| human | Q5 |
| P496 | ORCID iD | 0000-0002-6426-4510 |
| P1153 | Scopus author ID | 7006056499 |
| P69 | educated at | University of Sydney | Q487556 |
| P108 | employer | Laboratory of Molecular Biology | Q185800 |
| University of Sydney | Q487556 | ||
| University of New South Wales | Q734764 | ||
| University of Technology Sydney | Q1145731 | ||
| P735 | given name | David | Q18057751 |
| David | Q18057751 | ||
| P106 | occupation | researcher | Q1650915 |
| P21 | sex or gender | male | Q6581097 |
| Q43044563 | 1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis |
| Q41626997 | 2017 publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution: an update |
| Q112591891 | A lysine ring in HIV capsid pores coordinates IP6 to drive mature capsid assembly |
| Q27665603 | A novel structure of an antikinase and its inhibitor |
| Q93098080 | Fluorescence Biosensor for Real-Time Interaction Dynamics of Host Proteins with HIV-1 Capsid Tubes |
| Q41269115 | GATA1 directly mediates interactions with closely spaced pseudopalindromic but not distantly spaced double GATA sites on DNA. |
| Q27680544 | HIV-1 evades innate immune recognition through specific cofactor recruitment |
| Q30804067 | HIV-1 uses dynamic capsid pores to import nucleotides and fuel encapsidated DNA synthesis |
| Q27652319 | Histidine kinase regulation by a cyclophilin-like inhibitor |
| Q35377316 | Host cofactors and pharmacologic ligands share an essential interface in HIV-1 capsid that is lost upon disassembly. |
| Q56890367 | IP6 is an HIV pocket factor that prevents capsid collapse and promotes DNA synthesis |
| Q33870828 | Interactions between LHX3- and ISL1-family LIM-homeodomain transcription factors are conserved in Caenorhabditis elegans |
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| Q27676618 | New Insights into DNA Recognition by Zinc Fingers Revealed by Structural Analysis of the Oncoprotein ZNF217 |
| Q34298629 | Publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution. |
| Q34272674 | Reliable structural interpretation of small-angle scattering data from bio-molecules in solution--the importance of quality control and a standard reporting framework |
| Q30385150 | Small-angle scattering for structural biology--expanding the frontier while avoiding the pitfalls. |
| Q27673904 | Structural Basis for Hemoglobin Capture by Staphylococcus aureus Cell-surface Protein, IsdH |
| Q27681340 | Structure of the Hemoglobin-IsdH Complex Reveals the Molecular Basis of Iron Capture byStaphylococcus aureus |
| Q24652923 | Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state |
| Q112730151 | Target-induced clustering activates Trim-Away of pathogens and proteins |
| Q57093534 | The Human Immunodeficiency Virus Capsid Is More Than Just a Genome Package |
| Q57979820 | The Structure of the KinA-Sda Complex Suggests an Allosteric Mechanism of Histidine Kinase Inhibition |
| Q27666535 | The structure of TTHA0988 from Thermus thermophilus, a KipI-KipA homologue incorrectly annotated as an allophanate hydrolase |
| Q27700983 | The structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native α-globin haem pocket |
| Q27684913 | The structure of α-haemoglobin in complex with a haemoglobin-binding domain fromStaphylococcus aureusreveals the elusive α-haemoglobin dimerization interface |
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