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Professor Jill Trewhella

Deputy Vice-Chancellor (Research)

A14 - The Quadrangle
The University of Sydney

Telephone +61 2 8627 8150

Biographical details

Jill Trewhella is a Professor in the School of Molecular Bioscience and Deputy Vice-Chancellor (Research) at the University of Sydney. As DVC Research (since 2009) she has overseen the development of major collaborative, cross-disciplinary research programs with supporting infrastructure; such as the newly established Charles Perkins Centre that focuses on solutions for individuals and communities for the problems arising from the increasing incidence of obesity.

She earned BSc and MSc degrees in Mathematics and Physics (UNSW) and a PhD in Chemistry (University of Sydney) before moving to the USA for 25 years where she held significant leadership positions while pursuing her research. She was the founding Leader of the multi-disciplinary Bioscience Division, with more than 300 researchers working on projects such as the Human Genome Project, Structural Genomics of TB, the international HIV AIDS Gene Data Base, and stewarding National Institutes of Health research resources for flow cytometry and stable isotopes.

She returned to Australia in 2005 as an Australian Research Council Federation Fellow having gained international recognition for her contributions to our understanding of the molecular communication underpinning healthy function, with a particular emphasis on heart muscle proteins.

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Research interests

Jill is a biophysicist who uses physical methods to study bio-molecular structures as a basis for understanding their function. A major focus of her work is on the structural biology of how bio-molecules interact and communicate in order to carry out functions that involve multiple molecular actors working in concert. This work requires a multidisciplinary approach using molecular biology, biochemistry, and biophysical tools. One frequently used biophysical tool is the small-angle scattering of x-rays and neutrons in order to probe the solution conformations of proteins and the complexes they form in a wide variety of conditions and states of activity.

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Associations

  • Joint appointment at the Bragg Institute, Australian Nuclear Sciences and Technology Organisation (ANSTO)
  • Adjunct Professor of Chemistry, University of Utah

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Awards and honours

  • Fellow, Royal Society of New South Wales, 2011
  • Fellow, American Neutron Scattering Society, 2010
  • Rotary Centennial Award for Professional Excellence, 2005
  • Australian Federation Fellowship Award, to conduct research on “Molecular Mechanisms of Biochemical Regulation: Neutron and X-ray Scattering Studies,” 2004
  • AAAS Women in Science and Engineering Lecture Series in Latin America, showcasing the achievements of U.S. women scientists to wide audiences of scientists, educators, students, and policy-makers in Latin America. One of nine selected for the 2003-2004 lecture series.
  • NNSA Coin award for Exceptional Service for leadership after September 11 in the pursuit of the anthrax attacks and for creating a focus for new bio-threat capabilities in the Lab, including the successful creation of a BSL-3 facility
  • Fellow, American Association for the Advancement of Science, 2000
  • Outstanding Mentor Award, Los Alamos National Laboratory, 1999
  • Fellow, Los Alamos National Laboratory, in recognition of sustained outstanding scientific contributions, 1995
  • Fellows Prize, Los Alamos National Laboratory, in recognition of important contributions to the understanding of proteins in solution using biophysical measurements, 1995
  • Adjunct Associate Professor, Department of Cell Biology, University of New Mexico, 1989-...
  • University of Sydney Research Studentship, 1980
  • Commonwealth Post Graduate Award, 1975-1979
  • Physics Staff Thesis Prize, University of NSW 1975
  • Undergraduate Physics Prize, University of NSW, 1974

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Selected grants

2012

  • Australian Synchrotron Access Program; Smith I, Trewhella J; Australian Research Council (ARC)/Special Research Initiatives.
  • Molecular foundations for essential fine tuning of regulatory signals in healthy heart function; Trewhella J, Guss J; Australian Research Council (ARC)/Discovery Projects (DP).

2011

  • Structure Studies of Modular Proteins in Signal Transduction; Trewhella J; DVC Research/Bridging Support Grant.
  • Shared resource for protein discovery; Matthews J, Mabbutt B, Brown L, Paulsen I, Stock D, Sunde M, Trewhella J; Australian Research Council (ARC)/Linkage Infrastructure, Equipment and Facilities (LIEF).

2010

  • The structure of the HIV-1 matrix protein with human calmodulin; Trewhella J, Chow J; Australian Nuclear Science and Technology Organisation/Research Support.

2009

  • The structure of the HIV-1 Gag complex with human ESCRT-1; Trewhella J, Chow J; Australian Nuclear Science and Technology Organisation/Research Support.
  • Molecular Mechanisms of two-component signal transduction in bacteria; Trewhella J, Guss J; Australian Research Council/Discovery Projects (DP).
  • Structural basis of familial hypertrophic cardiomyopathy caused by myosin binding protein C; Trewhella J; DVC Research/Bridging Support Grant.

2008

  • 800 MHz NMR spectrometer for biomolecular structure-function analysis; Mackay J, Otting G, Kuchel P, Matthews J, Gell D, Trewhella J, Rutledge P, Messerle B, Vadas M, Graham R, Vandenberg J, Stock D, Ball G, Fazekas De St Groth B, Shine J; Australian Research Council (ARC)/Linkage Infrastructure, Equipment and Facilities (LIEF).
  • Transcriptional complexes in haematopiesis and T-cell Leukaemia; Matthews J, Guss J, Trewhella J; NHMRC/Project Grant.
  • 800 MHz NMR spectrometer for biomolecular structure function analysis; Vadas M, Stock D, Graham R, Shine J, Ball G, Matthews J, Gell D, Trewhella J, Rutledge P, Messerle B, Fazekas De St Groth B, Vandenberg J, Mackay J, Otting G, Kuchel P; Australian Research Council (ARC)/LIEF.
  • Effects of molecular crowding on protein structure - Access to Major Research Facilities Program (AMRFP); Trewhella J; Australian Nuclear Science and Technology Organisation/Access to Major Research Facilities Program.
  • Inhibition of histidine kinase signal sensing: a novel paradigm for antimicrobial development; King G, Guss J, Trewhella J; National Health and Medical Research Council/Project Grants.

2007

  • Structural Biology Centre for HIV/Host Interactions in Trafficking and Assembly; Sundquist W, Trewhella J; National Institutes of Health (USA)/Research Support.
  • Small-Angle Scattering Core for the Center for the Determination of Structures of HIV/Host Interacti; Trewhella J; National Institutes of Health/University of Utah.
  • Studies of the dynamic language of bio-molecular communication and signalling; Trewhella J; Australian Research Council (ARC)/Discovery.

2006

  • 3249 - Structural Studies Of Protein Complexes Aimed At Fundamental Advances In Understanding Life Processes, Including Diseased States; Trewhella J; Australian Institute of Nuclear Science and Engineering/Awards.
  • Facility for Structural Analysis of Bio-Molecular Complexes and Self Assembly; Trewhella J, Warr G, et a, Mabbutt B; Australian Research Council (ARC)/LIEF.
  • Structural characterisation of a natural inhibitor of sporulation bound to its histidine kinase target - NIST and SSRL, 26 May and 2 Jume 2006; Trewhella J; Australian Nuclear Science and Technology Organisation/Travel Grant.

2004

  • Molecular mechanisms of biochemical regulation: Neutron and x-ray scattering studies; Australian Research Council (ARC)/Federation Fellowship (FF).

2001

  • Structure and Dynamics of Protein Kinase A Signaling Complexes; Trewhella J; University of California, Directed Research Development/CULAR Project.

2000

  • Biological Neutron Scattering, a Collaboration with the Oak Ridge Structural Biology Center; Trewhella J; Department of Energy/Office of Biological and Environmental Research/Research Grant.

1998

  • Structural Changes and Signaling in Calcium Regulation; Trewhella J; NIH/Research Grant.
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Selected publications

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Book Chapters

  • Jacques, D., Guss, J., Trewhella, J. (2012). Antikinases: Their Structures and Roles in Two-component Signalling. In Roy Gross, Dagmar Beier (Eds.), Two-component Systems in Bacteria, (pp. 163-180). Norfolk, United Kingdom: Caister Academic Press.
  • Jeffries, C., Trewhella, J. (2012). Small-Angle Scattering. In Michael E. Wall (Eds.), Quantitative Biology: From Molecular to Cellular Systems, (pp. 113-151). Boca Raton, United States of America: CRC Press.
  • Whitten, A., Trewhella, J. (2009). Small-Angle Scattering and Neutron Contrast Variation for Studying Bio-molecular Complexes. In James W. Lee, Robert S. Foote (Eds.), Micro and Nano Technologies in Bioanalysis: Methods and Protocols, (pp. 307-324). New York, USA: Humana Press.
  • Trewhella, J., Krueger, J. (2002). Small-angle solution scattering reveals information on conformational dynamics in calcium-binding proteins and in their interactions with regulatory targets. In Hans J. Vogel (Eds.), Calcium-Binding Protein Protocols, (pp. 137-159). canada: Humana Press.

Journals

  • Mokbel, N., Ilkovski, B., Kreissl, M., Memo, M., Jeffries, C., Marttila, M., Lehtokari, V., Lemola, E., Gronholm, M., Menard, D., Trewhella, J., North, K., Clarke, N., et al (2013). K7del is a common TPM2 gene mutation associated with nemaline myopathy and raised myo�?bre calcium sensitivity. Brain: a journal of neurology, 136(2), 494-507.
  • Taylor, J., Chow, J., Jeffries, C., Kwan, A., Duff, A., Hamilton, W., Trewhella, J. (2012). Calmodulin Binds a Highly Extended HIV-1 MA Protein That Refolds Upon Its Release. Biophysical Journal, 103(3), 541-549.
  • Taraban, M., Weerasekare, M., Trewhella, J., Shi, X., Jeong, E., Yu, Y. (2012). Effects of Gadolinium Chelate on the Evolution of the Nanoscale Structure in Peptide Hydrogels. Peptide Science, 98(1), 50-58.
  • Jacques, D., Guss, J., Svergun, D., Trewhella, J. (2012). Publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution. Acta Crystallographica. Section D: Biological Crystallography, D68(6), 620-626.
  • Jacques, D., Guss, J., Trewhella, J. (2012). Reliable structural interpretation of small-angle scattering data from bio-molecules in solution - the importance of quality control and a standard reporting framework. B M C Structural Biology, 12, 1-3.
  • Bhati, M., Lee, C., Gadd, M., Jeffries, C., Kwan, A., Whitten, A., Trewhella, J., Mackay, J., Matthews, J. (2012). Solution Structure of the LIM-Homeodomain Transcription Factor Complex Lhx3/Ldb1 and the Effects of a Pituitary Mutation on Key Lhx3 Interactions. PLoS One, 7(7), 1-9.
  • Hynson, R., Jeffries, C., Trewhella, J., Cocklin, S. (2012). Solution structure studies of monomeric human TIP47/perilipin-3 reveal a highly extended conformation. Proteins: Structure, Function, and Bioinformatics, 80(8), 2046-2055.
  • Lu, Y., Kwan, A., Jeffries, C., Guss, J., Trewhella, J. (2012). The Motif of Human Cardiac Myosin-binding Protein C Is Required for Its Ca2+ -dependent Interaction with Calmodulin. Journal of Biological Chemistry, 287(37), 31596-31607.
  • Gao, J., Lu, Y., Browne, G., Yap, B., Trewhella, J., Hunter, N., Nguyen, K. (2012). The role of heme-binding by DNA-protective protein from starved-cells (Dps) in the tolerance of Porphyromonas gingivalis to heme toxicity. Journal of Biological Chemistry, 287(50), 42243-42258.
  • Jacques, D., Langley, D., Hynson, R., Whitten, A., Kwan, A., Guss, J., Trewhella, J. (2011). A Novel Structure of an Antikinase and Its Inhibitor. Journal of Molecular Biology, 405(1), 214-226.
  • Zhai, Q., Landesman, M., Chung, H., Dierkers, A., Jeffries, C., Trewhella, J., Hill, C., Sundquist, W. (2011). Activation of the Retroviral Budding Factor ALIX. Journal of Virology, 85(17), 9222-9226.
  • Taraban, M., Ramachandran, S., Gryczynski, I., Gryczynski, Z., Trewhella, J., Yu, Y. (2011). Effects of chain length on oligopeptide hydrogelation. Soft Matter, 7, 2624-2631.
  • Johansen, D., Jeffries, C., Hammouda, B., Trewhella, J., Goldenberg, D. (2011). Effects of Macromolecular Crowding on an Intrinsically Disordered Protein Characterized by Small-Angle Neutron Scattering with Contrast Matching. Biophysical Journal, 100(4), 1120-1128.
  • Johansen, D., Trewhella, J., Goldenberg, D. (2011). Fractal dimension of an intrinsically disordered protein: Small-angle X-ray scattering and computational study of the bacteriophage Lambda N protein. Protein Science, 20(12), 1955-1970.
  • Jeffries, C., Lu, Y., Hynson, R., Taylor, J., Ballesteros, M., Kwan, A., Trewhella, J. (2011). Human Cardiac Myosin Binding Protein C: Structural Flexibility within an Extended Modular Architecture. Journal of Molecular Biology, 414(5), 735-748.
  • Lu, Y., Jeffries, C., Trewhella, J. (2011). Invited review: Probing the structures of muscle regulatory proteins using small-angle solution scattering. Biopolymers: original research on biological molecules and assemblies, 95(8), 505-516.
  • Trewhella, J. (2011). Reflections of a Woman Scientist in the Year 2011. Australian Journal of Chemistry: an international journal for chemical science, 64(6), 666-668.
  • Weerasekare, M., Taraban, M., Shi, X., Jeong, E., Trewhella, J., Yu, Y. (2011). Sol and Gel States in Peptide Hydrogels Visualized by Gd(III)-enhanced Magnetic Resonance Imaging. Biopolymers: original research on biological molecules and assemblies, 96(6), 734-743.
  • Gadd, M., Bhati, M., Jeffries, C., Langley, D., Trewhella, J., Guss, J., Matthews, J. (2011). Structural Basis for Partial Redundancy in a Class of Transcription Factors, the LIM Homeodomain Proteins, in Neural Cell Type Specification. Journal of Biological Chemistry, 286(50), 42971-42980.
  • Lu, Y., Kwan, A., Trewhella, J., Jeffries, C. (2011). The C0C1 Fragment of Human Cardiac Myosin Binding Protein C Has Common Binding Determinants for Both Actin and Myosin. Journal of Molecular Biology, 413(5), 908-913.
  • Orlova, A., Galkin, V., Jeffries, C., Egelman, E., Trewhella, J. (2011). The N-Terminal Domains of Myosin Binding Protein C Can Bind Polymorphically to F-Actin. Journal of Molecular Biology, 412(3), 379-386.
  • Jacques, D., Langley, D., Kuramitsu, S., Yokoyama, S., Trewhella, J., Guss, J. (2011). The structure of TTHA0988 from Thermus thermophilus, a KipI-KipA homologue incorrectly annotated as an allophanate hydrolase. Acta Crystallographica. Section D: Biological Crystallography, 67(2), 105-111.
  • Hynson, R., Kwan, A., Jacques, D., Mackay, J., Trewhella, J. (2010). (1)H, (13)C and (15)N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis. Biomolecular N M R Assignments, 4(2), 167-169.
  • Siddiqui, K., Poljak, A., De Francisci, D., Guerriero, G., Pilak, O., Burg, D., Raftery, M., Parkin, D., Trewhella, J., Cavicchioli, R. (2010). A chemically modified alpha-amylase with a molten-globule state has entropically driven enhanced thermal stability. Protein Engineering Design and Selection (Print), 23(10), 769-780.
  • Chow, J., Jeffries, C., Kwan, A., Guss, J., Trewhella, J. (2010). Calmodulin Disrupts the Structure of the HIV-1 MA Protein. Journal of Molecular Biology, 400(4), 702-714.
  • Fenton, A., Williams, R., Trewhella, J. (2010). Changes in Small-Angle X-ray Scattering Parameters Observed upon Binding of Ligand to Rabbit Muscle Pyruvate Kinase are not Correlated with Allosteric Transitions. Biochemistry, 49(33), 7202-7209.
  • Ramachandran, S., Taraban, M., Trewhella, J., Gryczynski, I., Gryczynski, Z., Yu, Y. (2010). Effect of Temperature During Assembly on the Structure and Mechanical Properties of Peptide-Based Materials. Biomacromolecules, 11(6), 1502-1506.
  • Cross, A., Jeffries, C., Trewhella, J., Matthews, J. (2010). LIM Domain Binding Proteins 1 and 2 Have Different Oligomeric States. Journal of Molecular Biology, 399(1), 133-144.
  • Jacques, D., Trewhella, J. (2010). Small-angle scattering for structural biology - Expanding the frontier while avoiding the pitfalls. Protein Science, 19(4), 642-657.
  • Comoletti, D., Miller, M., Jeffries, C., Wilson, J., Demeler, B., Taylor, P., Trewhella, J., Nakagawa, T. (2010). The Macromolecular Architecture of Extracellular Domain of alphaNRXN1: Domain Organization, Flexibility, and Insights into Trans-Synaptic Disposition. Structure, 18(8), 1044-1053.
  • Siddiqui, K., Parkin, D., Curmi, P., De Francisci, D., Poljak, A., Barrow, K., Noble, M., Trewhella, J., Cavicchioli, R. (2009). A Novel Approach for Enhancing the Catalytic Efficiency of a Protease at Low Temperature: Reduction in Substrate Inhibition by Chemical Modification. Biotechnology and Bioengineering, 103(4), 676-686.
  • Claridge, J., Headey, S., Chow, J., Schwalbe, M., Edwards, P., Jeffries, C., Venugopal, H., Trewhella, J., Pascal, S. (2009). A picornaviral loop-to-loop replication complex. Journal of Structural Biology, 166(3), 251-262.
  • Mills, R., Trewhella, J., Qiu, T., Welte, T., Ryan, T., Hanley, T., Knott,, R., Lithgow, T., Mulhern, T. (2009). Domain organization of the monomeric form of the Tom70 mitochondrial import receptor. Journal of Molecular Biology, 388(5), 1043-1058.
  • Whitten, A., Smith, B., Menting, J., Margetts, M., McKern, N., Lovrecz, G., Adams, T., Richards, K., Bentley, J., Trewhella, J., et al (2009). Solution Structure of Ectodomains of the Insulin Receptor Family: The Ectodomain of the Type 1 Insulin-Like Growth Factor Receptor Displays Asymmetry of Ligand Binding Accompanied by Limited Conformational Change. Journal of Molecular Biology, 394(5), 878-892.
  • Jacques, D., Streamer, M., Rowland, S., King, G., Guss, J., Trewhella, J., Langley, D. (2009). Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state. Acta Crystallographica. Section D: Biological Crystallography, 65(6), 574-581.
  • Whitten, A., Jeffries, C., Harris, S., Trewhella, J. (2008). Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function. Proceedings of the National Academy of Sciences (PNAS), 105(47), 18360-18365.
  • Comoletti, D., Grishaev, A., Whitten, A., Taylor, P., Trewhella, J. (2008). Characterization of the solution structure of a neuroligin/β-neurexin complex. Chemico-Biological Interactions, 175, 150-155.
  • Griffin, M., Dobson, R., Pearce, F., Antonio, L., Whitten, A., Liew, C., Mackay, J., Trewhella, J., Jameson, G., Perugini, M., et al (2008). Evolution of quaternary structure in a homotetrameric enzyme. Journal of Molecular Biology, 380(4), 691-703.
  • Jacques, D., Langley, D., Jeffries, C., Cunningham, K., Burkholder, W., Guss, J., Trewhella, J. (2008). Histidine Kinase Regulation by a Cyclophilin-like Inhibitor. Journal of Molecular Biology, 384(2), 422-435.
  • Taraban, M., Zhan, H., Whitten, A., Langley, D., Matthews, K., Swint-Kruse, L., Trewhella, J. (2008). Ligand-induced conformational changes and conformational dynamics in the solution structure of the lactose repressor protein. Journal of Molecular Biology, 376(2), 466-481.
  • Whitten, A., Cai, S., Trewhella, J. (2008). MULCh: ModULes for the Analysis of Small-angle Neutron Contrast Variation Data from Biomolecular Assemblies. Journal of Applied Crystallography, 41(1), 222-226.
  • Grishaev, A., Tugarinov, V., Kay, L., Trewhella, J., Bax, A. (2008). Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints. Journal of Biomolecular NMR, 40(2), 95-106.
  • Wang, Y., Trewhella, J., Goldenberg, D. (2008). Small-angle X-ray scattering of reduced ribonuclease A: effects of solution conditions and comparisons with a computational model of unfolded proteins. Journal of Molecular Biology, 377(5), 1576-1592.
  • Jeffries, C., Whitten, A., Harris, S., Trewhella, J. (2008). Small-angle X-ray scattering reveals the N-terminal domain organization of cardiac myosin binding protein C. Journal of Molecular Biology, 377(4), 1186-1199.
  • Zhan, H., Taraban, M., Trewhella, J., Swint-Kruse, L. (2008). Subdividing Repressor Function: DNA Binding Affinity, Selectivity, and Allostery Can Be Altered by Amino Acid Substitution of Nonconserved Residues in a LacI/GalR Homologue. Biochemistry, 47, 8058-8069.
  • Trewhella, J. (2008). The different views from small angles. Proceedings of the National Academy of Sciences (PNAS), 105(13), 4967-4968.
  • Chan, J., Whitten, A., Jeffries, C., Bosanac, I., Mal, T., Ito, J., Porumb, H., Michikawa, T., Mikoshiba, K., Trewhella, J., et al (2007). Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. Journal of Molecular Biology, 373(5), 1269-1280.
  • Thuet, K., Trewhella, J., Fenton, A. (2007). Non-allosteric effector analogs, unique tools for identifying allosteric specific structural changes in pyruvate kinase. Biophysical Journal, , 386-386.
  • Howarth, J., Meller, J., Solaro, R., Trewhella, J., Rosevear, P. (2007). Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin. Journal of Molecular Biology, 373(3), 706-722.
  • Taraban, M., Zhan, H., Matthews, K., Swint-Kruse, L., Trewhella, J. (2007). Small angle scattering studies of LacI repressor. Biophysical Journal, 2007 Online Supplement(2007 Abstracts Issue), 52A (Poster)-52A.
  • Comoletti, D., Grishaev, A., Whitten, A., Tsigelny, I., Taylor, P., Trewhella, J. (2007). Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering. Structure, 15(6), 693-705.
  • Comoletti, D., Grishaev, A., Whitten, A., Tsigelny, I., Taylor, P., Trewhella, J. (2007). Synaptic Arrangement of the Neuroligin/β-Neurexin Complex Revealed by X-Ray and Neutron Scattering. Structure.
  • Whitten, A., Jacques, D., Hammouda, B., Hanley, T., King, G., Guss, J., Trewhella, J., Langley, D. (2007). The Structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. Journal of Molecular Biology, 368(2), 407-420.
  • Ramachandran, S., Trewhella, J., Tseng, Y., Yu, Y. (2006). Coassembling Peptide-Based Biomaterials: Effects of Pairing Equal and Unequal Chain Length Oligopeptides. Chemistry of Materials, 18(26), 6157-6162.
  • Trewhella, J. (2006). Neutrons reveal how nature uses structural themes and variation in biological regulation. Physica B: Condensed Matter, 385-386(2), 825-830.
  • Trewhella, J. (2006). Protein kinase A targeting and activation as seen by small-angle solution scattering. European Journal of Cell Biology, 85(7), 655-662.
  • Vigil, D., Blumenthal, D., Taylor, S., Trewhella, J. (2006). Solution scattering reveals large differences in the global structures of type II protein kinase a isoforms. Journal of Molecular Biology, 357(3), 880-889.
  • Trewhella, J. (2006). Structural themes and variations in protein kinase A as seen by small-angle scattering and neutron contrast variation. European Biophysics Journal, 35(7), 585-589.
  • Priddy, T., MacDonald, B., Heller, W., Nadeau, O., Trewhella, J., Carlson, G. (2005). Ca2+-induced structural changes in phosphorylase kinase detected by small-angle X-ray scattering. Protein Science, 14(4), 1039-1048.
  • Grishaev, A., Wu, J., Trewhella, J., Bax, A. (2005). Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data. Journal of the American Chemical Society, 127(47), 16621-16628.
  • Vigil, D., Blumenthal, D., Taylor, S., Trewhella, J. (2005). The Conformationally Dynamic C Helix of the RIα Subunit of Protein Kinase A Mediates Isoform-specific Domain Reorganization upon C Subunit Binding. Journal of Biological Chemistry, 280(42), 35521-35527.
  • Heller, W., Vigil, D., Brown, S., Blumenthal, D., Taylor, S., Trewhella, J. (2004). C Subunits Binding to the Protein Kinase A RIα Dimer Induce a Large Conformational Change. Journal of Biological Chemistry, 279(18), 19084-19090.
  • Vigil, D., Blumenthal, D., Heller, W., Brown, S., Canaves, J., Taylor, S., Trewhella, J. (2004). Conformational differences among solution structures of the type Iα , IIα and IIβ protein kinase A regulatory subunit homodimers: role of the linker regions. Journal of Molecular Biology, 337(5), 1183-1194.
  • Vigil, D., Blumenthal, D., Brown, S., Taylor, S., Trewhella, J. (2004). Differential effects of substrate on type I and type II PKA holoenzyme dissociation. Biochemistry, 43(19), 5629-5636.
  • Heller, W., Krueger, J., Trewhella, J. (2003). Further insights into calmodulin-myosin light chain kinase interaction from solution scattering and shape restoration. Biochemistry, 42(36), 10579-10588.
  • Wall, M., Francis, S., Corbin, J., Grimes, K., Richie-Jannetta, R., Kotera, J., MacDonald, B., Gibson, R., Trewhella, J. (2003). Mechanisms associated with cGMP binding and activation of cGMP-dependent protein kinase. Proceedings of the National Academy of Sciences (PNAS), 100(5), 2380-2385.
  • Heller, W., Finley, N., Dong, W., Timmins, P., Cheung, H., Rosevear, P., Trewhella, J. (2003). Small-angle neutron scattering with contrast variation reveals spatial relationships between the three subunits in the ternary cardiac troponin complex and the effects of troponin I phosphorylation. Biochemistry, 42(25), 7790-7800.
  • Harris, S., Heller, W., Greaser, M., Moss, R., Trewhella, J. (2003). Solution Structure of Heavy Meromyosin by Small-angle Scattering. Journal of Biological Chemistry, 278(8), 6034-6040.
  • Tung, C., Walsh, D., Trewhella, J. (2002). A structural model of the catalytic subunit regulatory subunit dimeric complex of the cAMP-dependent protein kinase. Journal of Biological Chemistry, 277(14), 12423-12431.
  • Heller, W., Abusamhadneh, E., Finley, N., Rosevear, P., Trewhella, J. (2002). The solution structure of a cardiac troponin C-troponin I-troponin T complex shows a somewhat compact troponin C interacting with an extended troponin I-troponin T component. Biochemistry, 41(52), 15654-15663.
  • Krueger, J., Gallagher, S., Zhi, G., Geguchadze, R., Persechini, A., Stull, J., Trewhella, J. (2001). Activation of myosin light chain kinase requires translocation of bound calmodulin. Journal of Biological Chemistry.
  • Vigil, D., Gallagher, S., Trewhella, J., Garcia, A. (2001). Functional Dynamics of the Hydrophobic Cleft in the N-Domain of Calmodulin. Biophysical Journal, 80(5), 2082-2092.
  • Gallagher, S., Gao, Z., Li, S., Dyer, B., Trewhella, J., Lee, K. (2001). There is communication between all four Ca(2+)-bindings sites of calcineurin B. Biochemistry, 40(40), 12094-12102.

2013

  • Mokbel, N., Ilkovski, B., Kreissl, M., Memo, M., Jeffries, C., Marttila, M., Lehtokari, V., Lemola, E., Gronholm, M., Menard, D., Trewhella, J., North, K., Clarke, N., et al (2013). K7del is a common TPM2 gene mutation associated with nemaline myopathy and raised myo�?bre calcium sensitivity. Brain: a journal of neurology, 136(2), 494-507.

2012

  • Jacques, D., Guss, J., Trewhella, J. (2012). Antikinases: Their Structures and Roles in Two-component Signalling. In Roy Gross, Dagmar Beier (Eds.), Two-component Systems in Bacteria, (pp. 163-180). Norfolk, United Kingdom: Caister Academic Press.
  • Taylor, J., Chow, J., Jeffries, C., Kwan, A., Duff, A., Hamilton, W., Trewhella, J. (2012). Calmodulin Binds a Highly Extended HIV-1 MA Protein That Refolds Upon Its Release. Biophysical Journal, 103(3), 541-549.
  • Taraban, M., Weerasekare, M., Trewhella, J., Shi, X., Jeong, E., Yu, Y. (2012). Effects of Gadolinium Chelate on the Evolution of the Nanoscale Structure in Peptide Hydrogels. Peptide Science, 98(1), 50-58.
  • Jacques, D., Guss, J., Svergun, D., Trewhella, J. (2012). Publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution. Acta Crystallographica. Section D: Biological Crystallography, D68(6), 620-626.
  • Jacques, D., Guss, J., Trewhella, J. (2012). Reliable structural interpretation of small-angle scattering data from bio-molecules in solution - the importance of quality control and a standard reporting framework. B M C Structural Biology, 12, 1-3.
  • Jeffries, C., Trewhella, J. (2012). Small-Angle Scattering. In Michael E. Wall (Eds.), Quantitative Biology: From Molecular to Cellular Systems, (pp. 113-151). Boca Raton, United States of America: CRC Press.
  • Bhati, M., Lee, C., Gadd, M., Jeffries, C., Kwan, A., Whitten, A., Trewhella, J., Mackay, J., Matthews, J. (2012). Solution Structure of the LIM-Homeodomain Transcription Factor Complex Lhx3/Ldb1 and the Effects of a Pituitary Mutation on Key Lhx3 Interactions. PLoS One, 7(7), 1-9.
  • Hynson, R., Jeffries, C., Trewhella, J., Cocklin, S. (2012). Solution structure studies of monomeric human TIP47/perilipin-3 reveal a highly extended conformation. Proteins: Structure, Function, and Bioinformatics, 80(8), 2046-2055.
  • Lu, Y., Kwan, A., Jeffries, C., Guss, J., Trewhella, J. (2012). The Motif of Human Cardiac Myosin-binding Protein C Is Required for Its Ca2+ -dependent Interaction with Calmodulin. Journal of Biological Chemistry, 287(37), 31596-31607.
  • Gao, J., Lu, Y., Browne, G., Yap, B., Trewhella, J., Hunter, N., Nguyen, K. (2012). The role of heme-binding by DNA-protective protein from starved-cells (Dps) in the tolerance of Porphyromonas gingivalis to heme toxicity. Journal of Biological Chemistry, 287(50), 42243-42258.

2011

  • Jacques, D., Langley, D., Hynson, R., Whitten, A., Kwan, A., Guss, J., Trewhella, J. (2011). A Novel Structure of an Antikinase and Its Inhibitor. Journal of Molecular Biology, 405(1), 214-226.
  • Zhai, Q., Landesman, M., Chung, H., Dierkers, A., Jeffries, C., Trewhella, J., Hill, C., Sundquist, W. (2011). Activation of the Retroviral Budding Factor ALIX. Journal of Virology, 85(17), 9222-9226.
  • Taraban, M., Ramachandran, S., Gryczynski, I., Gryczynski, Z., Trewhella, J., Yu, Y. (2011). Effects of chain length on oligopeptide hydrogelation. Soft Matter, 7, 2624-2631.
  • Johansen, D., Jeffries, C., Hammouda, B., Trewhella, J., Goldenberg, D. (2011). Effects of Macromolecular Crowding on an Intrinsically Disordered Protein Characterized by Small-Angle Neutron Scattering with Contrast Matching. Biophysical Journal, 100(4), 1120-1128.
  • Johansen, D., Trewhella, J., Goldenberg, D. (2011). Fractal dimension of an intrinsically disordered protein: Small-angle X-ray scattering and computational study of the bacteriophage Lambda N protein. Protein Science, 20(12), 1955-1970.
  • Jeffries, C., Lu, Y., Hynson, R., Taylor, J., Ballesteros, M., Kwan, A., Trewhella, J. (2011). Human Cardiac Myosin Binding Protein C: Structural Flexibility within an Extended Modular Architecture. Journal of Molecular Biology, 414(5), 735-748.
  • Lu, Y., Jeffries, C., Trewhella, J. (2011). Invited review: Probing the structures of muscle regulatory proteins using small-angle solution scattering. Biopolymers: original research on biological molecules and assemblies, 95(8), 505-516.
  • Trewhella, J. (2011). Reflections of a Woman Scientist in the Year 2011. Australian Journal of Chemistry: an international journal for chemical science, 64(6), 666-668.
  • Weerasekare, M., Taraban, M., Shi, X., Jeong, E., Trewhella, J., Yu, Y. (2011). Sol and Gel States in Peptide Hydrogels Visualized by Gd(III)-enhanced Magnetic Resonance Imaging. Biopolymers: original research on biological molecules and assemblies, 96(6), 734-743.
  • Gadd, M., Bhati, M., Jeffries, C., Langley, D., Trewhella, J., Guss, J., Matthews, J. (2011). Structural Basis for Partial Redundancy in a Class of Transcription Factors, the LIM Homeodomain Proteins, in Neural Cell Type Specification. Journal of Biological Chemistry, 286(50), 42971-42980.
  • Lu, Y., Kwan, A., Trewhella, J., Jeffries, C. (2011). The C0C1 Fragment of Human Cardiac Myosin Binding Protein C Has Common Binding Determinants for Both Actin and Myosin. Journal of Molecular Biology, 413(5), 908-913.
  • Orlova, A., Galkin, V., Jeffries, C., Egelman, E., Trewhella, J. (2011). The N-Terminal Domains of Myosin Binding Protein C Can Bind Polymorphically to F-Actin. Journal of Molecular Biology, 412(3), 379-386.
  • Jacques, D., Langley, D., Kuramitsu, S., Yokoyama, S., Trewhella, J., Guss, J. (2011). The structure of TTHA0988 from Thermus thermophilus, a KipI-KipA homologue incorrectly annotated as an allophanate hydrolase. Acta Crystallographica. Section D: Biological Crystallography, 67(2), 105-111.

2010

  • Hynson, R., Kwan, A., Jacques, D., Mackay, J., Trewhella, J. (2010). (1)H, (13)C and (15)N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis. Biomolecular N M R Assignments, 4(2), 167-169.
  • Siddiqui, K., Poljak, A., De Francisci, D., Guerriero, G., Pilak, O., Burg, D., Raftery, M., Parkin, D., Trewhella, J., Cavicchioli, R. (2010). A chemically modified alpha-amylase with a molten-globule state has entropically driven enhanced thermal stability. Protein Engineering Design and Selection (Print), 23(10), 769-780.
  • Chow, J., Jeffries, C., Kwan, A., Guss, J., Trewhella, J. (2010). Calmodulin Disrupts the Structure of the HIV-1 MA Protein. Journal of Molecular Biology, 400(4), 702-714.
  • Fenton, A., Williams, R., Trewhella, J. (2010). Changes in Small-Angle X-ray Scattering Parameters Observed upon Binding of Ligand to Rabbit Muscle Pyruvate Kinase are not Correlated with Allosteric Transitions. Biochemistry, 49(33), 7202-7209.
  • Ramachandran, S., Taraban, M., Trewhella, J., Gryczynski, I., Gryczynski, Z., Yu, Y. (2010). Effect of Temperature During Assembly on the Structure and Mechanical Properties of Peptide-Based Materials. Biomacromolecules, 11(6), 1502-1506.
  • Cross, A., Jeffries, C., Trewhella, J., Matthews, J. (2010). LIM Domain Binding Proteins 1 and 2 Have Different Oligomeric States. Journal of Molecular Biology, 399(1), 133-144.
  • Jacques, D., Trewhella, J. (2010). Small-angle scattering for structural biology - Expanding the frontier while avoiding the pitfalls. Protein Science, 19(4), 642-657.
  • Comoletti, D., Miller, M., Jeffries, C., Wilson, J., Demeler, B., Taylor, P., Trewhella, J., Nakagawa, T. (2010). The Macromolecular Architecture of Extracellular Domain of alphaNRXN1: Domain Organization, Flexibility, and Insights into Trans-Synaptic Disposition. Structure, 18(8), 1044-1053.

2009

  • Siddiqui, K., Parkin, D., Curmi, P., De Francisci, D., Poljak, A., Barrow, K., Noble, M., Trewhella, J., Cavicchioli, R. (2009). A Novel Approach for Enhancing the Catalytic Efficiency of a Protease at Low Temperature: Reduction in Substrate Inhibition by Chemical Modification. Biotechnology and Bioengineering, 103(4), 676-686.
  • Claridge, J., Headey, S., Chow, J., Schwalbe, M., Edwards, P., Jeffries, C., Venugopal, H., Trewhella, J., Pascal, S. (2009). A picornaviral loop-to-loop replication complex. Journal of Structural Biology, 166(3), 251-262.
  • Mills, R., Trewhella, J., Qiu, T., Welte, T., Ryan, T., Hanley, T., Knott,, R., Lithgow, T., Mulhern, T. (2009). Domain organization of the monomeric form of the Tom70 mitochondrial import receptor. Journal of Molecular Biology, 388(5), 1043-1058.
  • Whitten, A., Trewhella, J. (2009). Small-Angle Scattering and Neutron Contrast Variation for Studying Bio-molecular Complexes. In James W. Lee, Robert S. Foote (Eds.), Micro and Nano Technologies in Bioanalysis: Methods and Protocols, (pp. 307-324). New York, USA: Humana Press.
  • Whitten, A., Smith, B., Menting, J., Margetts, M., McKern, N., Lovrecz, G., Adams, T., Richards, K., Bentley, J., Trewhella, J., et al (2009). Solution Structure of Ectodomains of the Insulin Receptor Family: The Ectodomain of the Type 1 Insulin-Like Growth Factor Receptor Displays Asymmetry of Ligand Binding Accompanied by Limited Conformational Change. Journal of Molecular Biology, 394(5), 878-892.
  • Jacques, D., Streamer, M., Rowland, S., King, G., Guss, J., Trewhella, J., Langley, D. (2009). Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state. Acta Crystallographica. Section D: Biological Crystallography, 65(6), 574-581.

2008

  • Whitten, A., Jeffries, C., Harris, S., Trewhella, J. (2008). Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function. Proceedings of the National Academy of Sciences (PNAS), 105(47), 18360-18365.
  • Comoletti, D., Grishaev, A., Whitten, A., Taylor, P., Trewhella, J. (2008). Characterization of the solution structure of a neuroligin/β-neurexin complex. Chemico-Biological Interactions, 175, 150-155.
  • Griffin, M., Dobson, R., Pearce, F., Antonio, L., Whitten, A., Liew, C., Mackay, J., Trewhella, J., Jameson, G., Perugini, M., et al (2008). Evolution of quaternary structure in a homotetrameric enzyme. Journal of Molecular Biology, 380(4), 691-703.
  • Jacques, D., Langley, D., Jeffries, C., Cunningham, K., Burkholder, W., Guss, J., Trewhella, J. (2008). Histidine Kinase Regulation by a Cyclophilin-like Inhibitor. Journal of Molecular Biology, 384(2), 422-435.
  • Taraban, M., Zhan, H., Whitten, A., Langley, D., Matthews, K., Swint-Kruse, L., Trewhella, J. (2008). Ligand-induced conformational changes and conformational dynamics in the solution structure of the lactose repressor protein. Journal of Molecular Biology, 376(2), 466-481.
  • Whitten, A., Cai, S., Trewhella, J. (2008). MULCh: ModULes for the Analysis of Small-angle Neutron Contrast Variation Data from Biomolecular Assemblies. Journal of Applied Crystallography, 41(1), 222-226.
  • Grishaev, A., Tugarinov, V., Kay, L., Trewhella, J., Bax, A. (2008). Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints. Journal of Biomolecular NMR, 40(2), 95-106.
  • Wang, Y., Trewhella, J., Goldenberg, D. (2008). Small-angle X-ray scattering of reduced ribonuclease A: effects of solution conditions and comparisons with a computational model of unfolded proteins. Journal of Molecular Biology, 377(5), 1576-1592.
  • Jeffries, C., Whitten, A., Harris, S., Trewhella, J. (2008). Small-angle X-ray scattering reveals the N-terminal domain organization of cardiac myosin binding protein C. Journal of Molecular Biology, 377(4), 1186-1199.
  • Zhan, H., Taraban, M., Trewhella, J., Swint-Kruse, L. (2008). Subdividing Repressor Function: DNA Binding Affinity, Selectivity, and Allostery Can Be Altered by Amino Acid Substitution of Nonconserved Residues in a LacI/GalR Homologue. Biochemistry, 47, 8058-8069.
  • Trewhella, J. (2008). The different views from small angles. Proceedings of the National Academy of Sciences (PNAS), 105(13), 4967-4968.

2007

  • Chan, J., Whitten, A., Jeffries, C., Bosanac, I., Mal, T., Ito, J., Porumb, H., Michikawa, T., Mikoshiba, K., Trewhella, J., et al (2007). Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. Journal of Molecular Biology, 373(5), 1269-1280.
  • Thuet, K., Trewhella, J., Fenton, A. (2007). Non-allosteric effector analogs, unique tools for identifying allosteric specific structural changes in pyruvate kinase. Biophysical Journal, , 386-386.
  • Howarth, J., Meller, J., Solaro, R., Trewhella, J., Rosevear, P. (2007). Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin. Journal of Molecular Biology, 373(3), 706-722.
  • Taraban, M., Zhan, H., Matthews, K., Swint-Kruse, L., Trewhella, J. (2007). Small angle scattering studies of LacI repressor. Biophysical Journal, 2007 Online Supplement(2007 Abstracts Issue), 52A (Poster)-52A.
  • Comoletti, D., Grishaev, A., Whitten, A., Tsigelny, I., Taylor, P., Trewhella, J. (2007). Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering. Structure, 15(6), 693-705.
  • Comoletti, D., Grishaev, A., Whitten, A., Tsigelny, I., Taylor, P., Trewhella, J. (2007). Synaptic Arrangement of the Neuroligin/β-Neurexin Complex Revealed by X-Ray and Neutron Scattering. Structure.
  • Whitten, A., Jacques, D., Hammouda, B., Hanley, T., King, G., Guss, J., Trewhella, J., Langley, D. (2007). The Structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. Journal of Molecular Biology, 368(2), 407-420.

2006

  • Ramachandran, S., Trewhella, J., Tseng, Y., Yu, Y. (2006). Coassembling Peptide-Based Biomaterials: Effects of Pairing Equal and Unequal Chain Length Oligopeptides. Chemistry of Materials, 18(26), 6157-6162.
  • Trewhella, J. (2006). Neutrons reveal how nature uses structural themes and variation in biological regulation. Physica B: Condensed Matter, 385-386(2), 825-830.
  • Trewhella, J. (2006). Protein kinase A targeting and activation as seen by small-angle solution scattering. European Journal of Cell Biology, 85(7), 655-662.
  • Vigil, D., Blumenthal, D., Taylor, S., Trewhella, J. (2006). Solution scattering reveals large differences in the global structures of type II protein kinase a isoforms. Journal of Molecular Biology, 357(3), 880-889.
  • Trewhella, J. (2006). Structural themes and variations in protein kinase A as seen by small-angle scattering and neutron contrast variation. European Biophysics Journal, 35(7), 585-589.

2005

  • Priddy, T., MacDonald, B., Heller, W., Nadeau, O., Trewhella, J., Carlson, G. (2005). Ca2+-induced structural changes in phosphorylase kinase detected by small-angle X-ray scattering. Protein Science, 14(4), 1039-1048.
  • Grishaev, A., Wu, J., Trewhella, J., Bax, A. (2005). Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data. Journal of the American Chemical Society, 127(47), 16621-16628.
  • Vigil, D., Blumenthal, D., Taylor, S., Trewhella, J. (2005). The Conformationally Dynamic C Helix of the RIα Subunit of Protein Kinase A Mediates Isoform-specific Domain Reorganization upon C Subunit Binding. Journal of Biological Chemistry, 280(42), 35521-35527.

2004

  • Heller, W., Vigil, D., Brown, S., Blumenthal, D., Taylor, S., Trewhella, J. (2004). C Subunits Binding to the Protein Kinase A RIα Dimer Induce a Large Conformational Change. Journal of Biological Chemistry, 279(18), 19084-19090.
  • Vigil, D., Blumenthal, D., Heller, W., Brown, S., Canaves, J., Taylor, S., Trewhella, J. (2004). Conformational differences among solution structures of the type Iα , IIα and IIβ protein kinase A regulatory subunit homodimers: role of the linker regions. Journal of Molecular Biology, 337(5), 1183-1194.
  • Vigil, D., Blumenthal, D., Brown, S., Taylor, S., Trewhella, J. (2004). Differential effects of substrate on type I and type II PKA holoenzyme dissociation. Biochemistry, 43(19), 5629-5636.

2003

  • Heller, W., Krueger, J., Trewhella, J. (2003). Further insights into calmodulin-myosin light chain kinase interaction from solution scattering and shape restoration. Biochemistry, 42(36), 10579-10588.
  • Wall, M., Francis, S., Corbin, J., Grimes, K., Richie-Jannetta, R., Kotera, J., MacDonald, B., Gibson, R., Trewhella, J. (2003). Mechanisms associated with cGMP binding and activation of cGMP-dependent protein kinase. Proceedings of the National Academy of Sciences (PNAS), 100(5), 2380-2385.
  • Heller, W., Finley, N., Dong, W., Timmins, P., Cheung, H., Rosevear, P., Trewhella, J. (2003). Small-angle neutron scattering with contrast variation reveals spatial relationships between the three subunits in the ternary cardiac troponin complex and the effects of troponin I phosphorylation. Biochemistry, 42(25), 7790-7800.
  • Harris, S., Heller, W., Greaser, M., Moss, R., Trewhella, J. (2003). Solution Structure of Heavy Meromyosin by Small-angle Scattering. Journal of Biological Chemistry, 278(8), 6034-6040.

2002

  • Tung, C., Walsh, D., Trewhella, J. (2002). A structural model of the catalytic subunit regulatory subunit dimeric complex of the cAMP-dependent protein kinase. Journal of Biological Chemistry, 277(14), 12423-12431.
  • Trewhella, J., Krueger, J. (2002). Small-angle solution scattering reveals information on conformational dynamics in calcium-binding proteins and in their interactions with regulatory targets. In Hans J. Vogel (Eds.), Calcium-Binding Protein Protocols, (pp. 137-159). canada: Humana Press.
  • Heller, W., Abusamhadneh, E., Finley, N., Rosevear, P., Trewhella, J. (2002). The solution structure of a cardiac troponin C-troponin I-troponin T complex shows a somewhat compact troponin C interacting with an extended troponin I-troponin T component. Biochemistry, 41(52), 15654-15663.

2001

  • Krueger, J., Gallagher, S., Zhi, G., Geguchadze, R., Persechini, A., Stull, J., Trewhella, J. (2001). Activation of myosin light chain kinase requires translocation of bound calmodulin. Journal of Biological Chemistry.
  • Vigil, D., Gallagher, S., Trewhella, J., Garcia, A. (2001). Functional Dynamics of the Hydrophobic Cleft in the N-Domain of Calmodulin. Biophysical Journal, 80(5), 2082-2092.
  • Gallagher, S., Gao, Z., Li, S., Dyer, B., Trewhella, J., Lee, K. (2001). There is communication between all four Ca(2+)-bindings sites of calcineurin B. Biochemistry, 40(40), 12094-12102.
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