

Journal of the American Chemical Society, 2014, 136, 219-225, 10.1021/ja408765u

 

2013

Slavov, N., Carey, J. and Linse, S.

Calmodulin Transduces Ca2+ Oscillations into Differential Regulation of Its Target Proteins

Acs Chemical Neuroscience, 2013, 4, 601-612, 10.1021/cn300218d

 

Knight, S. D., Presto, J., Linse, S. and Johansson, J.

The Brichos Domain, Amyloid Fibril Formation, and Their Relationship

Biochemistry, 2013, 52, 7523-7531, 10.1021/bi400908x

 

Hellstrand, E., Nowacka, A., Topgaard, D., Linse, S. and Sparr, E.

Membrane Lipid Co-Aggregation with Alpha-Synuclein Fibrils

Plos One, 2013, 8, 10.1371/journal.pone.0077235

 

Hellstrand, E., Kukora, S., Shuman, C. F., Steenbergen, S., Thulin, E., Kohli, A., Krouse, B., Linse, S. and Akerfeldt, K. S.

Forster Resonance Energy Transfer Studies of Calmodulin Produced by Native Protein Ligation Reveal Inter-Domain Electrostatic Repulsion

Febs Journal, 2013, 280, 2675-2687, 10.1111/febs.12269

 

Hellstrand, E., Grey, M., Ainalem, M.-L., Ankner, J., Forsyth, V. T., Fragneto, G., Haertlein, M., Dauvergne, M.-T., Nilsson, H., Brundin, P., Linse, S., Nylander, T. and Sparr, E.

Adsorption of Alpha-Synuclein to Supported Lipid Bilayers: Positioning and Role of Electrostatics

Acs Chemical Neuroscience, 2013, 4, 1339-1351, 10.1021/cn400066t

 

Ekvall, M. T., Bianco, G., Linse, S., Linke, H., Backman, J. and Hansson, L.-A.

Three-Dimensional Tracking of Small Aquatic Organisms Using Fluorescent Nanoparticles

Plos One, 2013, 8, 10.1371/journal.pone.0078498

 

Cohen, S. I. A., Linse, S., Luheshi, L. M., Hellstrand, E., White, D. A., Rajah, L., Otzen, D. E., Vendruscolo, M., Dobson, C. M. and Knowles, T. P. J.

Proliferation of Amyloid-Beta 42 Aggregates Occurs through a Secondary Nucleation Mechanism

Proceedings of the National Academy of Sciences of the United States of America, 2013, 110, 9758-9763, 10.1073/pnas.1218402110

 

2012

Willander, H., Presto, J., Askarieh, G., Biverstal, H., Frohm, B., Knight, S. D., Johansson, J. and Linse, S.

Brichos Domains Efficiently Delay Fibrillation of Amyloid Beta-Peptide

Journal of Biological Chemistry, 2012, 287, 31608-31617, 10.1074/jbc.M112.393157

 

Wahlstrom, A., Cukalevski, R., Danielsson, J., Jarvet, J., Onagi, H., Rebek, J., Jr., Linse, S. and Graslund, A.

Specific Binding of a Beta-Cyclodextrin Dimer to the Amyloid Beta Peptide Modulates the Peptide Aggregation Process

Biochemistry, 2012, 51, 4280-4289, 10.1021/bi300341j

 

Oslakovic, C., Cedervall, T., Linse, S. and Dahlback, B.

Polystyrene Nanoparticles Affecting Blood Coagulation

Nanomedicine-Nanotechnology Biology and Medicine, 2012, 8, 981-986, 10.1016/j.nano.2011.12.001

 

Ferreira, S. A., Oslakovic, C., Cukalevski, R., Frohm, B., Dahlback, B., Linse, S., Gama, F. M. and Cedervall, T.

Biocompatibility of Mannan Nanogel-Safe Interaction with Plasma Proteins

Biochimica Et Biophysica Acta-General Subjects, 2012, 1820, 1043-1051, 10.1016/j.bbagen.2012.04.015

 

Dell'Orco, D., Sulmann, S., Linse, S. and Koch, K.-W.

Dynamics of Conformational Ca2+-Switches in Signaling Networks Detected by a Planar Plasmonic Device

Analytical Chemistry, 2012, 84, 2982-2989, 10.1021/ac300213j

 

Dell'Orco, D., Lundqvist, M., Cedervall, T. and Linse, S.

Delivery Success Rate of Engineered Nanoparticles in the Presence of the Protein Corona: A Systems-Level Screening

Nanomedicine-Nanotechnology Biology and Medicine, 2012, 8, 1271-1281, 10.1016/j.nano.2012.02.006

 

Cukalevski, R., Boland, B., Frohm, B., Thulin, E., Walsh, D. and Linse, S.

Role of Aromatic Side Chains in Amyloid Beta-Protein Aggregation

Acs Chemical Neuroscience, 2012, 3, 1008-1016, 10.1021/cn300073s

 

Cedervall, T., Hansson, L.-A., Lard, M., Frohm, B. and Linse, S.

Food Chain Transport of Nanoparticles Affects Behaviour and Fat Metabolism in Fish

Plos One, 2012, 7, 10.1371/journal.pone.0032254

 

Cabaleiro-Lago, C., Szczepankiewicz, O. and Linse, S.

The Effect of Nanoparticles on Amyloid Aggregation Depends on the Protein Stability and Intrinsic Aggregation Rate

Langmuir, 2012, 28, 1852-1857, 10.1021/la203078w

 

Reddy, S. B., Anders, R. F., Beeson, J. G., Farnert, A., Kironde, F., Berenzon, S. K., Wahlgren, M., Linse, S. and Persson, K. E. M.

High Affinity Antibodies to Plasmodium Falciparum Merozoite Antigens Are Associated with Protection from Malaria

PLoS One, 2012, 7, 10.1371/journal.pone.0032242

 

Behnen, P., Davis, E., Delaney, E., Frohm, B., Bauer, M., Cedervall, T., O'Connell, D., Akerfeldt, K. S. and Linse, S.

Calcium-Dependent Interaction of Calmodulin with Human 80s Ribosomes and Polyribosomes

Biochemistry, 2012, 51, 6718-6727, 10.1021/bi3005939