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1. Full Text ATP binding and hydrolysis disrupt the high-affinity interaction between the heme ABC transporter HmuUV and its cognate substrate-binding protein
by Qasem-Abdullah, Hiba and Perach, Michal and Livnat-Levanon, Nurit and Lewinson, Oded
The Journal of biological chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 35, pp. 14617 - 14624
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Surface Plasmon Resonance | Hemeproteins - genetics | Heme - metabolism | Protein Multimerization | Bacterial Proteins - chemistry | Holoenzymes - chemistry | Recombinant Proteins | Cell Membrane - chemistry | ATP-Binding Cassette Transporters - chemistry | Holoenzymes - metabolism | ATP-Binding Cassette Transporters - genetics | Heme - chemistry | Adenosine Triphosphate - metabolism | Hemeproteins - chemistry | Apoenzymes - metabolism | ATP-Binding Cassette Transporters - metabolism | Carrier Proteins - chemistry | Receptors, Cell Surface - chemistry | Cell Membrane - metabolism | Protein Interaction Domains and Motifs | Dimerization | Immobilized Proteins - chemistry | Yersinia pestis - metabolism | Hemeproteins - metabolism | Immobilized Proteins - genetics | Bacterial Proteins - genetics | Models, Molecular | Receptors, Cell Surface - metabolism | Hydrolysis | Carrier Proteins - genetics | Carrier Proteins - metabolism | Apoenzymes - genetics | Immobilized Proteins - metabolism | Apoenzymes - chemistry | Bacterial Proteins - metabolism | Holoenzymes - genetics | Molecular Docking Simulation | Kinetics | Adenosine Triphosphate - chemistry | Receptors, Cell Surface - genetics | Index Medicus | Membrane Biology | ATPase | membrane protein | protein-protein interaction | surface plasmon resonance (SPR) | ABC transporter | ATP
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2. Full Text Serum FHR1 binding to necrotic-type cells activates monocytic inflammasome and marks necrotic sites in vasculopathies
by Irmscher, Sarah and Brix, Silke R and Zipfel, Svante L. H and Halder, Luke D and Mutlutuerk, Sibel and Wulf, Sonia and Girdauskas, Evaldas and Reichenspurner, Hermann and Stahl, Rolf A. K and Jungnickel, Berit and Wiech, Thorsten and Zipfel, Peter F and Skerka, Christine
Nature communications, ISSN 2041-1723, 07/2019, Volume 10, Issue 1, pp. 2961 - 14
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Malondialdehyde - metabolism | Inflammation - pathology | Inflammasomes - metabolism | Vascular Diseases - pathology | Human Umbilical Vein Endothelial Cells - metabolism | Receptors, G-Protein-Coupled - metabolism | Serum - metabolism | NLR Family, Pyrin Domain-Containing 3 Protein - metabolism | Humans | Type C Phospholipases - metabolism | Monocytes - metabolism | Complement System Proteins - metabolism | Necrosis | Complement C3b Inactivator Proteins - metabolism | Inflammation - metabolism | C-Reactive Protein - metabolism | Interleukin-1beta - metabolism | Models, Biological | Immobilized Proteins - metabolism | Inflammation Mediators - metabolism | Monocytes - pathology | Protein Binding | Lipoproteins, LDL - metabolism | Vascular Diseases - metabolism | G protein-coupled receptors | Target recognition | Medical treatment | Antibodies | Inflammation | Tumor necrosis factor-α | IL-1β | Blood | Inflammatory diseases | Phospholipase C | Interleukin 18 | Diseases | Proteins | Interleukin 6 | Phospholipase | Monocytes | Complement factor H | Vasculitis | Arteriosclerosis | N-Terminus | Atherosclerosis | Plaques | Index Medicus
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3. Full Text The soluble periplasmic domains of Escherichia coli cell division proteins FtsQ/FtsB/FtsL form a trimeric complex with submicromolar affinity
by Glas, Marjolein and Bart Van Den Berg Van Saparoea, H and McLaughlin, Stephen H and Roseboom, Winfried and Liu, Fan and Koningstein, Gregory M and Fish, Alexander and Den Blaauwen, Tanneke and Heck, Albert J R and De Jong, Luitzen and Bitter, Wilbert and De Esch, Iwan J P and Luirink, Joen
The Journal of biological chemistry, ISSN 0021-9258, 08/2015, Volume 290, Issue 35, pp. 21498 - 21509
Molecular Biology | Biochemistry | Cell Biology | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Molecular Weight | Molecular Sequence Data | Structure-Activity Relationship | Ultracentrifugation | Escherichia coli - cytology | Protein Subunits - metabolism | Cell Cycle Proteins - chemistry | Multiprotein Complexes - metabolism | Peptides - metabolism | Periplasm - metabolism | Cell Division | Light | Mass Spectrometry | Escherichia coli - metabolism | Membrane Proteins - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Peptides - chemistry | Cell Cycle Proteins - metabolism | Solubility | Models, Molecular | Escherichia coli Proteins - metabolism | Cross-Linking Reagents - metabolism | Membrane Proteins - chemistry | Biosensing Techniques | Immobilized Proteins - metabolism | Protein Binding | Protein Subunits - chemistry | Escherichia coli Proteins - chemistry | Index Medicus | analytical ultracentrifugation | Microbiology | Escherichia coli (E. coli) | cell division | protein-protein interaction | surface plasmon resonance (SPR) | protein cross-linking | mass spectrometry (MS)
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4. Full Text Endoplasmic reticulum-resident protein 57 (ERp57) oxidatively inactivates human transglutaminase 2
by Yi, Michael C and Melkonian, Arek V and Ousey, James A and Khosla, Chaitan
The Journal of biological chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 8, pp. 2640 - 2649
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Enzymes, Immobilized - metabolism | Oxidants - pharmacology | Human Umbilical Vein Endothelial Cells - metabolism | Membrane Glycoproteins - metabolism | Glutathione - metabolism | Protein Disulfide-Isomerases - metabolism | GTP-Binding Proteins - antagonists & inhibitors | Humans | Membrane Glycoproteins - chemistry | Oxidants - metabolism | Extracellular Matrix - metabolism | Transglutaminases - genetics | Protein Disulfide-Isomerases - antagonists & inhibitors | Protein Transport - drug effects | GTP-Binding Proteins - genetics | Thioredoxins - genetics | Oxidoreductases Acting on Sulfur Group Donors - chemistry | Protein Processing, Post-Translational - drug effects | RNA Interference | Biocatalysis - drug effects | Human Umbilical Vein Endothelial Cells - cytology | Thioredoxins - metabolism | Peptide Fragments - genetics | Transglutaminases - antagonists & inhibitors | Transglutaminases - chemistry | Allosteric Regulation - drug effects | Oxidoreductases Acting on Sulfur Group Donors - metabolism | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | GTP-Binding Proteins - chemistry | Oxidation-Reduction | Extracellular Matrix - drug effects | Cells, Cultured | Hydrogen Peroxide - pharmacology | Recombinant Proteins - chemistry | Membrane Glycoproteins - genetics | Extracellular Matrix - enzymology | Peptide Fragments - chemistry | Protein Disulfide-Isomerases - genetics | Human Umbilical Vein Endothelial Cells - enzymology | Cystine - metabolism | Transglutaminases - metabolism | Oxidoreductases Acting on Sulfur Group Donors - genetics | Enzymes, Immobilized - antagonists & inhibitors | GTP-Binding Proteins - metabolism | Index Medicus | Editors' Picks | post-translational modification (PTM) | PDIA3 | transglutaminase | thioredoxin | disulfide | oxidation-reduction (redox) | ERp57 | redox switch | celiac disease | transglutaminase 2 | protein disulfide isomerase family A member 3
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5. Full Text Immobilizing affinity proteins to nitrocellulose: a toolbox for paper-based assay developers
by Holstein, Carly A and Holstein, Carly A and Chevalier, Aaron and Chevalier, Aaron and Bennett, Steven and Bennett, Steven and Anderson, Caitlin E and Anderson, Caitlin E and Keniston, Karen and Keniston, Karen and Olsen, Cathryn and Olsen, Cathryn and Li, Bing and Li, Bing and Bales, Brian and Bales, Brian and Moore, David R and Moore, David R and Fu, Elain and Fu, Elain and Baker, David and Baker, David and Yager, Paul and Yager, Paul
Analytical and bioanalytical chemistry, ISSN 1618-2642, 2/2016, Volume 408, Issue 5, pp. 1335 - 1346
Biochemistry, general | Protein immobilization | Protein engineering | Chemistry | Analytical Chemistry | Food Science | Characterization and Evaluation of Materials | Laboratory Medicine | Paper-based assays | Environmental Monitoring/Analysis | Nitrocellulose | Biochemistry & Molecular Biology | Physical Sciences | Life Sciences & Biomedicine | Biochemical Research Methods | Chemistry, Analytical | Science & Technology | Recombinant Proteins - metabolism | Streptavidin - chemistry | Immobilized Proteins - chemistry | Antibodies - metabolism | Antibodies - chemistry | Bacterial Proteins - chemistry | Recombinant Proteins - chemistry | Collodion - chemistry | Collodion - metabolism | Carrier Proteins - metabolism | Streptavidin - metabolism | Immobilized Proteins - metabolism | Bacterial Proteins - metabolism | Carrier Proteins - chemistry | Paper | Chromatography, Affinity - methods | Physiological aspects | Biological assay | Methods | Cellulose | Index Medicus | Anchors | Proteins | Cellulose esters | Tools | Affinity | Binders | Recombinant
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6. Full Text Receptor oligomerization and beyond: A case study in bone morphogenetic proteins
by Heinecke, Kai and Seher, Axel and Schmitz, Werner and Mueller, Thomas D and Sebald, Walter and Nickel, Joachim
BMC biology, ISSN 1741-7007, 09/2009, Volume 7, Issue 1, pp. 59 - 59
Biology | Life Sciences & Biomedicine - Other Topics | Life Sciences & Biomedicine | Science & Technology | Detergents - chemistry | Protein Interaction Domains and Motifs - physiology | Bone Morphogenetic Protein Receptors - genetics | Humans | Bacterial Proteins - chemistry | Cercopithecus aethiops | Activins - metabolism | Recombinant Fusion Proteins - metabolism | Activin Receptors - genetics | Bone Morphogenetic Proteins - isolation & purification | Activin Receptors - isolation & purification | Bone Morphogenetic Proteins - metabolism | Growth Differentiation Factor 5 - genetics | Transfection | Growth Differentiation Factor 5 - isolation & purification | Cholic Acids - chemistry | Binding Sites | Bone Morphogenetic Proteins - genetics | Growth Differentiation Factor 5 - chemistry | Bone Morphogenetic Protein Receptors - isolation & purification | Immobilized Proteins - chemistry | Bacterial Proteins - genetics | Bone Morphogenetic Protein Receptors - metabolism | Mutant Proteins - metabolism | Recombinant Fusion Proteins - chemistry | Activin Receptors - chemistry | Activin Receptors - metabolism | Animals | Models, Biological | Mutant Proteins - chemistry | Protein Isoforms | Activins - isolation & purification | Biosensing Techniques | Immobilized Proteins - metabolism | Cell Line, Tumor | Protein Binding | Bacterial Proteins - metabolism | Growth Differentiation Factor 5 - metabolism | Ligands | Activins - genetics | Bone Morphogenetic Proteins - chemistry | Kinetics | Bacterial Proteins - isolation & purification | COS Cells | Bone Morphogenetic Protein Receptors - chemistry | Activins - chemistry | Physiological aspects | Bone morphogenetic proteins | Cell receptors | Cellular signal transduction | Research | Transforming growth factors | Index Medicus
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7. Full Text Mechanism of pathogen recognition by human dectin-2
by Feinberg, Hadar and Jégouzo, Sabine A. F and Rex, Maximus J and Drickamer, Kurt and Weis, William I and Taylor, Maureen E and SLAC National Accelerator Lab., Menlo Park, CA (United States)
The Journal of biological chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 32, pp. 13402 - 13414
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Epitopes - metabolism | Disaccharides - metabolism | Humans | Crystallography, X-Ray | Phylogeny | Disaccharides - chemistry | Lectins, C-Type - genetics | Lectins, C-Type - chemistry | Lectins, C-Type - metabolism | Mannose - metabolism | Oligosaccharides - chemistry | Escherichia coli - metabolism | Polysaccharides - chemistry | Protein Interaction Domains and Motifs | Inclusion Bodies - metabolism | Binding Sites | Peptide Fragments - genetics | Mannose - chemistry | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Immobilized Proteins - chemistry | Immobilized Proteins - genetics | Escherichia coli - immunology | Models, Molecular | Recombinant Proteins - chemistry | Oligosaccharides - metabolism | Immunity, Innate | Polysaccharides - metabolism | Peptide Fragments - chemistry | Immobilized Proteins - metabolism | Ligands | Protein Conformation | Epitopes - chemistry | Kinetics | Carbohydrate Conformation | Index Medicus | BASIC BIOLOGICAL SCIENCES | protein structure | lectin | CLEC6A | carbohydrate-binding protein | macrophage | Glycobiology and Extracellular Matrices | glycobiology
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8. Full Text Proteins in Mesoporous Silicates
by Hudson, Sarah and Cooney, Jakki and Magner, Edmond
Angewandte Chemie (International ed.), ISSN 1433-7851, 10/2008, Volume 47, Issue 45, pp. 8582 - 8594
functionalization | silicates | mesoporous materials | proteins | biocatalysis | Proteins | Biocatalysis | Mesoporous materials | Silicates | Functionalization | Physical Sciences | Chemistry | Chemistry, Multidisciplinary | Science & Technology | Enzymes - chemistry | Enzymes, Immobilized - chemistry | Enzymes, Immobilized - metabolism | Silicates - chemistry | Particle Size | Proteins - metabolism | Silicates - metabolism | Adsorption | Surface Properties | Porosity | Proteins - chemistry | Enzymes - metabolism | Index Medicus
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