M. Sunde

发表

J. Matthews, M. Sunde, 2012, Advances in experimental medicine and biology.

The power of two: protein dimerization in biology.

J. Matthews, M. Sunde, Neelan J Marianayagam, 2004, Trends in biochemical sciences.

Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry.

C. Dobson, C. Robinson, M. Sunde, 2000, Biophysical journal.

Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein.

C. Dobson, C. MacPhee, J. Carver, 2005, Biochemistry.

Amyloid fibril formation by bovine milk alpha s2-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha s1-casein.

J. Carver, M. Sunde, H. Ecroyd, 2008, Biochemistry.

Common core structure of amyloid fibrils by synchrotron X-ray diffraction.

L. Serpell, C. Blake, P. Fraser, 1997, Journal of molecular biology.

The protofilament substructure of amyloid fibrils.

L. Serpell, P. Fraser, M. Benson, 2000, Journal of molecular biology.

Amyloid fibril formation by an SH3 domain.

I D Campbell, C. Dobson, I. Campbell, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Hydrophobins—Unique Fungal Proteins

J. Latgé, M. Sunde, J. I. Guijarro, 2012, PLoS pathogens.

Microbial functional amyloids serve diverse purposes for structure, adhesion and defence

M. Sunde, N. Shanmugam, M. Baker, 2019, Biophysical Reviews.

Backbone dynamics of oxidised and reduced forms of human atrial natriuretic peptide.

M. Sunde, R. Broadhurst, K. Stott, 2004, Journal of structural biology.

Polymorphism and higher order structures of protein nanofibers from crude mixtures of fish lens crystallins: toward useful materials.

C. Roux, L. Domigan, M. Sunde, 2012, Biopolymers.

Fungal Hydrophobins and Their Self-Assembly into Functional Nanomaterials.

M. Sunde, Victor Lo, Jennifer I-Chun Lai, 2019, Advances in experimental medicine and biology.

Formation of Amphipathic Amyloid Monolayers from Fungal Hydrophobin Proteins.

M. Sunde, A. Kwan, Victor Lo, 2020, Methods in molecular biology.

Solution structure and interface‐driven self‐assembly of NC2, a new member of the Class II hydrophobin proteins

M. Sunde, A. Kwan, Q. Ren, 2014, Proteins.

Cell-free expression of natively folded hydrophobins.

G. Otting, M. Sunde, A. Kwan, 2020, Protein expression and purification.

A gain-of-function TBX20 mutation causes congenital atrial septal defects, patent foramen ovale and cardiac valve defects

A. Mégarbané, R. Dietz, R. Harvey, 2009, Journal of Medical Genetics.

Molecular mechanisms of fibrillogenesis and the protective role of amyloid P component: two possible avenues for therapy.

S. Radford, D. Booth, C. Robinson, 1996, Ciba Foundation symposium.

Dissection of multi‐protein complexes using mass spectrometry: Subunit interactions in transthyretin and retinol‐binding protein complexes

C. Dobson, C. Robinson, M. Sunde, 1998, Proteins.

The RHIM of the Immune Adaptor Protein TRIF Forms Hybrid Amyloids with Other Necroptosis-Associated Proteins

M. Sunde, Y. Gambin, E. Sierecki, 2022, Molecules.

Viral M45 and necroptosis‐associated proteins form heteromeric amyloid assemblies

M. Sunde, Y. Gambin, E. Sierecki, 2018, EMBO reports.

The RHIM within the M45 protein from murine cytomegalovirus forms heteromeric amyloid fibrils with RIPK1 and RIPK3

M. Sunde, Y. Gambin, E. Sierecki, 2018, bioRxiv.

Versatile naphthalimide tetrazines for fluorogenic bioorthogonal labelling

M. Sunde, D. Jacquemin, Sarah R. Ball, 2021, RSC chemical biology.

RHIM-based protein:protein interactions in microbial defence against programmed cell death by necroptosis.

M. Sunde, M. Baker, M. Steain, 2020, Seminars in cell & developmental biology.

Don't Turn Off the Tap! The Importance of Discovery Science to the Australian Cardiovascular Sector and Improving Clinical Outcomes Into the Future.

G. Figtree, R. Harvey, M. Sunde, 2022, Heart, lung & circulation.

Surface functionalization of carbon nanomaterials by self-assembling hydrophobin proteins.

F. Braet, Wenrong Yang, M. Sunde, 2013, Biopolymers.

Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity.

Christopher G. Adda, C. Masters, C. Robinson, 2004, Journal of molecular biology.

Amyloid fibril formation by αS1- and β-casein implies that fibril formation is a general property of all casein proteins.

J. Carver, M. Sunde, C. Holt, 2022, Biochimica et biophysica acta. Proteins and proteomics.

Hydrophobin Rodlets on the Fungal Cell Wall.

M. Sunde, A. Kwan, Sarah R. Ball, 2019, Current topics in microbiology and immunology.

Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry.

C. Dobson, C. Robinson, J. Kelly, 1998, Journal of molecular biology.

Mutations in cardiac T-box factor gene TBX20 are associated with diverse cardiac pathologies, including defects of septation and valvulogenesis and cardiomyopathy.

Mauro W. Costa, C. Hayward, D. Fatkin, 2007, American journal of human genetics.

Varicella zoster virus encodes a viral decoy RHIM to inhibit cell death

M. Sunde, Y. Gambin, E. Sierecki, 2020, bioRxiv.

Molecular Characteristics and Biological Functions of Surface-Active and Surfactant Proteins.

M. Sunde, A. Kwan, Chi L. L. Pham, 2017, Annual review of biochemistry.

Improved conditions for the removal of 2-oxoacyl groups from the N-terminus of proteins.

M. Sunde, H. Dixon, M. Sparkes, 1998, Biochimica et biophysica acta.

The C-terminal Domain of Eos Forms a High Order Complex in Solution*

J. Mackay, M. Sunde, M. Crossley, 2003, Journal of Biological Chemistry.

Sticky-end assembly of a designed peptide fiber provides insight into protein fibrillogenesis.

D N Woolfson, D. Woolfson, M. Sunde, 2000, Biochemistry.

Structural analysis of hydrophobins.

Joel P Mackay, J. Mackay, M. Sunde, 2008, Micron.

Native disulphide-linked dimers facilitate amyloid fibril formation by bovine milk αS2-casein.

Glyn L. Devlin, P. Hoffmann, J. Carver, 2020, Biophysical chemistry.

Probing Structural Changes during Self-assembly of Surface-Active Hydrophobin Proteins that Form Functional Amyloids in Fungi.

R. Cappai, M. Sunde, A. Kwan, 2018, Journal of molecular biology.

The Role of RodA-Conserved Cysteine Residues in the Aspergillus fumigatus Conidial Surface Organization

J. Latgé, M. Sunde, O. Kniemeyer, 2020, Journal of fungi.

Cryo‐electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing

Elena Orlova, C. Dobson, E. Orlova, 1999, The EMBO journal.

EspL is a bacterial cysteine protease effector that cleaves RHIM proteins to block necroptosis and inflammation

Laura F. Dagley, M. Sunde, S. Masters, 2017, Nature Microbiology.

Identification of the key LMO2-binding determinants on Ldb1.

Joel P Mackay, J. Visvader, J. Mackay, 2006, Journal of molecular biology.

Zinc Fingers‐‐Folds for Many Occasions

J. Matthews, M. Sunde, Margaret Sunde, 2002, IUBMB life.

Herpes simplex virus encoded ICP6 protein forms functional amyloid assemblies with necroptosis-associated host proteins.

M. Sunde, Y. Gambin, E. Sierecki, 2020, Biophysical chemistry.

Functional amyloid: widespread in Nature, diverse in purpose.

M. Sunde, A. Kwan, Margaret Sunde, 2014, Essays in biochemistry.

Beta2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils.

C. Robinson, M. Sunde, D. Brancaccio, 1998, European journal of biochemistry.

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

Christopher M. Dobson, Sheena E. Radford, Carol V. Robinson, 1997, Nature.

Solid-State NMR Structure Determination from Diagonal-Compensated, Sparsely Nonuniform-Sampled 4D Proton–Proton Restraints

S. Hyberts, G. Wagner, M. Sunde, 2014, Journal of the American Chemical Society.

Solid-state NMR spectroscopy of functional amyloid from a fungal hydrophobin: a well-ordered β-sheet core amidst structural heterogeneity.

M. Sunde, A. Kwan, A. Duff, 2012, Angewandte Chemie.

Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex

J. Visvader, M. Maher, J. Matthews, 2004, The EMBO journal.

Plasmodium falciparum merozoite surface protein 2 is unstructured and forms amyloid-like fibrils.

Christopher G. Adda, M. Foley, V. Murphy, 2009, Molecular and biochemical parasitology.

Competition between LIM-binding domains.

J. Matthews, M. Sunde, C. Jeffries, 2008, Biochemical Society transactions.

Recruitment of Class I Hydrophobins to the Air:Water Interface Initiates a Multi-step Process of Functional Amyloid Formation*

M. Sunde, A. Kwan, N. Byrne, 2011, The Journal of Biological Chemistry.

Fungal Hydrophobin Proteins Produce Self-Assembling Protein Films with Diverse Structure and Chemical Stability

M. Sunde, A. Kwan, Victor Lo, 2014, Nanomaterials.

Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS

Joel P. Mackay, Wenrong Yang, Ann H. Kwan, 2012, Proceedings of the National Academy of Sciences.

Assembly and disassembly of Aspergillus fumigatus conidial rodlets

Quentin Giai Gianetto, A. Beaussart, J. Latgé, 2019, Cell surface.

Solution structure and interface‐driven self‐assembly of NC2, a new member of the Class II hydrophobin proteins

M. Sunde, A. Kwan, Q. Ren, 2014, Proteins.

Backbone and sidechain 1H, 13C and 15N chemical shift assignments of the hydrophobin MPG1 from the rice blast fungus Magnaporthe oryzae

M. Sunde, A. Kwan, A. Rey, 2013, Biomolecular NMR assignments.

Intrinsic disorder modulates protein self-assembly and aggregation

D. Frenkel, C. Dobson, M. Sunde, 2012, Proceedings of the National Academy of Sciences.

From the globular to the fibrous state: protein structure and structural conversion in amyloid formation

C. Blake, M. Sunde, C C Blake, 1998, Quarterly Reviews of Biophysics.

The molecular basis of amyloidosis

L. Serpell, C. Blake, M. Sunde, 1997, Cellular and Molecular Life Sciences CMLS.

The structure of amyloid fibrils by electron microscopy and X-ray diffraction.

C. Blake, M. Sunde, C Blake, 1997, Advances in protein chemistry.

Conformational Switching and Fibrillogenesis in the Amyloidogenic Fragment of Apolipoprotein A-I*

J. Torres, M. Sunde, E. Monzani, 2003, The Journal of Biological Chemistry.

Amyloid fibrils derived from the apolipoprotein A1 Leu174Ser variant contain elements of ordered helical structure

M. Sunde, G. Esposito, P. Viglino, 2001, Protein science : a publication of the Protein Society.

Strategies for the molecular imaging of amyloid and the value of multi-modal approach.

M. Sunde, E. New, Amandeep Kaur, 2020, ACS sensors.

The crystal structure of transthyretin from chicken.

C. Blake, M. Sunde, S. Richardson, 1996, European journal of biochemistry.

Protein interactions: is seeing believing?

Merlin Crossley, Joel P Mackay, Jason A. Lowry, 2007, Trends in biochemical sciences.

Backbone and sidechain 1H, 13C and 15N chemical shift assignments of the hydrophobin DewA from Aspergillus nidulans

J. Mackay, M. Sunde, A. Kwan, 2012, Biomolecular NMR assignments.

Perphenazine-macrocycle conjugates divert Aβ42 towards non-toxic aggregates by monomer sequestration

M. Kassiou, M. Sunde, A. Kwan, 2020, bioRxiv.

A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation.

S. Radford, Susan Jones, L. Serpell, 2003, Journal of molecular biology.

Examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs.

P E Fraser, E P Morris, L. Serpell, 1995, Journal of molecular biology.

Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro.

S. Radford, M. Sunde, P. Kirwin-Jones, 2000, Biochemistry.

Analysis of the structure and conformational states of DewA gives insight into the assembly of the fungal hydrophobins.

M. Sunde, A. Kwan, Vanessa K Morris, 2013, Journal of molecular biology.

Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme

C. Dobson, C. Robinson, M. Sunde, 2002, Nature Structural Biology.

Serum Albumin Prevents Protein Aggregation and Amyloid Formation and Retains Chaperone-like Activity in the Presence of Physiological Ligands

A. Nunez, M. Sunde, S. Easterbrook-Smith, 2012, The Journal of Biological Chemistry.

A molecular model of the amyloid fibril.

L. Serpell, C. Blake, M. Sunde, 1996, Ciba Foundation symposium.

Conformational stability and DNA binding specificity of the cardiac T-box transcription factor Tbx20.

Mauro W. Costa, J. Mackay, R. Harvey, 2009, Journal of molecular biology.

Mechanism of block of the hERG K+ channel by the scorpion toxin CnErg1.

M. Sunde, A. Hill, J. Vandenberg, 2007, Biophysical journal.

Interaction of the Molecular Chaperone αB-Crystallin with α-Synuclein: Effects on Amyloid Fibril Formation and Chaperone Activity

Christopher G. Adda, C. Masters, C. Robinson, 2004 .

Perphenazine-macrocycle conjugates divert Aβ42 towards non-toxic aggregates by monomer sequestration

M. Kassiou, M. Sunde, A. Kwan, 2020, bioRxiv.

Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants.

C. Dobson, C. Robinson, A. Miranker, 1999, Biochemistry.

X-ray fiber diffraction of amyloid fibrils.

L. Serpell, P. Fraser, M. Sunde, 1999, Methods in enzymology.

TC-1 is a novel tumorigenic and natively disordered protein associated with thyroid cancer.

L. Young, J. Mackay, J. Matthews, 2004, Cancer research.

Structural basis for rodlet assembly in fungal hydrophobins.

J. Mackay, J. Matthews, M. Sunde, 2006, Proceedings of the National Academy of Sciences of the United States of America.

Two forms and two faces, multiple states and multiple uses: Properties and applications of the self-assembling fungal hydrophobins.

M. Sunde, A. Kwan, Q. Ren, 2013, Biopolymers.

The Cys3-Cys4 loop of the hydrophobin EAS is not required for rodlet formation and surface activity.

A. Mark, J. Mackay, M. Sunde, 2008, Journal of molecular biology.

Self-assembly of MPG1, a hydrophobin protein from the rice blast fungus that forms functional amyloid coatings, occurs by a surface-driven mechanism

M. Sunde, A. Kwan, T. Knowles, 2016, Scientific Reports.

Functional Amyloids: Where Supramolecular Amyloid Assembly Controls Biological Activity or Generates New Functionality.

M. Sunde, Caitlin L Johnston, Jessica A Buchanan, 2022, Journal of molecular biology.

Heterologously-expressed and Liposome-reconstituted Human Transient Receptor Potential Melastatin 4 Channel (TRPM4) is a Functional Tetramer

R. Whan, R. Graham, M. Sunde, 2016, Scientific Reports.

Perphenazine-Macrocycle Conjugates Rapidly Sequester the Aβ42 Monomer and Prevent Formation of Toxic Oligomers and Amyloid.

M. Kassiou, M. Sunde, A. Kwan, 2022, ACS chemical neuroscience.

Structure of the HERG K+ Channel S5P Extracellular Linker

P. Kuchel, M. Sunde, S. Breit, 2003, Journal of Biological Chemistry.

Plasmodium falciparum merozoite surface protein 2 is unstructured and forms amyloid-like fibrils

Christopher G. Adda, M. Foley, V. Murphy, 2009 .

Single‐Molecule Two‐Color Coincidence Detection of Unlabeled alpha‐Synuclein Aggregates

A. Pastore, M. Horrocks, D. Clarke, 2023, Angewandte Chemie.

Two-color coincidence single-molecule pulldown for the specific detection of disease-associated protein aggregates

M. Horrocks, M. Sunde, S. Gandhi, 2023, bioRxiv.

A fluorescent amyloid sensor for quantitative super-resolution imaging of amyloid fibril assembly.

M. Sunde, E. New, Amandeep Kaur, 2021 .

A gain-of-function TBX20 mutation causes congenital atrial septal defects, patent foramen ovale and cardiac valve defects

A. Mégarbané, R. Dietz, R. Harvey, 2009, Journal of Medical Genetics.

iPSC-Derived PSEN2 (N141I) Astrocytes and Microglia Exhibit a Primed Inflammatory Phenotype

M. Kassiou, M. Sunde, M. A. Sullivan, 2022, bioRxiv.

Solid-state NMR spectroscopy of functional amyloid from a fungal hydrophobin: a well-ordered β-sheet core amidst structural heterogeneity.

M. Sunde, A. Kwan, A. Duff, 2012, Angewandte Chemie.

Surface-Induced Hydrophobin Assemblies with Versatile Properties and Distinct Underlying Structures.

M. Sunde, A. Kwan, Victor Lo, 2023, Biomacromolecules.

Access to side-chain carbon information in deuterated solids under fast MAS through non-rotor-synchronized mixing.

S. Becker, M. Sunde, A. Kwan, 2016, Chemical communications.

Amyloid fibril formation, structure and domain swapping of acyl‐coenzyme A thioesterase‐7

J. Carver, M. Sunde, J. Forwood, 2023, The FEBS journal.

Competition between LIM-binding domains.

J. Matthews, M. Sunde, C. Jeffries, 2008, Biochemical Society transactions.

Recruitment of Class I Hydrophobins to the Air:Water Interface Initiates a Multi-step Process of Functional Amyloid Formation*

M. Sunde, A. Kwan, Q. Ren, 2011, The Journal of Biological Chemistry.

NMR characterization of an assembling RHIM (RIP Homotypic Interaction Motif) amyloid reveals a cryptic region for self-recognition.

M. Sunde, Chi L. L. Pham, K. Wilde, 2023, The Journal of biological chemistry.