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Results: 27
Unique charge-dependent constraint on collagen recognition by integrin α10β1.
Samir W Hamaia, Daisy Luff, Emma J Hunter, Jean-Daniel Malcor, Dominique Bihan, Donald Gullberg, Richard W Farndale
Oct 31, 2016
C2C12 cells Cartilage GROGER Integrin I domain Triple-helical peptides Amino Acid Motifs Amino Acid Sequence Animals Binding Sites cations Divalent Cell Line Collagen Type II Edetic Acid Gene Expression Humans Integrin alpha Chains Magnesium Mice Models Molecular Muscle Fibers Skeletal Peptides Protein Binding Protein Conformation alpha-Helical Protein Conformation beta-Strand Protein Interaction Domains and Motifs Recombinant Proteins Sequence Alignment Static Electricity
Structural and functional analysis of two small leucine-rich repeat proteoglycans, fibromodulin and chondroadherin.
Patricia Paracuellos, Sebastian Kalamajski, Arkadiusz Bonna, Dominique Bihan, Richard W Farndale, Erhard Hohenester
Jan 24, 2018
The small leucine-rich proteoglycans (SLRPs) are important regulators of extracellular matrix assembly and cell signalling. We have determined crystal structures at ~2.2Å resolution of human fibromodulin and chondroadherin, two...
Collagen Leucine-rich repeat X-ray crystallography Amino Acid Sequence Crystallography X-Ray Cystine Extracellular Matrix Proteins fibromodulin HEK293 Cells Humans Hydrophobic and Hydrophilic Interactions Models Molecular Protein Binding Protein Conformation beta-Strand Protein Interaction Domains and Motifs Protein Structure Quaternary Solutions
The Amyloid Fibril-Forming β-Sheet Regions of Amyloid β and α-Synuclein Preferentially Interact with the Molecular Chaperone 14-3-3ζ.
Danielle M Williams, David C Thorn, Christopher M Dobson, Sarah Meehan, Sophie E Jackson, Joanna M Woodcock, John A Carver
Jan 06, 2022
14-3-3 proteins are abundant, intramolecular proteins that play a pivotal role in cellular signal transduction by interacting with phosphorylated ligands. In addition, they are molecular chaperones that prevent protein unfolding...
14-3-3 Proteins NMR spectroscopy Amyloid fibril amyloid β molecular chaperone α-synuclein 14-3-3 Proteins Amyloid Amyloid beta-Peptides Humans Molecular Chaperones Protein Aggregates Protein Binding Protein Conformation Protein Conformation beta-Strand Protein Interaction Domains and Motifs Protein Unfolding ALPHA-SYNUCLEIN
Stoichiometric and irreversible cysteine-selective protein modification using carbonylacrylic reagents
B Bernardim, PMSD Cal, MJ Matos, BL Oliveira, N Martínez-Sáez, IS Albuquerque, E Perkins, F Corzana, ACB Burtoloso, G Jiménez-Osés, GJL Bernardes
Nov 04, 2016
Acetonitriles Acrylates Amino Acid Sequence Annexin A5 Benzoates Cross-Linking Reagents Cysteine HEK293 Cells Humans Immunoconjugates Maleimides Protein Conformation alpha-Helical Protein Conformation beta-Strand Protein Stability Receptor ErbB-2 Staining and Labeling Stereoisomerism Sulfides Trastuzumab
JMJD5 is a human arginyl C-3 hydroxylase.
Sarah E Wilkins, Md Saiful Islam, Joan M Gannon, Suzana Markolovic, Richard J Hopkinson, Wei Ge, Christopher J Schofield, Rasheduzzaman Chowdhury
Jun 26, 2020
Oxygenase-catalysed post-translational modifications of basic protein residues, including lysyl hydroxylations and Nε-methyl lysyl demethylations, have important cellular roles. Jumonji-C (JmjC) domain-containing protein 5...
Arginine Carrier Proteins Catalytic Domain Cloning Molecular Crystallography X-Ray Escherichia coli Gene Expression Genetic Vectors Histone Demethylases Humans Hydroxylation Kinetics Lysine Membrane Proteins Models Molecular Protein Binding Protein Conformation alpha-Helical Protein Conformation beta-Strand Protein Folding Protein Interaction Domains and Motifs Recombinant Proteins ribosomal protein S6 Stereoisomerism Substrate Specificity Thermodynamics
Structure of KAP1 tripartite motif identifies molecular interfaces required for retroelement silencing.
Guido A Stoll, Shun-Ichiro Oda, Zheng-Shan Chong, Minmin Yu, Stephen H McLaughlin, Yorgo Modis
Jun 19, 2019
Endogenous retrovirus epigenetic silencing transcriptional repressor transposable element ubiquitin E3 ligase Amino Acid Sequence Binding Sites Chromatin Chromatin Assembly and Disassembly Cloning Molecular Crystallography X-Ray Epigenesis Genetic Escherichia coli Gene Expression Gene Silencing Genetic Vectors Humans Models Molecular Protein Binding Protein Conformation alpha-Helical Protein Conformation beta-Strand Protein Interaction Domains and Motifs Protein Multimerization Recombinant Proteins Repressor Proteins Retroelements Sequence Alignment Sequence Homology Amino Acid Transcription Genetic Tripartite Motif-Containing Protein 28
MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography.
Max TB Clabbers, Susannah Holmes, Timothy W Muusse, Parimala R Vajjhala, Sara J Thygesen, Alpeshkumar K Malde, Dominic JB Hunter, Tristan I Croll, Leonie Flueckiger, Jeffrey D Nanson, Md Habibur Rahaman, Andrew Aquila, Mark S Hunter, Mengning Liang, Chun Hong Yoon, Jingjing Zhao, Nadia A Zatsepin, Brian Abbey, Emma Sierecki, Yann Gambin, Katryn J Stacey, Connie Darmanin, Bostjan Kobe, Hongyi Xu, Thomas Ve
May 06, 2021
MyD88 and MAL are Toll-like receptor (TLR) adaptors that signal to induce pro-inflammatory cytokine production. We previously observed that the TIR domain of MAL (MALTIR) forms filaments in vitro and induces formation of...
Crystallography Dimerization HEK293 Cells Humans Membrane Glycoproteins Models Molecular Molecular Dynamics Simulation Mutation Myeloid Differentiation Factor 88 Protein Conformation alpha-Helical Protein Conformation beta-Strand Protein Domains Receptors Interleukin-1 Recombinant Proteins Signal Transduction Toll-Like Receptor 4
DJ-1 can form β-sheet structured aggregates that co-localize with pathological amyloid deposits.
Katalin Solti, Wei-Li Kuan, Balázs Fórizs, Gergely Kustos, Judith Mihály, Zoltán Varga, Balázs Herberth, Éva Moravcsik, Róbert Kiss, Manuela Kárpáti, Anna Mikes, Yanyan Zhao, Tímea Imre, Jean-Christophe Rochet, Franklin Aigbirhio, Caroline H Williams-Gray, Roger A Barker, Gergely Tóth
Oct 03, 2019
EXPRESS
Amide I deconvolution Savitzky–Golay adjacent averaging fast Fourier transform filter protein secondary structures signal smoothing similarity index Algorithms Fourier Analysis Hair Humans Protein Conformation alpha-Helical Protein Conformation beta-Strand Proteins spectroscopy Fourier Transform Infrared
A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion.
Mathieu Botte, Nathan R Zaccai, Jelger Lycklama À Nijeholt, Remy Martin, Kèvin Knoops, Gabor Papai, Juan Zou, Aurélien Deniaud, Manikandan Karuppasamy, Qiyang Jiang, Abhishek Singha Roy, Klaus Schulten, Patrick Schultz, Juri Rappsilber, Giuseppe Zaccai, Imre Berger, Ian Collinson, Christiane Schaffitzel
Dec 01, 2017
The conserved SecYEG protein-conducting channel and the accessory proteins SecDF-YajC and YidC constitute the bacterial holo-translocon (HTL), capable of protein-secretion and membrane-protein insertion. By employing an...
Binding Sites Cloning Molecular Cryoelectron Microscopy Escherichia coli Escherichia coli Proteins Gene Expression Genetic Vectors Membrane Transport Proteins Methanocaldococcus Models Molecular neutron diffraction Protein Binding Protein Conformation alpha-Helical Protein Conformation beta-Strand Protein Interaction Domains and Motifs Protein Transport Recombinant Proteins SEC Translocation Channels SCATTERING Small Angle Structural Homology Protein Substrate Specificity Thermus thermophilus
Biophotonics of Native Silk Fibrils.
Ulyana Shimanovich, Dorothea Pinotsi, Klimentiy Shimanovich, Na Yu, Sreenath Bolisetty, Jozef Adamcik, Raffaele Mezzenga, Jerome Charmet, Fritz Vollrath, Ehud Gazit, Christopher M Dobson, Gabriele Kaminski Schierle, Chris Holland, Clemens F Kaminski, Tuomas PJ Knowles
May 07, 2019
MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography.
Max T B Clabbers, Susannah Holmes, Timothy W Muusse, Parimala R Vajjhala, Sara J Thygesen, Alpeshkumar K Malde, Dominic J B Hunter, Tristan I Croll, Leonie Flueckiger, Jeffrey D Nanson, Md Habibur Rahaman, Andrew Aquila, Mark S Hunter, Mengning Liang, Chun Hong Yoon, Jingjing Zhao, Nadia A Zatsepin, Brian Abbey, Emma Sierecki, Yann Gambin, Katryn J Stacey, Connie Darmanin, Bostjan Kobe, Hongyi Xu, Thomas Ve
Jun 11, 2021
MyD88 and MAL are Toll-like receptor (TLR) adaptors that signal to induce pro-inflammatory cytokine production. We previously observed that the TIR domain of MAL (MALTIR) forms filaments in vitro and induces formation...
Humans Membrane Glycoproteins Receptors Interleukin-1 Recombinant Proteins Crystallography Signal Transduction Dimerization Mutation Models Molecular Toll-Like Receptor 4 Myeloid Differentiation Factor 88 Molecular Dynamics Simulation HEK293 Cells Protein Conformation alpha-Helical Protein Domains Protein Conformation beta-Strand
Published by: Nature Communications
Purification of Recombinant α-synuclein
Amberley D Stephens, Dijana Matak-Vinkovic, Ana Fernandez-Villegas, Gabriele S Kaminski Schierle
Nov 23, 2020
The initial state of the intrinsically disordered protein α-synuclein (aSyn), e.g., the presence of oligomers and degradation products, or the presence of contaminants and adducts can greatly influence the aggregation kinetics...
Cell Line Cell Survival Chemical Precipitation Chromatography Gel Chromatography Ion Exchange Chromatography Liquid Escherichia coli Humans Intrinsically Disordered Proteins Microscopy Electron Transmission Protein Aggregates Protein Conformation Protein Conformation beta-Strand Recombinant Proteins Spectrometry Mass Electrospray Ionization ALPHA-SYNUCLEIN
Stabilization and Characterization of Cytotoxic Aβ40 Oligomers Isolated from an Aggregation Reaction in the Presence of Zinc Ions.
Benedetta Mannini, Johnny Habchi, Sean Chia, Francesco S Ruggeri, Michele Perni, Tuomas PJ Knowles, Christopher M Dobson, Michele Vendruscolo
Nov 01, 2018
Alzheimer’s disease OC-positive aggregates Protein oligomer aggregates Amyloid antiparallel oligomer metal ions Alzheimer Disease Amyloid beta-Peptides Animals Caenorhabditis elegans Cell Line Tumor Cell Survival Humans In Vitro Techniques Movement Neuroblastoma Neurons Peptide Fragments Polymers Protein Aggregates protein aggregation Pathological Protein Conformation beta-Strand Zinc
mCSM-PPI2
Benchmarking Binding Sites Crystallography X-Ray Datasets as Topic Humans Internet Machine Learning Mutation Missense Protein Binding Protein Conformation alpha-Helical Protein Conformation beta-Strand Protein Interaction Domains and Motifs Protein Interaction Mapping Proteins Software Thermodynamics
Defining α-synuclein species responsible for Parkinson's disease phenotypes in mice.
Jessica M Froula, Marta Castellana-Cruz, Nadia M Anabtawi, José D Camino, Serene W Chen, Drake R Thrasher, Jennifer Freire, Allen A Yazdi, Sheila Fleming, Christopher M Dobson, Janet R Kumita, Nunilo Cremades, Laura A Volpicelli-Daley
May 31, 2019
Parkinson's disease (PD) is a neurodegenerative disorder characterized by fibrillar neuronal inclusions composed of aggregated α-synuclein (α-syn). These inclusions are associated with behavioral and pathological PD phenotypes....
LEWY BODY Parkinson's Disease Amyloid Cytotoxicity fibril motor-behavior defect Neurodegenerative disease oligomer protein aggregation α-synuclein Amyloid Animals Behavior Animal Corpus Striatum Disease Models Animal Dopaminergic Neurons Male Mice Parkinson Disease Phenotype Protein Aggregates Protein Conformation beta-Strand ALPHA-SYNUCLEIN
Structure and mechanotransmission mechanism of the MacB ABC transporter superfamily.
MacB is an ABC transporter that collaborates with the MacA adaptor protein and TolC exit duct to drive efflux of antibiotics and enterotoxin STII out of the bacterial cell. Here we present the structure of ATP-bound MacB and...
ABC transporter X-ray crystallography tripartite efflux pump ATP-Binding Cassette Transporters Adenosine Triphosphate Aggregatibacter actinomycetemcomitans Bacterial Outer Membrane Proteins Binding Sites Biological Transport Cell Cycle Proteins Crystallography X-Ray Cystic Fibrosis Transmembrane Conductance Regulator Escherichia coli Escherichia coli Proteins Gene Expression Models Molecular Protein Binding Protein Conformation alpha-Helical Protein Conformation beta-Strand Protein Interaction Domains and Motifs Protein Multimerization Recombinant Proteins Substrate Specificity
mCSM–NA
Binding Sites DNA DNA-Binding Proteins Humans Internet Machine Learning Models Molecular Models Statistical Mutation Missense Protein Binding Protein Conformation alpha-Helical Protein Conformation beta-Strand Protein Interaction Domains and Motifs Protein Stability RNA-Binding Proteins Reverse Genetics Software Thermodynamics
Investigating the Effect of Chain Connectivity on the Folding of a Beta-Sheet Protein On and Off the Ribosome.
Andrew P Marsden, Jeffrey J Hollins, Charles O'Neill, Pavel Ryzhov, Sally Higson, Carolina ATF Mendonça, Tristan O Kwan, Lee Gyan Kwa, Annette Steward, Jane Clarke
Dec 11, 2018
Determining the relationship between protein folding pathways on and off the ribosome remains an important area of investigation in biology. Studies on isolated domains have shown that alteration of the separation of residues in...
Heat treatment of thioredoxin fusions increases the purity of α-helical transmembrane protein constructs.
Membrane proteins play key roles in cellular signaling and transport, represent the majority of drug targets, and are implicated in many diseases. Their relevance renders them important subjects for structural, biophysical, and...
Heat treatment Membrane Proteins Protein purification thioredoxin ATP Synthetase Complexes Bacterial Proteins Cloning Molecular Cystic Fibrosis Transmembrane Conductance Regulator Escherichia coli Fusobacteria Gene Expression Genetic Vectors Hot Temperature Humans Models Molecular Protein Conformation alpha-Helical Protein Conformation beta-Strand Protein Interaction Domains and Motifs Protein Subunits Recombinant Fusion Proteins Solubility Thioredoxins
The Knotted Protein UCH-L1 Exhibits Partially Unfolded Forms under Native Conditions that Share Common Structural Features with Its Kinetic Folding Intermediates.
Shih-Chi Lou, Svava Wetzel, Hongyu Zhang, Elizabeth W Crone, Yun-Tzai Lee, Sophie E Jackson, Shang-Te Danny Hsu
Apr 27, 2016
folding intermediate folding pathway knotted protein partially unfolded form ubiquitin C-terminal hydrolase Deuterium Deuterium Exchange Measurement Humans Hydrogen Hydrogen-Ion Concentration Kinetics Magnetic Resonance Spectroscopy Protein Conformation alpha-Helical Protein Conformation beta-Strand Protein Denaturation Protein Folding Ubiquitin Thiolesterase
Cryo-EM structural analysis of FADD
Joanna L Fox, Michelle A Hughes, Xin Meng, Nikola A Sarnowska, Ian R Powley, Rebekah Jukes-Jones, David Dinsdale, Timothy J Ragan, Louise Fairall, John WR Schwabe, Nobuhiro Morone, Kelvin Cain, Marion MacFarlane
Mar 05, 2021
Regulated cell death is essential in development and cellular homeostasis. Multi-protein platforms, including the Death-Inducing Signaling Complex (DISC), co-ordinate cell fate via a core FADD:Caspase-8 complex and its...
CASP8 and FADD-Like Apoptosis Regulating Protein Caspase 8 Catalytic Domain Cloning Molecular Cryoelectron Microscopy Death Domain Receptor Signaling Adaptor Proteins Escherichia coli Fas-Associated Death Domain Protein Gene Expression Genetic Vectors HEK293 Cells Humans Models Molecular Protein Binding Protein Conformation alpha-Helical Protein Conformation beta-Strand Protein Interaction Domains and Motifs Protein Isoforms Protein Multimerization Receptor-Interacting Protein Serine-Threonine Kinases Recombinant Proteins Regulated Cell Death Tumor Necrosis Factor-alpha
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