ORCID Profile
0000-0002-6992-0601
Current Organisation
National Cancer Institute
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Biochemistry and Cell Biology | Structural Biology (incl. Macromolecular Modelling) | Characterisation of Biological Macromolecules | Cellular Immunology | Proteomics and Intermolecular Interactions (excl. Medical Proteomics) |
Expanding Knowledge in the Biological Sciences | Immune System and Allergy | Infectious Diseases
Publisher: Elsevier BV
Date: 2021
Publisher: Elsevier BV
Date: 03-2010
DOI: 10.1016/J.STR.2010.01.001
Abstract: Mg-chelatase catalyzes the first committed step of the chlorophyll biosynthetic pathway, the ATP-dependent insertion of Mg(2+) into protoporphyrin IX (PPIX). Here we report the reconstruction using single-particle cryo-electron microscopy of the complex between subunits BchD and BchI of Rhodobacter capsulatus Mg-chelatase in the presence of ADP, the nonhydrolyzable ATP analog AMPPNP, and ATP at 7.5 A, 14 A, and 13 A resolution, respectively. We show that the two AAA+ modules of the subunits form a unique complex of 3 dimers related by a three-fold axis. The reconstructions demonstrate substantial differences between the conformations of the complex in the presence of ATP and ADP, and suggest that the C-terminal integrin-I domains of the BchD subunits play a central role in transmitting conformational changes of BchI to BchD. Based on these data a model for the function of magnesium chelatase is proposed.
Publisher: American Association for the Advancement of Science (AAAS)
Date: 08-11-2013
Abstract: The regulation of gene expression is critical for almost every aspect of biology. Transcription—generating an RNA copy of a gene—requires the assembly of a large pre-initiation complex (PIC) at every RNA polymerase II (pol II) promoter. Roughly 32 proteins—the subunits of pol II and the general transcription factors—form a PIC that can recognize a minimal TATA-box promoter, select a transcription start site, and synthesize a nascent transcript. Murakami et al. (p. 10.1126/science.1238724 , published online 26 September see the Perspective by Malik and Roeder ) determined the three-dimensional map of the Saccharomyces cerevisiae 30-subunit PIC using cryo-electron microscopy. The saddle-shaped TATA binding protein, the boot-shaped transcription factor IIA (TFIIA), and promoter DNA ∼27 bp downstream of the TATA-box could all be seen. Cross-linking and mass spectrometry was used to determine the spatial proximity of the 30 subunits, revealing that the PIC forms two lobes with TFIIF forming a bridge between them.
Publisher: Elsevier BV
Date: 2020
Publisher: American Association for the Advancement of Science (AAAS)
Date: 17-07-2015
Abstract: Electron microscopy is a powerful technique for taking snapshots of particles or images at near-atomic resolution. Park et al. studied free-floating platinum nanoparticles using electron microscopy and liquid cells (see the Perspective by Colliex). Using analytical techniques developed to study biological molecules, they reconstructed the threedimensional features of the Pt particles at near-atomic resolution. This approach has the scope to study a mixed population of particles one at a time and to study their synthesis as it occurs in solution. Science , this issue p. 290 see also p. 232
Publisher: MDPI AG
Date: 18-07-2017
Publisher: American Chemical Society (ACS)
Date: 08-01-2021
Publisher: Elsevier BV
Date: 11-2009
DOI: 10.1016/J.STR.2009.09.007
Abstract: The general transcription factor IID (TFIID) is required for initiation of RNA polymerase II-dependent transcription at many eukaryotic promoters. TFIID comprises the TATA-binding protein (TBP) and several conserved TBP-associated factors (TAFs). Recognition of the core promoter by TFIID assists assembly of the preinitiation complex. Using cryo-electron microscopy in combination with methods for ab initio single-particle reconstruction and heterogeneity analysis, we have produced density maps of two conformational states of Schizosaccharomyces pombe TFIID, containing and lacking TBP. We report that TBP-binding is coupled to a massive histone-fold domain rearrangement. Moreover, docking of the TBP-TAF1(N-terminus) atomic structure to the TFIID map and reconstruction of a TAF-promoter DNA complex helps to account for TAF-dependent regulation of promoter-TBP and promoter-TAF interactions.
Publisher: Elsevier BV
Date: 10-2017
DOI: 10.1016/J.SBI.2017.03.003
Abstract: Cryogenic electron microscopy (cryo-EM) and single-particle analysis now enables the determination of high-resolution structures of macromolecular assemblies that have resisted X-ray crystallography and other approaches. Successful high-resolution structure determination by cryo-EM always depends on the quality of the protein s le. While structural heterogeneity remains a key challenge for cryo-EM, it also represents a rare opportunity to study the intrinsic conformational flexibility of macromolecular assemblies. Here, we review the key technological advancements that have made this 'resolution revolution' possible and give a concise overview of the technical challenges that needed to be overcome to allow high-resolution structure determination.
Publisher: American Association for the Advancement of Science (AAAS)
Date: 22-08-2014
Abstract: Size and shape drive the properties of metal nanoparticles. Understanding the factors that affect their growth is central to making use of the particles in a range of applications. Liao et al. tracked the growth of platinum nanoparticle shapes at high resolution using state-of-the-art liquid cells for in situ monitoring inside an electron microscope. The authors tracked changes in the growth rates at different crystal facets caused by differences in the mobility of the capping ligand. Science , this issue p. 916
Publisher: American Association for the Advancement of Science (AAAS)
Date: 29-01-2021
Abstract: Algorithms for atomic-resolution 3D reconstruction of nanocrystals imaged in solution with electron microscopy are introduced.
Publisher: Elsevier BV
Date: 09-2019
DOI: 10.1016/J.JSB.2019.07.004
Abstract: Cryogenic electron microscopy (cryo-EM) allows structure determination of macromolecular assemblies that have resisted other structural biology approaches because of their size and heterogeneity. These challenging multi-protein targets are typically susceptible to dissociation and/or denaturation upon cryo-EM grid preparation, and often require crosslinking prior to freezing. Several approaches for gentle on-column or in-tube crosslinking have been developed. On-column crosslinking is not widely applicable because of the poor separation properties of gel filtration techniques. In-tube crosslinking frequently causes s le aggregation and/or precipitation. Gradient-based crosslinking through the GraFix method is more robust, but very time-consuming and necessitates specialised expensive equipment. Furthermore, removal of the glycerol typically involves significant s le loss and may cause destabilization detrimental to the s le quality. Here, we introduce an alternative procedure: AgarFix (Agarose Fixation). The s le is embedded in an agarose matrix that keeps the molecules separated, thus preventing formation of aggregates upon cross-inking. Gentle crosslinking is accomplished by diffusion of the cross-linker into the agarose drop. The s le is recovered by diffusion or electroelution and can readily be used for cryo-EM specimen preparation. AgarFix requires minimal equipment and basic lab experience, making it widely accessible to the cryo-EM community.
Publisher: Elsevier BV
Date: 06-2016
DOI: 10.1016/J.STR.2016.04.006
Abstract: A critical step in the analysis of novel cryogenic electron microscopy (cryo-EM) single-particle datasets is the identification of homogeneous subsets of images. Methods for solving this problem are important for data quality assessment, ab initio 3D reconstruction, and analysis of population ersity due to the heterogeneous nature of macromolecules. Here we formulate a stochastic algorithm for identification of homogeneous subsets of images. The purpose of the method is to generate improved 2D class averages that can be used to produce a reliable 3D starting model in a rapid and unbiased fashion. We show that our method overcomes inherent limitations of widely used clustering approaches and proceed to test the approach on six publicly available experimental cryo-EM datasets. We conclude that, in each instance, ab initio 3D reconstructions of quality suitable for initialization of high-resolution refinement are produced from the cluster centers.
Publisher: American Society for Microbiology
Date: 05-07-2017
Abstract: An unorthodox, surprising mechanism of resistance to the antibiotic linezolid was revealed by cryo-electron microscopy (cryo-EM) in the 70S ribosomes from a clinical isolate of Staphylococcus aureus . This high-resolution structural information demonstrated that a single amino acid deletion in ribosomal protein uL3 confers linezolid resistance despite being located 24 Å away from the linezolid binding pocket in the peptidyl-transferase center. The mutation induces a cascade of allosteric structural rearrangements of the rRNA that ultimately results in the alteration of the antibiotic binding site. IMPORTANCE The growing burden on human health caused by various antibiotic resistance mutations now includes prevalent Staphylococcus aureus resistance to last-line antimicrobial drugs such as linezolid and daptomycin. Structure-informed drug modification represents a frontier with respect to designing advanced clinical therapies, but success in this strategy requires rapid, facile means to shed light on the structural basis for drug resistance (D. Brown, Nat Rev Drug Discov 14:821–832, 2015, 0.1038/nrd4675 ). Here, detailed structural information demonstrates that a common mechanism is at play in linezolid resistance and provides a step toward the redesign of oxazolidinone antibiotics, a strategy that could thwart known mechanisms of linezolid resistance.
Publisher: Elsevier BV
Date: 04-2008
Publisher: American Association for the Advancement of Science (AAAS)
Date: 03-04-2020
Abstract: A challenge in the fabrication of nanoparticles is that even for particles of uniform size, there will still be a distribution in the atomic arrangements and surface capping ligands from one particle to the next. Using liquid-cell transmission electron microscopy, Kim et al. reconstructed the structure of in idual nanocrystals synthesized in one batch while they were still in solution. A comparison of multiple particles showed structural heterogeneity and differences between the interior and the outer shell of the in idual nanoparticles, as well as nanoparticles containing extended defects and thus differences in internal strain, all of which can affect the physical and chemical properties of each particle. Science , this issue p. 60
Publisher: MDPI AG
Date: 04-07-2019
DOI: 10.3390/IJMS20133290
Abstract: The general transcription factor TFIID is a core promoter selectivity factor that recognizes DNA sequence elements and nucleates the assembly of a pre-initiation complex (PIC). The mechanism by which TFIID recognizes the promoter is poorly understood. The TATA-box binding protein (TBP) is a subunit of the multi-protein TFIID complex believed to be key in this process. We reconstituted transcription from highly purified components on a ribosomal protein gene (RPS5) and discovered that TFIIDΔTBP binds and rearranges the promoter DNA topology independent of TBP. TFIIDΔTBP binds ~200 bp of the promoter and changes the DNA topology to a larger extent than the nucleosome core particle. We show that TBP inhibits the DNA binding activities of TFIIDΔTBP and conclude that the complete TFIID complex may represent an auto-inhibited state. Furthermore, we show that the DNA binding activities of TFIIDΔTBP are required for assembly of a PIC poised to select the correct transcription start site (TSS).
Publisher: Proceedings of the National Academy of Sciences
Date: 24-10-2006
Abstract: CDK8 (cyclin-dependent kinase 8), along with CycC, Med12, and Med13, form a repressive module (the Cdk8 module) that prevents RNA polymerase II (pol II) interactions with Mediator. Here, we report that the ability of the Cdk8 module to prevent pol II interactions is independent of the Cdk8-dependent kinase activity. We use electron microscopy and single-particle reconstruction to demonstrate that the Cdk8 module forms a distinct structural entity that binds to the head and middle region of Mediator, thereby sterically blocking interactions with pol II.
Publisher: Elsevier BV
Date: 08-2017
DOI: 10.1016/J.DRUGALCDEP.2017.03.023
Abstract: Tobacco smoking is a major cause of morbidity and mortality among people living with HIV (PLHIV). Due to the limited success of standard abstinence-focused smoking cessation strategies in this population, there is growing interest in tobacco harm reduction (THR) approaches as an additional strategy to address these high smoking rates. This study explored the attitudes of health practitioners who provide healthcare to PLHIV towards THR. 179 Australian health practitioners who provide healthcare to PLHIV completed an online survey that measured their attitudes towards THR approaches, including switching from cigarettes to e-cigarettes or vaporised nicotine products (VNPs). Respondents supported the concept of THR but were undecided on the role of VNPs. Respondents most commonly reported 'don't know' or 'undecided' responses to statements regarding VNPs. More respondents, however, agreed than disagreed that switching from smoking to long-term vaping could reduce risk (36% and 22% respectively) and be an effective strategy to help PLHIV to quit smoking (37% agree and 17% disagree). Only a minority of respondents (20%) agreed that VNPs are too harmful to recommend to patients, however around half (53%) were undecided. Despite supporting the principle of THR, health practitioners may require more evidence and knowledge about VNPs before being willing to consider them as a suitable intervention strategy.
Publisher: Wiley
Date: 06-09-2017
DOI: 10.1002/PRO.3266
Publisher: Elsevier BV
Date: 2008
DOI: 10.1016/J.JMB.2007.11.028
Abstract: The generation of ab initio three-dimensional (3D) models is a bottleneck in the studies of large macromolecular assemblies by single-particle cryo-electron microscopy. We describe here a novel method, in which established methods for two-dimensional image processing are combined with newly developed programs for joint rotational 3D alignment of a large number of class averages (RAD) and calculation of 3D volumes from aligned projections (VolRec). We demonstrate the power of the method by reconstructing an approximately 660-kDa ATP-fueled AAA+ motor to 7.5 A resolution, with secondary structure elements identified throughout the structure. We propose the method as a generally applicable automated strategy to obtain 3D reconstructions from unstained single particles imaged in vitreous ice.
Publisher: Elsevier BV
Date: 11-2018
DOI: 10.1016/J.JSB.2018.08.005
Abstract: Cryogenic electron microscopy (cryo-EM) and single-particle analysis enables determination of near-atomic resolution structures of biological molecules. However, large computational requirements limit throughput and rapid testing of new image processing tools. We developed PRIME, an algorithm part of the SIMPLE software suite, for determination of the relative 3D orientations of single-particle projection images. PRIME has primarily found use for generation of an initial ab initio 3D reconstruction. Here we show that the strategy behind PRIME, iterative estimation of per-particle orientation distributions with stochastic hill climbing, provides a competitive approach to near-atomic resolution single-particle 3D reconstruction. A number of mathematical techniques for accelerating the convergence rate are introduced, leading to a speedup of nearly two orders of magnitude. We benchmarked our developments on numerous publicly available data sets and conclude that near-atomic resolution ab initio 3D reconstructions can be obtained with SIMPLE in a matter of hours, using standard over-the-counter CPU workstations.
Publisher: Springer Science and Business Media LLC
Date: 28-03-2016
DOI: 10.1038/NSMB.3196
Publisher: Elsevier BV
Date: 07-2009
DOI: 10.1016/J.JSB.2009.04.009
Abstract: Three-dimensional (3D) structure determination from electron microscopic images of single molecules can be difficult for particles with low or no internal symmetry, and for images with low signal-to-noise ratio (SNR), due to the existence of false maxima in the scoring function used for orientation search. In attempt to improve robustness of orientation parameter refinement towards noise and poor starting reconstruction quality, we have developed a method for common lines-based orientation search in Fourier space. The Fourier-space formulation enables inclusion of resolution (spatial frequency of the low-pass limit) as a variable that is adjusted in a particle-dependent, self-adaptive manner. The method allows for the underlying 3D structure to be estimated to high resolution, and requires only a crude, low-resolution reconstruction as starting-point for refinement. Benchmarking of the method is performed on experimental and synthetic data.
Publisher: Oxford University Press (OUP)
Date: 18-06-2020
DOI: 10.1093/NAR/GKAA519
Abstract: The poliovirus type I IRES is able to recruit ribosomal machinery only in the presence of host factor PCBP2 that binds to stem–loop IV of the IRES. When PCBP2 is cleaved in its linker region by viral proteinase 3CD, translation initiation ceases allowing the next stage of replication to commence. Here, we investigate the interaction of PCBP2 with the apical region of stem–loop IV (SLIVm) of poliovirus RNA in its full-length and truncated form. CryoEM structure reconstruction of the full-length PCBP2 in complex with SLIVm solved to 6.1 Å resolution reveals a compact globular complex of PCBP2 interacting with the cruciform RNA via KH domains and featuring a prominent GNRA tetraloop. SEC-SAXS, SHAPE and hydroxyl-radical cleavage establish that PCBP2 stabilizes the SLIVm structure, but upon cleavage in the linker domain the complex becomes more flexible and base accessible. Limited proteolysis and REMSA demonstrate the accessibility of the linker region in the PCBP2/SLIVm complex and consequent loss of affinity of PCBP2 for the SLIVm upon cleavage. Together this study sheds light on the structural features of the PCBP2/SLIV complex vital for ribosomal docking, and the way in which this key functional interaction is regulated following translation of the poliovirus genome.
Publisher: Springer Science and Business Media LLC
Date: 04-02-2121
DOI: 10.1038/NCOMMS10588
Abstract: The membrane attack complex (MAC) erforin-like protein complement component 9 (C9) is the major component of the MAC, a multi-protein complex that forms pores in the membrane of target pathogens. In contrast to homologous proteins such as perforin and the cholesterol-dependent cytolysins (CDCs), all of which require the membrane for oligomerisation, C9 assembles directly onto the nascent MAC from solution. However, the molecular mechanism of MAC assembly remains to be understood. Here we present the 8 Å cryo-EM structure of a soluble form of the poly-C9 component of the MAC. These data reveal a 22-fold symmetrical arrangement of C9 molecules that yield an 88-strand pore-forming β-barrel. The N-terminal thrombospondin-1 (TSP1) domain forms an unexpectedly extensive part of the oligomerisation interface, thus likely facilitating solution-based assembly. These TSP1 interactions may also explain how additional C9 subunits can be recruited to the growing MAC subsequent to membrane insertion.
Publisher: American Association for the Advancement of Science (AAAS)
Date: 04-05-2021
DOI: 10.1126/SCISIGNAL.ABC4078
Abstract: Mutations that dysregulate a protein complex may promote cancer metastasis by enhancing Rac1 activation.
Publisher: Elsevier BV
Date: 08-2013
DOI: 10.1016/J.STR.2013.07.002
Abstract: Low-dose electron microscopy of cryo-preserved in idual biomolecules (single-particle cryo-EM) is a powerful tool for obtaining information about the structure and dynamics of large macromolecular assemblies. Acquiring images with low dose reduces radiation damage, preserves atomic structural details, but results in low signal-to-noise ratio of the in idual images. The projection directions of the two-dimensional images are random and unknown. The grand challenge is to achieve the precise three-dimensional (3D) alignment of many (tens of thousands to millions) noisy projection images, which may then be combined to obtain a faithful 3D map. An accurate initial 3D model is critical for obtaining the precise 3D alignment required for high-resolution (<10 Å) map reconstruction. We report a method (PRIME) that, in a single step and without prior structural knowledge, can generate an accurate initial 3D map directly from the noisy images.
Publisher: American Chemical Society (ACS)
Date: 15-04-2011
DOI: 10.1021/BI200058A
Abstract: Thioredoxin and thioredoxin reductase can regulate cell metabolism through redox regulation of disulfide bridges or through removal of H(2)O(2). These two enzymatic functions are combined in NADPH-dependent thioredoxin reductase C (NTRC), which contains an N-terminal thioredoxin reductase domain fused with a C-terminal thioredoxin domain. Rice NTRC exists in different oligomeric states, depending on the absence or presence of its NADPH cofactor. It has been suggested that the different oligomeric states may have erse activity. Thus, the redox status of the chloroplast could influence the oligomeric state of NTRC and thereby its activity. We have characterized the oligomeric states of NTRC from barley (Hordeum vulgare L.). This also includes a structural model of the tetrameric NTRC derived from cryo-electron microscopy and single-particle reconstruction. We conclude that the tetrameric NTRC is a dimeric arrangement of two NTRC homodimers. Unlike that of rice NTRC, the quaternary structure of barley NTRC complexes is unaffected by addition of NADPH. The activity of NTRC was tested with two different enzyme assays. The N-terminal part of NTRC was tested in a thioredoxin reductase assay. A peroxide sensitive Mg-protoporphyrin IX monomethyl ester (MPE) cyclase enzyme system of the chlorophyll biosynthetic pathway was used to test the catalytic ability of both the N- and C-terminal parts of NTRC. The different oligomeric assembly states do not exhibit significantly different activities. Thus, it appears that the activities are independent of the oligomeric state of barley NTRC.
Publisher: Elsevier BV
Date: 12-2012
DOI: 10.1016/J.JSB.2012.07.010
Abstract: The open source software suite SIMPLE: Single-particle IMage Processing Linux Engine provides data analysis methods for single-particle cryo-electron microscopy (cryo-EM). SIMPLE addresses the problem of obtaining 3D reconstructions from 2D projections only, without using an input reference volume for approximating orientations. The SIMPLE reconstruction algorithm is tailored to asymmetrical and structurally heterogeneous single-particles. Its basis is global optimization with the use of Fourier common lines. The advance that enables ab initio reconstruction and heterogeneity analysis is the separation of the tasks of in-plane alignment and projection direction determination via bijective orientation search - a new concept in common lines-based strategies. Bijective orientation search ides the configuration space into two groups of paired parameters that are optimized separately. The first group consists of the rotations and shifts in the plane of the projection the second group consists of the projection directions and state assignments. In SIMPLE, ab initio reconstruction is feasible because the 3D in-plane alignment is approximated using reference-free 2D rotational alignment. The subsequent common lines-based search hence searches projection directions and states only. Thousands of class averages are analyzed simultaneously in a matter of hours. Novice SIMPLE users get a head start via the well documented front-end. The structured, object-oriented back-end invites advanced users to develop new alignment and reconstruction algorithms. An overview of the package is presented together with benchmarks on simulated data. Executable binaries, source code, and documentation are available at simple.stanford.edu.
Publisher: American Chemical Society (ACS)
Date: 04-2008
DOI: 10.1021/BI800052M
Publisher: Annual Reviews
Date: 02-06-2015
DOI: 10.1146/ANNUREV-BIOCHEM-060614-034226
Abstract: About 20 years ago, the first three-dimensional (3D) reconstructions at subnanometer ( -Å) resolution of an icosahedral virus assembly were obtained by cryogenic electron microscopy (cryo-EM) and single-particle analysis. Since then, thousands of structures have been determined to resolutions ranging from 30 Å to near atomic ( Å). Almost overnight, the recent development of direct electron detectors and the attendant improvement in analysis software have advanced the technology considerably. Near-atomic-resolution reconstructions can now be obtained, not only for megadalton macromolecular complexes or highly symmetrical assemblies but also for proteins of only a few hundred kilodaltons. We discuss the developments that led to this breakthrough in high-resolution structure determination by cryo-EM and point to challenges that lie ahead.
Publisher: AIP Publishing
Date: 21-04-2015
DOI: 10.1063/1.4918726
Abstract: Intense femtosecond x-ray pulses from free-electron laser sources allow the imaging of in idual particles in a single shot. Early experiments at the Linac Coherent Light Source (LCLS) have led to rapid progress in the field and, so far, coherent diffractive images have been recorded from biological specimens, aerosols, and quantum systems with a few-tens-of-nanometers resolution. In March 2014, LCLS held a workshop to discuss the scientific and technical challenges for reaching the ultimate goal of atomic resolution with single-shot coherent diffractive imaging. This paper summarizes the workshop findings and presents the roadmap toward reaching atomic resolution, 3D imaging at free-electron laser sources.
Publisher: Elsevier BV
Date: 08-2006
DOI: 10.1016/J.MICRON.2005.11.014
Abstract: Three-dimensional (3D) reconstructions of the two 8.4 MDa Rapana thomasiana hemocyanin isoforms, RtH1 and RtH2, have been obtained by cryoelectron microscopy of molecules embedded in vitreous ice and single particle image processing. The final 3D structures of the RtH1 and RtH2 didecamers at 19 A and 16 A resolution, respectively, are very similar to earlier reconstructions of gastropodan hemocyanins, revealing structural features such as the obliquely oriented subunits, the five- and two-fold symmetrical axes. Three new interactions are defined two of them connecting the arch and the wall while the third is formed between the collar and the wall. The collar-wall connection and one of the arch-wall connections are positioned between two in idual subunit dimers, while the second arch-wall connection is located between two subunits within the subunit dimer. All three interactions establish connections to the first tier of the wall. Furthermore, for each interaction we have allocated two first tier functional units most likely involved in forming the connections.
Publisher: Elsevier BV
Date: 07-2010
DOI: 10.1016/J.STR.2010.06.001
Abstract: We have developed methods for ab initio three-dimensional (3D) structure determination from projection images of randomly oriented single molecules coexisting in multiple functional states, to aid the study of complex s les of macromolecules and nanoparticles by electron microscopy (EM). New algorithms for the determination of relative 3D orientations and conformational state assignment of single-molecule projection images are combined with well-established techniques for alignment and statistical image analysis. We describe how the methodology arrives at homogeneous groups of images aligned in 3D and discuss application to experimental EM data sets of the Escherichia coli ribosome and yeast RNA polymerase II.
Location: United States of America
Location: Sweden
Start Date: 2016
End Date: 2016
Funder: Australian Research Council
View Funded ActivityStart Date: 2009
End Date: 2010
Funder: Swedish Research Council
View Funded ActivityStart Date: 2017
End Date: 2019
Funder: Australian Research Council
View Funded ActivityStart Date: 2018
End Date: 2020
Funder: National Health and Medical Research Council
View Funded ActivityStart Date: 2016
End Date: 2018
Funder: National Health and Medical Research Council
View Funded ActivityStart Date: 2017
End Date: 2019
Funder: National Health and Medical Research Council
View Funded ActivityStart Date: 2017
End Date: 2019
Funder: National Health and Medical Research Council
View Funded ActivityStart Date: 2017
End Date: 2017
Funder: Australian Research Council
View Funded ActivityStart Date: 2017
End Date: 12-2020
Amount: $399,500.00
Funder: Australian Research Council
View Funded ActivityStart Date: 04-2017
End Date: 12-2017
Amount: $850,000.00
Funder: Australian Research Council
View Funded ActivityStart Date: 2016
End Date: 12-2016
Amount: $590,000.00
Funder: Australian Research Council
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