{"id":231,"date":"2019-06-27T16:22:24","date_gmt":"2019-06-27T06:22:24","guid":{"rendered":"https:\/\/www.protein.physics.unsw.edu.au\/?page_id=231"},"modified":"2019-07-04T15:06:40","modified_gmt":"2019-07-04T05:06:40","slug":"references","status":"publish","type":"page","link":"https:\/\/www.protein.physics.unsw.edu.au\/?page_id=231","title":{"rendered":"Publications"},"content":{"rendered":"\n<h1 class=\"wp-block-heading\"> Membrane Remodelling &amp; Metamorphic Proteins<\/h1>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<ol class=\"wp-block-list\"><li>Structural characterization suggests models for monomeric and dimeric forms of full-length ezrin&nbsp;<em>JM Phang, et al,&nbsp;<\/em><em>Biochemical Journal 473 (18), 2763-2782<\/em><\/li><li>Interaction of human Chloride Intracellular Channel Protein 1 (CLIC1) with lipid bilayers: a fluorescence study&nbsp;<em>JE Hare, et al,&nbsp;<\/em><em>Biochemistry 55 (27), 3825-3833<\/em><\/li><li>CLIC1 regulates dendritic cell antigen processing and presentation by modulating phagosome acidification and proteolysis&nbsp;<em>K Salao, et al,&nbsp;<\/em><em>Biology open, bio. 018119<\/em><\/li><li>Members of the chloride intracellular ion channel protein family demonstrate glutaredoxin-like enzymatic activity&nbsp;<em>H Al Khamici et al,<\/em>&nbsp;<em>PloS one 10 (1), e115699<\/em><\/li><li>Metformin repositioning as antitumoral agent: selective antiproliferative effects in human glioblastoma stem cells, via inhibition of CLIC1-mediated ion current&nbsp;<em>M Gritti, et al,<\/em>&nbsp;<em>Oncotarget 5 (22), 11252<\/em><\/li><li>CLIC proteins, ezrin, radixin, moesin and the coupling of membranes to the actin cytoskeleton: a smoking gun?&nbsp;<em>L Jiang,et al,<\/em>&nbsp;<em>Biochimica et Biophysica Acta (BBA)-Biomembranes 1838 (2), 643-657<\/em><\/li><li>Point mutations in the transmembrane region of the clic1 ion channel selectively modify its biophysical properties&nbsp;<em>S Averaimo, et al,<\/em>&nbsp;<em>PloS one 8 (9), e74523<\/em><\/li><li>Regulation of the membrane insertion and conductance activity of the metamorphic chloride intracellular channel protein CLIC1 by cholesterol&nbsp;<em>SM Valenzuela,et al,<\/em>&nbsp;<em>PLoS One 8 (2), e56948<\/em><\/li><li>Intracellular chloride channel protein CLIC1 regulates macrophage function through modulation of phagosomal acidification&nbsp;<em>L Jiang,et al.,<\/em>&nbsp;<em>J Cell Sci 125 (22), 5479-5488<\/em><\/li><li>Transmembrane extension and oligomerization of the CLIC1 chloride intracellular channel protein upon membrane interaction&nbsp;<em>SC Goodchild,et al<\/em>&nbsp;<em>Biochemistry 50 (50), 10887-10897<\/em><\/li><li>Structural gymnastics of multifunctional metamorphic proteins&nbsp;<em>SC Goodchild, et al,<\/em>&nbsp;<em>Biophysical reviews 3 (3), 143<\/em><\/li><li>Crystal structure of importin\u2010\u03b1 bound to a peptide bearing the nuclear localisation signal from chloride intracellular channel protein 4&nbsp;<em>AV Mynott, et al,<\/em>&nbsp;<em>The FEBS journal 278 (10), 1662-1675<\/em><\/li><li>S-nitrosylation regulates nuclear translocation of chloride intracellular channel protein CLIC4&nbsp;<em>M Malik, et al,<\/em>&nbsp;<em>Journal of Biological Chemistry 285 (31), 23818-23828<\/em><\/li><li>Metamorphic response of the CLIC1 chloride intracellular ion channel protein upon membrane interaction&nbsp;<em>SC Goodchild, et al,<\/em>&nbsp;<em>Biochemistry 49 (25), 5278-5289<\/em><\/li><li>The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins?&nbsp;<em>DR Littler, et al,<\/em>&nbsp;<em>FEBS letters 584 (10), 2093-2101<\/em><\/li><li>Structure of human CLIC3 at 2 \u00c5 resolution&nbsp;<em>DR Littler, et al,<\/em>&nbsp;<em>Proteins: Structure, Function, and Bioinformatics 78 (6), 1594-1600<\/em><\/li><li>Generation and characterization of mice with null mutation of the chloride intracellular channel 1 gene&nbsp;<em>MR Qiu,et al,<\/em>&nbsp;<em>genesis 48 (2), 127-136<\/em><\/li><li>Oxidation promotes insertion of the CLIC1 chloride intracellular channel into the membrane&nbsp;<em>SC Goodchild, et al,<\/em>&nbsp;<em>European biophysics journal 39 (1), 129<\/em><\/li><li>CLIC1 function is required for \u03b2-amyloid-induced generation of reactive oxygen species by microglia&nbsp;<em>RH Milton, et al,<\/em>&nbsp;<em>Journal of Neuroscience 28 (45), 11488-11499<\/em><\/li><li>Comparison of vertebrate and invertebrate CLIC proteins: The crystal structures of Caenorhabditis elegans EXC\u20104 and Drosophila melanogaster DmCLIC&nbsp;<em>DR Littler, et al,<\/em>&nbsp;<em>Proteins: Structure, Function, and Bioinformatics 71 (1), 364-378<\/em><\/li><li>Structure of the Janus protein human CLIC2&nbsp;<em>BA Cromer, et al,<\/em>&nbsp;<em>Journal of molecular biology 374 (3), 719-731<\/em><\/li><li>Crystal structure of the soluble form of the redox\u2010regulated chloride ion channel protein CLIC4&nbsp;<em>DR Littler,et al,<\/em>&nbsp;<em>The FEBS journal 272 (19), 4996-5007<\/em><\/li><li>Involvement of the intracellular ion channel CLIC1 in microglia-mediated \u03b2-amyloid-induced neurotoxicity&nbsp;<em>G Novarino, et al,<\/em>&nbsp;<em>Journal of Neuroscience 24 (23), 5322-5330<\/em><\/li><li>The intracellular chloride ion channel protein CLIC1 undergoes a redox-controlled structural transition&nbsp;<em>DR Littler, et al,<\/em>&nbsp;<em>Journal of Biological Chemistry 279 (10), 9298-9305<\/em><\/li><li>Recombinant CLIC1 (NCC27) assembles in lipid bilayers via a pH-dependent two-state process to form chloride ion channels with identical characteristics to those observed in Chinese hamster ovary cells expressing CLIC1&nbsp;<em>K Warton, et al, Journal of Biological Chemistry<\/em><\/li><li>NCC27 (CLIC1) interacts with artifical bylayer in a pH dependent manner to form chloride ion channels&nbsp;<em>M Mazzanti, et al,<\/em>&nbsp;<em>Biophysical Journal 82 (1), 244A-244A<\/em><\/li><li>Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-\u00c5 resolution&nbsp;<em>SJ Harrop, et al,<\/em>&nbsp;<em>Journal of Biological Chemistry 276 (48), 44993-45000<\/em><\/li><\/ol>\n\n\n\n<hr class=\"wp-block-separator is-style-wide\"\/>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<h1 class=\"wp-block-heading\">Nanomachines &amp; Molecular Motors  <\/h1>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<ol class=\"wp-block-list\"><li>Construction of a chassis for a tripartite protein-based molecular motor&nbsp;<em>LSR Small,et al.,&nbsp;ACS synthetic biology 6 (6), 1096-1102<\/em><\/li><li>Motor properties from persistence: a linear molecular walker lacking spatial and temporal asymmetry&nbsp;<em>MJ Zuckermann et al,<\/em>&nbsp;<em>New Journal of Physics 17 (5), 055017<\/em><\/li><li>Design and construction of the lawnmower, an artificial burnt-bridges motor&nbsp;<em>S Kovacic et al,<\/em>&nbsp;<em>IEEE transactions on nanobioscience 14 (3), 305-312<\/em><\/li><li>Construction and characterization of kilobasepair densely labeled peptide-DNA&nbsp;<em>S Kovacic et al,<\/em>&nbsp;<em>Biomacromolecules 15 (11), 4065-4072<\/em><\/li><li>Introducing a Kinesin-Inspired Nanomotor Concept&nbsp;<em>MJ Zuckermann, et al,<\/em>&nbsp;<em>Biophysical Journal 106 (2), 782a<\/em><\/li><li>Light Driven Conformational Switching: An Approach to Creating Designed Protein Motion&nbsp;<em>E Bromley,et al,<\/em>&nbsp;<em>Biophysical Journal 106 (2), 244a-245a<\/em><\/li><li>Fluidic switching in nanochannels for the control of Inchworm: a synthetic biomolecular motor with a power stroke&nbsp;<em>CS Niman,et al,<\/em>&nbsp;<em>Nanoscale 6 (24), 15008-15019<\/em><\/li><li>The Lawnmower: An Autonomous Synthetic Protein Motor&nbsp;<em>L Samii, et al,<\/em>&nbsp;<em>Biophysical Journal 104 (2), 545a<\/em><\/li><li>Controlled microfluidic switching in arbitrary time-sequences with low drag&nbsp;<em>CS Niman, et al,<\/em>&nbsp;<em>Lab on a Chip 13 (12), 2389-2396<\/em><\/li><li>Squaring the circle in peptide assembly: from fibers to discrete nanostructures by de novo design&nbsp;<em>AL Boyle, et al,<\/em>&nbsp;<em>Journal of the American Chemical Society 134 (37), 15457-15467<\/em><\/li><li>The Inchworm: Construction of a Biomolecular Motor with a Power Stroke&nbsp;<em>M Balaz, et al,<\/em>&nbsp;<em>Biophysical Journal 102 (3), 206a<\/em><\/li><li>Microfluidic Device for Controlled Fluid Switching to be used with Chemically Powered Molecular Motors on Surface Bound Tracks&nbsp;<em>C Niman,et al,<\/em>&nbsp;<em>Biophysical Journal 102 (3), 717a<\/em><\/li><li>Design and construction of a one-dimensional DNA track for an artificial molecular motor&nbsp;S Kovacic, et al,&nbsp;Journal of Nanomaterials 2012, 6<\/li><li>Tuning the performance of an artificial protein motor&nbsp;<em>NJ Kuwada, et al,<\/em>Physical Review E 84 (3), 031922<\/li><li>Time-dependent motor properties of multipedal molecular spiders&nbsp;<em>L Samii,et al,<\/em>&nbsp;<em>Physical Review E 84 (3), 031111<\/em><\/li><li>Simulation Studies of a TRI-PEDAL, Protein-Based Artificial Molecular Motor&nbsp;<em>NJ Kuwada, et al,<\/em>&nbsp;<em>Biophysical Journal 98 (3), 388a<\/em><\/li><li>The tumbleweed: towards a synthetic protein motor&nbsp;<em>EHC Bromley,et al,<\/em>&nbsp;<em>HFSP journal 3 (3), 204-212<\/em><\/li><li>Synthetic, Protein-Based Molecular Motors&nbsp;<em>NJ Kuwada, et al,<\/em>&nbsp;<em>Biophysical Journal 96 (3), 300a<\/em><\/li><\/ol>\n\n\n\n<hr class=\"wp-block-separator is-style-wide\"\/>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<h1 class=\"wp-block-heading\">Non-Trivial Quantum Effects in Biology   <\/h1>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<ol class=\"wp-block-list\"><li>Cooperative Subunit Refolding of a Light\u2010Harvesting Protein through a Self\u2010Chaperone Mechanism&nbsp;<em>AJ Laos et al.,&nbsp;<\/em><em>Angewandte Chemie 129 (29), 8504-8508<\/em><\/li><li>Vibronic resonances facilitate excited-state coherence in light-harvesting proteins at room temperature&nbsp;<em>F Novelli et al,<\/em>&nbsp;<em>The journal of physical chemistry letters 6 (22), 4573-4580<\/em><\/li><li>Spectroscopic studies of cryptophyte light harvesting proteins: vibrations and coherent oscillations&nbsp;<em>PC Arpin et al,<\/em>&nbsp;<em>The Journal of Physical Chemistry B 119 (31), 10025-10034<\/em><\/li><li>Polymersomes prepared from thermoresponsive fluorescent protein\u2013polymer bioconjugates: capture of and report on drug and protein payloads&nbsp;<em>CK Wong et al<\/em>&nbsp;<em>Angewandte Chemie International Edition 54 (18), 5317-5322<\/em><\/li><li>Disentangling Electronic and Vibrational Coherence in the Phycocyanin-645 Light-Harvesting Complex&nbsp;<em>JA Davis, et al,<\/em>&nbsp;<em>Ultrafast Phenomena XIX, 591-594<\/em><\/li><li>Single-residue insertion switches the quaternary structure and exciton states of cryptophyte light-harvesting proteins&nbsp;<em>SJ Harrop, et al,<\/em>&nbsp;<em>Proceedings of the National Academy of Sciences 111 (26), E2666-E2675<\/em><\/li><li>Quantum Coherence and its Impact on Biomimetic Light-Harvesting&nbsp;<em>AJ Laos, et al,&nbsp;Australian Journal of Chemistry 67 (5), 729-739<\/em><\/li><li>Coherence dynamics in light-harvesting complexes with two-colour spectroscopy&nbsp;<em>GH Richards, et al,<\/em>&nbsp;<em>EPJ Web of Conferences 41, 08009<\/em><\/li><li>Excited state coherent dynamics in light-harvesting complexes from photosynthetic marine algae&nbsp;<em>GH Richards, et al,<\/em>&nbsp;<em>Journal of Physics B: Atomic, Molecular and Optical Physics 45 (15), 154015<\/em><\/li><li>Electronic coherence lineshapes reveal hidden excitonic correlations in photosynthetic light harvesting&nbsp;<em>CY Wong, et al,<\/em>&nbsp;<em>Nature chemistry 4 (5), 396<\/em><\/li><li>Coherent vibronic coupling in light-harvesting complexes from photosynthetic marine algae&nbsp;<em>GH Richards, et al,<\/em>&nbsp;<em>The journal of physical chemistry letters 3 (2), 272-277<\/em><\/li><li>Quantitative investigations of quantum coherence for a light-harvesting protein at conditions simulating photosynthesis&nbsp;<em>DB Turner, et al,<\/em>&nbsp;<em>Physical Chemistry Chemical Physics 14 (14), 4857-4874<\/em><\/li><li>Flow of excitation energy in the cryptophyte light-harvesting antenna phycocyanin 645&nbsp;<em>A Marin, et al,<\/em>&nbsp;<em>Biophysical journal 101 (4), 1004-1013<\/em><\/li><li>Comparison of electronic and vibrational coherence measured by two-dimensional electronic spectroscopy&nbsp;<em>DB Turner, et al,<\/em>&nbsp;<em>The Journal of Physical Chemistry Letters 2 (15), 1904-1911<\/em><\/li><li>Coherently wired light-harvesting in photosynthetic marine algae at ambient temperature&nbsp;<em>E Collini,et al,<\/em>&nbsp;<em>Nature 463 (7281), 644<\/em><\/li><li>Phycobiliprotein diffusion in chloroplasts of cryptophyte Rhodomonas CS24&nbsp;<em>T Mirkovic, et al,<\/em>&nbsp;<em>Photosynthesis research 100 (1), 7-17<\/em><\/li><li>Phycocyanin sensitizes both photosystem I and photosystem II in cryptophyte Chroomonas CCMP270 cells&nbsp;<em>CD van der Weij-De, et al,<\/em>&nbsp;<em>Biophysical journal 94 (6), 2423-2433<\/em><\/li><li>Ultrafast light harvesting dynamics in the cryptophyte phycocyanin 645&nbsp;<em>T Mirkovic, et al,<\/em>&nbsp;<em>Photochemical &amp; Photobiological Sciences 6 (9), 964-975<\/em><\/li><li>How energy funnels from the phycoerythrin antenna complex to photosystem I and photosystem II in cryptophyte Rhodomonas CS24 cells&nbsp;<em>CD van der Weij-De Wit, et al,<\/em>&nbsp;<em>The Journal of Physical Chemistry B 110 (49), 25066-25073<\/em><\/li><li>The photophysics of cryptophyte light-harvesting&nbsp;<em>AB Doust, et al,<\/em>&nbsp;<em>Journal of Photochemistry and Photobiology A: Chemistry 184 (1-2), 1-17<\/em><\/li><li>Mediation of ultrafast light-harvesting by a central dimer in phycoerythrin 545 studied by transient absorption and global analysis&nbsp;<em>AB Doust, et al,<\/em>&nbsp;<em>The Journal of Physical Chemistry B 109 (29), 14219-14226<\/em><\/li><li>Structural studies of a cryptophyte light harvesting phycocyanin PC645&nbsp;<em>KE Wilk, et al, T<\/em><em>he Febs Journal 272, 454<\/em><\/li><li>Developing a structure\u2013function model for the cryptophyte phycoerythrin 545 using ultrahigh resolution crystallography and ultrafast laser spectroscopy&nbsp;<em>AB Doust, et al,<\/em>&nbsp;<em>Journal of molecular biology 344 (1), 135-153<\/em><\/li><\/ol>\n\n\n\n<hr class=\"wp-block-separator is-style-wide\"\/>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<h1 class=\"wp-block-heading\">Dynamic Pattern Formation in Cells  <\/h1>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<ol class=\"wp-block-list\"><li>Non-linear Min protein interactions generate harmonics that signal mid-cell division in Escherichia coli,<em>&nbsp;JC Walsh, CN Angstmann, IG Duggin, PMG Curmi,&nbsp;PloS one 12 (10), e0185947<\/em><\/li><li>Developing a genetic manipulation system for the Antarctic archaeon, Halorubrum lacusprofundi: investigating acetamidase gene function<em>Y Liao, et al,<\/em>&nbsp;<em>Scientific reports 6, 34639<\/em><\/li><li>Patterning of the MinD cell division protein in cells of arbitrary shape can be predicted using a heuristic dispersion relation&nbsp;<em>JC Walsh, et al,<\/em>&nbsp;<em>AIMS Biophysics<\/em><\/li><li>Molecular interactions of the Min protein system reproduce spatiotemporal patterning in growing and dividing Escherichia coli cells&nbsp;<em>JC Walsh, et al,PloS one 10 (5), e0128148<\/em><\/li><\/ol>\n\n\n\n<hr class=\"wp-block-separator is-style-wide\"\/>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<h1 class=\"wp-block-heading\">Archaea &amp; Cold Adaptation<\/h1>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<ol class=\"wp-block-list\"><li>Single TRAM domain RNA\u2010binding proteins in Archaea: functional insight from Ctr3 from the Antarctic methanogen Methanococcoides burtonii&nbsp;<em>KS Siddiqui, et al,&nbsp;<\/em><em>Environmental microbiology 18 (9), 2810-2824<\/em><\/li><li>Characterization of a temperature-responsive two component regulatory system from the Antarctic archaeon, Methanococcoides burtonii&nbsp;<em>T Najnin, et al,&nbsp;<\/em><em>Scientific reports 6, 24278<\/em><\/li><li>The RNA polymerase subunits E\/F from the Antarctic archaeon Methanococcoides burtonii bind to specific species of mRNA&nbsp;<em>D De Francisci, et al,<\/em>&nbsp;<em>Environmental microbiology 13 (8), 2039-2055<\/em><\/li><li>Chaperonins from an Antarctic archaeon are predominantly monomeric: crystal structure of an open state monomer<em>&nbsp;O Pilak, et al,<\/em>&nbsp;<em>Environmental microbiology 13 (8), 2232-2249<\/em><\/li><li>Crystal structure of Lsm3 octamer from Saccharomyces cerevisiae: implications for Lsm ring organisation and recruitment&nbsp;<em>N Naidoo, et al,&nbsp;<\/em><em>Journal of molecular biology 377 (5), 1357-1371<\/em><\/li><li>Structure and function of cold shock proteins in archaea&nbsp;<em>L Giaquinto, et al,<\/em>&nbsp;<em>Journal of bacteriology 189 (15), 5738-5748<\/em><\/li><li>Role of lysine versus arginine in enzyme cold\u2010adaptation: Modifying lysine to homo\u2010arginine stabilizes the cold\u2010adapted \u03b1\u2010amylase from Pseudoalteramonas haloplanktis&nbsp;<em>KS Siddiqui,et al,<\/em>&nbsp;<em>PROTEINS: Structure, Function, and Bioinformatics 64 (2), 486-501<\/em><\/li><li>17 Proteins from Psychrophiles&nbsp;<em>R Cavicchioli, et al,<\/em>&nbsp;<em>Methods in Microbiology 35, 395-436<\/em><\/li><li>Predicted Roles for Hypothetical Proteins in the Low-Temperature Expressed Proteome of the Antarctic Archaeon Methanococcoides burtonii&nbsp;<em>NFW Saunders, et al,<\/em>&nbsp;<em>Journal of proteome research 4 (2), 464-472<\/em><\/li><li>A proteomic determination of cold adaptation in the Antarctic archaeon, Methanococcoides burtonii&nbsp;<em>A Goodchild, et al,<\/em>&nbsp;<em>Molecular microbiology 53 (1), 309-321<\/em><\/li><li>An online database for the detection of novel archaeal sequences in human ESTs&nbsp;<em>NFW Saunders, et al,<\/em>&nbsp;<em>Bioinformatics 20 (15), 2361-2362<\/em><\/li><li>Pathogenic archaea: do they exist?&nbsp;<em>R Cavicchioli, et al,<\/em>&nbsp;Bioessays 25 (11), 1119-1128<\/li><li>Mechanisms of thermal adaptation revealed from the genomes of the Antarctic Archaea Methanogenium frigidum and Methanococcoides burtonii&nbsp;<em>NFW Saunders, et al,<\/em>&nbsp;<em>Genome research 13 (7), 1580-1588<\/em><\/li><li>Homomeric Ring Assemblies of Eukaryotic Sm Proteins Have Affinity for Both RNA and DNA crystal structure of an oligomeric complex of yeast Smf&nbsp;<em>BM Collins, et al,<\/em>&nbsp;<em>Journal of Biological Chemistry 278 (19), 17291-17298<\/em><\/li><li>Crystal structure of a heptameric Sm-like protein complex from archaea: implications for the structure and evolution of snRNPs1&nbsp;<em>BM Collins, et al,<\/em>&nbsp;<em>Journal of molecular biology 309 (4), 915-923<\/em><\/li><li>Cold stress response in Archaea<em>&nbsp;R Cavicchioli, et al,&nbsp;Extremophiles 4 (6), 321-331<\/em><\/li><\/ol>\n\n\n\n<hr class=\"wp-block-separator is-style-wide\"\/>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<h1 class=\"wp-block-heading\"> Molecular Chaperones <\/h1>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<ol class=\"wp-block-list\"><li> Chaperonins from an Antarctic archaeon are predominantly monomeric: crystal structure of an open state monomer&nbsp;<em>O Pilak, et al,Environmental microbiology 13 (8), 2232-2249<\/em><\/li><\/ol>\n\n\n\n<hr class=\"wp-block-separator is-style-wide\"\/>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<h1 class=\"wp-block-heading\">Integrons and Gene Cassette Proteins<\/h1>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<ol class=\"wp-block-list\"><li>Integron gene cassettes: a repository of novel protein folds with distinct interaction sites&nbsp;<em>V Sureshan, et al,<\/em>&nbsp;<em>PLoS One 8 (1), e5293<\/em><\/li><li>Crystal structure of an integron gene cassette-associated protein from Vibrio cholerae identifies a cationic drug-binding module&nbsp;<em>CN Deshpande, et al,<\/em>&nbsp;<em>PLoS One 6 (3), e16934<\/em><\/li><li>Structural genomics of the bacterial mobile metagenome: an overview&nbsp;<em>A Robinson, et al,<\/em>&nbsp;<em>Structural Proteomics, 589-595<\/em><\/li><li>A putative house\u2010cleaning enzyme encoded within an integron array: 1.8 \u00c5 crystal structure defines a new MazG subtype&nbsp;<em>A Robinson,et al,<\/em>&nbsp;<em>Molecular microbiology 66 (3), 610-621<\/em><\/li><li>Integron-associated mobile gene cassettes code for folded proteins: the structure of Bal32a, a new member of the adaptable \u03b1+ \u03b2 barrel family&nbsp;<em>A Robinson, et al,<\/em>&nbsp;<em>Journal of molecular biology 346 (5), 1229-1241<\/em><\/li><li>In vivo protein cyclization promoted by a circularly permuted Synechocystis sp. PCC6803 DnaB mini-intein&nbsp;<em>NK Williams, et al,<\/em>&nbsp;<em>Journal of Biological Chemistry 277 (10), 7790-7798<\/em><\/li><\/ol>\n\n\n\n<hr class=\"wp-block-separator is-style-wide\"\/>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<h1 class=\"wp-block-heading\">Protease Inhibitors and Serpins<\/h1>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<ol class=\"wp-block-list\"><li>Arabidopsis AtSerpin1, crystal structure and in vivo interaction with its target protease responsive to dessication-21 (RD21)&nbsp;<em>N Lampl, et al,<\/em>&nbsp;<em>Journal of Biological Chemistry 285 (18), 13550-13560<\/em><\/li><li>Plasminogen activator inhibitor-2 is highly tolerant to P8 residue substitution\u2014implications for serpin mechanistic model and prediction of nsSNP activities&nbsp;<em>DA Di Giusto,et al,<\/em>&nbsp;<em>Journal of molecular biology 353 (5), 1069-1080<\/em><\/li><li>Serpins in unicellular Eukarya, Archaea, and Bacteria: sequence analysis and evolution&nbsp;<em>TH Roberts,et al,<\/em>&nbsp;<em>Journal of molecular evolution 59 (4), 437-447<\/em><\/li><li>Interaction between the P14 residue and strand 2 of \u03b2-sheet B is critical for reactive center loop insertion in plasminogen activator inhibitor-2&nbsp;<em>DN Saunders, et al,<\/em>&nbsp;<em>Journal of Biological Chemistry 276 (46), 43383-43389<\/em><\/li><li>Crystal structure of the complex of plasminogen activator inhibitor 2 with a peptide mimicking the reactive center loop&nbsp;<em>L Jankova, et al,<\/em>&nbsp;<em>Journal of Biological Chemistry 276 (46), 43374-43382<\/em><\/li><\/ol>\n\n\n\n<hr class=\"wp-block-separator is-style-wide\"\/>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<h1 class=\"wp-block-heading\"> \u03b2  Sheet Structures in Proteins<\/h1>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<ol class=\"wp-block-list\"><li>Twist and shear in \u03b2-sheets and \u03b2-ribbons&nbsp;<em>BK Ho &amp;&nbsp;PMG Curmi<\/em>&nbsp;<em>Journal of molecular biology 317 (2), 291-308<\/em><\/li><li>An analysis of side chain interactions and pair correlations within antiparallel \u03b2\u2010sheets: The differences between backbone hydrogen\u2010bonded and non\u2010hydrogen\u2010bonded residue pairs<em>&nbsp;M. A. Wouters &amp;&nbsp;PMG Curmi<\/em>&nbsp;<em>Proteins.&nbsp;1995 Jun;22(2):119-31<\/em><\/li><\/ol>\n\n\n\n<hr class=\"wp-block-separator is-style-wide\"\/>\n","protected":false},"excerpt":{"rendered":"<p>Membrane Remodelling &amp; Metamorphic Proteins Structural characterization suggests models for monomeric and dimeric forms of full-length ezrin&nbsp;JM Phang, et al,&nbsp;Biochemical Journal 473 (18), 2763-2782 Interaction of human Chloride Intracellular Channel Protein 1 (CLIC1) with lipid bilayers: a fluorescence study&nbsp;JE Hare, et al,&nbsp;Biochemistry 55 (27), 3825-3833 CLIC1 regulates dendritic cell antigen processing and presentation by modulating phagosome acidification and proteolysis&nbsp;K Salao, et al,&nbsp;Biology open, bio. 018119 Members of the chloride intracellular<\/p>\n<div class=\"read-more\"><a class=\"btn read-more-btn\" href=\"https:\/\/www.protein.physics.unsw.edu.au\/?page_id=231\">Read More<\/a><\/div>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-231","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=\/wp\/v2\/pages\/231","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=231"}],"version-history":[{"count":5,"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=\/wp\/v2\/pages\/231\/revisions"}],"predecessor-version":[{"id":265,"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=\/wp\/v2\/pages\/231\/revisions\/265"}],"wp:attachment":[{"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=231"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}