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1. Full Text Proteins in Mesoporous Silicates
by Hudson, Sarah and Cooney, Jakki and Magner, Edmond
Angewandte Chemie International Edition, ISSN 1433-7851, 10/2008, Volume 47, Issue 45, pp. 8582 - 8594
Mesoporous silicates (MPS) have an ordered pore structure with dimensions comparable to many biological molecules. They have been extensively explored as... 
functionalization | silicates | mesoporous materials | proteins | biocatalysis | Proteins | Biocatalysis | Mesoporous materials | Silicates | Functionalization | PENICILLIN-G ACYLASE | CARBON MOLECULAR-SIEVES | ENZYME IMMOBILIZATION | CHEMISTRY, MULTIDISCIPLINARY | CYTOCHROME-C | ORGANIC-SOLVENTS | NANOPOROUS SUPPORT | ALUMINUM INCORPORATION | CATALYTIC-ACTIVITY | FUNCTIONALIZED MONOLAYERS | BOVINE SERUM-ALBUMIN | Enzymes - chemistry | Enzymes, Immobilized - chemistry | Enzymes, Immobilized - metabolism | Silicates - chemistry | Particle Size | Proteins - metabolism | Silicates - metabolism | Adsorption | Surface Properties | Porosity | Proteins - chemistry | Enzymes - metabolism
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2. 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
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 35, pp. 14617 - 14624
Using the energy of ATP hydrolysis, ABC transporters catalyze the trans-membrane transport of molecules. In bacteria, these transporters partner with a... 
ANTHRACIS VIRULENCE DETERMINANT | MALTOSE TRANSPORT | BTUCD-F | MECHANISM | YERSINIA-PESTIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CASSETTE TRANSPORTER | CRYSTAL-STRUCTURES | MULTIDRUG-RESISTANCE | HISTIDINE PERMEASE | 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 | Membrane Biology | ATPase | membrane protein | protein-protein interaction | surface plasmon resonance (SPR) | ABC transporter | ATP
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3. Full Text Immobilizing affinity proteins to nitrocellulose: a toolbox for paper-based assay developers
by Holstein, Carly A and Chevalier, Aaron and Bennett, Steven and Anderson, Caitlin E and Keniston, Karen and Olsen, Cathryn and Li, Bing and Bales, Brian and Moore, David R and Fu, Elain and Baker, David and Yager, Paul
Analytical and Bioanalytical Chemistry, ISSN 1618-2642, 2/2016, Volume 408, Issue 5, pp. 1335 - 1346
To enable enhanced paper-based diagnostics with improved detection capabilities, new methods are needed to immobilize affinity reagents to porous substrates,... 
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 | CHEMISTRY, ANALYTICAL | MECHANISM | BIOCHEMICAL RESEARCH METHODS | BIOASSAYS | BIOCHIPS | STRATEGIES | DIAGNOSTIC DEVICES | POINT | CELLULOSE | 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 | Anchors | Proteins | Cellulose esters | Tools | Affinity | Binders | Recombinant
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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
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 8, pp. 2640 - 2649
Transglutaminase 2 (TG2) is a ubiquitously expressed, intracellular as well as extracellular protein with multiple modes of post-translational regulation,... 
SELECTIVE-INHIBITION | HUMAN THIOREDOXIN-1 | ACTIVE-SITE | THROMBUS FORMATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ISOMERASE | THIOL-DISULFIDE EXCHANGE | EXTRACELLULAR-MATRIX | QUIESCIN-SULFHYDRYL OXIDASE | TISSUE TRANSGLUTAMINASE | CELIAC-DISEASE | 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 | 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 The cancer glycocalyx mechanically primes integrin-mediated growth and survival
by Paszek, Matthew J and Dufort, Christopher C and Rossier, Olivier and Bainer, Russell and Mouw, Janna K and Godula, Kamil and Hudak, Jason E and Lakins, Jonathon N and Wijekoon, Amanda C and Cassereau, Luke and Rubashkin, Matthew G and Magbanua, Mark J and Thorn, Kurt S and Davidson, Michael W and Rugo, Hope S and Park, John W and Hammer, Daniel A and Giannone, Grégory and Bertozzi, Carolyn R and Weaver, Valerie M
Nature, ISSN 0028-0836, 2014, Volume 511, Issue 7509, pp. 319 - 325
Malignartcy is associated with altered expression of glycans and glycoprotems that contribute the cellular glycocalyx. We constructed a glycoprotein expression... 
GLYCOPOLYMERS | MULTIDISCIPLINARY SCIENCES | X-RAY | DYNAMICS | RECEPTOR | HYALURONAN | TENSION | CELL-ADHESION | NANOSCALE | MICROSCOPY | SCATTERING | Neoplasms - metabolism | Cell Proliferation | Humans | Glycoproteins - metabolism | Integrins - chemistry | Receptors, Cell Surface | Molecular Targeted Therapy | Breast - metabolism | Integrins - metabolism | Fibroblasts | Glycocalyx - chemistry | Breast - pathology | Mucin-1 - metabolism | Immobilized Proteins - chemistry | Breast - cytology | Cell Survival | Animals | Neoplasm Metastasis - pathology | Immobilized Proteins - metabolism | Neoplastic Cells, Circulating | Cell Line, Tumor | Protein Binding | Mice | Neoplasms - pathology | Glycocalyx - metabolism | Physiological aspects | Glycocalyx | Glycoproteins | Properties | Cancer cells | Integrins
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6. Full Text Control of the Graphene–Protein Interface Is Required To Preserve Adsorbed Protein Function
by Alava, Thomas and Mann, Jason A and Théodore, Cécile and Benitez, Jaime J and Dichtel, William R and Parpia, Jeevak M and Craighead, Harold G
Analytical Chemistry, ISSN 0003-2700, 03/2013, Volume 85, Issue 5, pp. 2754 - 2759
Graphene’s suite of useful properties makes it of interest for use in biosensors. However, graphene interacts strongly with hydrophobic components of... 
CONCANAVALIN-A | CHEMISTRY, ANALYTICAL | RESONANCE ENERGY-TRANSFER | BIOSENSOR | ADSORPTION | SOLID-SURFACES | Adsorption | Bacillus subtilis - cytology | Concanavalin A - chemistry | Plant Proteins - chemistry | Cell Wall - metabolism | Teichoic Acids - metabolism | Canavalia - chemistry | Cells, Immobilized - metabolism | Lipopolysaccharides - metabolism | Concanavalin A - metabolism | Plant Proteins - metabolism | Graphite - chemistry | Usage | Graphene | Analysis | Quartz crystals | Chemical properties | Electron configuration | Biosensors | Protein binding
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7. Full Text C3 glomerulopathy-associated CFHR1 mutation alters FHR oligomerization and complement regulation
by Tortajada, Agustín and Yébenes, Hugo and Abarrategui-Garrido, Cynthia and Anter, Jaouad and García-Fernández, Jesús M and Martínez-Barricarte, Rubén and Alba-Domínguez, María and Malik, Talat H and Bedoya, Rafael and Pérez, Rocío Cabrera and Trascasa, Margarita López and Pickering, Matthew C and Harris, Claire L and Sánchez-Corral, Pilar and Llorca, Oscar and De Córdoba, Santiago Rodríguez
Journal of Clinical Investigation, ISSN 0021-9738, 06/2013, Volume 123, Issue 6, pp. 2434 - 2446
C3 glomerulopathies (C3G) are a group of severe renal diseases with distinct patterns of glomerular inflammation and C3 deposition caused by complement... 
ECULIZUMAB | GLOMERULONEPHRITIS | MEDICINE, RESEARCH & EXPERIMENTAL | PROVIDES INSIGHTS | HEMOLYTIC-UREMIC SYNDROME | MPGN-II | MACULAR DEGENERATION | HEPARIN | H-RELATED PROTEINS | DENSE-DEPOSIT DISEASE | REVEALS | Gene Duplication | Hemolysis | Immobilized Proteins - chemistry | Kidney - pathology | Complement C3 - metabolism | Humans | Middle Aged | Protein Multimerization | Complement C3b Inactivator Proteins - genetics | Complement C3b Inactivator Proteins - chemistry | Male | Sequence Analysis, DNA | Kidney Diseases - genetics | Complement System Proteins - metabolism | Complement C3b Inactivator Proteins - metabolism | Complement C3 - chemistry | Pedigree | Immobilized Proteins - metabolism | Protein Structure, Quaternary | Complement System Proteins - isolation & purification | Protein Binding | Female | Mutagenesis, Insertional | Child | Glomerulonephritis | Complement factor H | Gene mutations | Physiological aspects | Causes of | Genetic aspects | Research | Proteins | Competition | Plasma | Carbohydrates | Mutation | Crystal structure
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8. Full Text HaloTag: A Novel Protein Labeling Technology for Cell Imaging and Protein Analysis
by Los, Georgyi V and Encell, Lance P and McDougall, Mark G and Hartzell, Danette D and Karassina, Natasha and Zimprich, Chad and Wood, Monika G and Learish, Randy and Ohana, Rachel Friedman and Urh, Marjeta and Simpson, Dan and Mendez, Jacqui and Zimmerman, Kris and Otto, Paul and Vidugiris, Gediminas and Zhu, Ji and Darzins, Aldis and Klaubert, Dieter H and Bulleit, Robert F and Wood, Keith V
ACS Chemical Biology, ISSN 1554-8929, 06/2008, Volume 3, Issue 6, pp. 373 - 382
We have designed a modular protein tagging system that allows different functionalities to be linked onto a single genetic fusion, either in solution, in... 
Fluorescent Dyes - chemistry | Hydrocarbons, Chlorinated - chemistry | Humans | Enzymes, Immobilized | NF-kappa B - metabolism | Proteins - analysis | DNA - metabolism | Luminescent Measurements - methods | DNA - chemistry | Animals | Proteins - metabolism | DNA - analysis | Sensitivity and Specificity | Staining and Labeling | Cells - metabolism | Luminescent Proteins - chemistry | Biosensing Techniques - methods | Proteins - chemistry | Binding Sites | Cells - cytology | NF-kappa B - analysis
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9. Full Text Video imaging of walking myosin v by high-speed atomic force microscopy
by Kodera, Noriyuki and Yamamoto, Daisuke and Ishikawa, Ryoki and Ando, Toshio
Nature, ISSN 0028-0836, 11/2010, Volume 468, Issue 7320, pp. 72 - 76
The dynamic behaviour of myosin V molecules translocating along actin filaments has been mainly studied by optical microscopy. The processive hand-over-hand... 
HAND-OVER-HAND | MECHANISM | ACTIN | CONTRACTION | MULTIDISCIPLINARY SCIENCES | MOVEMENT | COORDINATION | PROCESSIVE MYOSIN | BACTERIORHODOPSIN | POWER STROKE | ADP | Myosin Type V - chemistry | Biotinylation | Immobilized Proteins - chemistry | Movement | Myosin Type V - metabolism | Myosin Type V - ultrastructure | Protein Unfolding | Actins - metabolism | Actins - ultrastructure | Immobilized Proteins - ultrastructure | Animals | Time Factors | Adenosine Triphosphate - metabolism | Chickens | Immobilized Proteins - metabolism | Actins - chemistry | Video Recording | Protein Conformation | Microscopy, Atomic Force - methods | Adenosine Diphosphate - metabolism | Physiological aspects | Atomic force microscopy | Usage | Research | Structure | Myosin | Proteins | Motion pictures | Lipids | Behavior | Dynamic structural analysis | Walking | Molecular structure | Dynamics | High speed | Biomolecules
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10. Full Text One-Pot Synthesis of Protein-Embedded Metal–Organic Frameworks with Enhanced Biological Activities
by Lyu, Fengjiao and Zhang, Yifei and Zare, Richard N and Ge, Jun and Liu, Zheng
Nano Letters, ISSN 1530-6984, 10/2014, Volume 14, Issue 10, pp. 5761 - 5765
Protein molecules were directly embedded in metal–organic frameworks (MOFs) by a coprecipitation method. The protein molecules majorly embedded on the surface... 
nanomaterials | Enzyme | biocatalysis | metal-organic framework | STORAGE | CAPACITY | PHYSICS, CONDENSED MATTER | COMPLEX | PHYSICS, APPLIED | ENZYME-ACTIVITY | STABILITY | MATERIALS SCIENCE, MULTIDISCIPLINARY | CHEMISTRY, PHYSICAL | NANOSCIENCE & NANOTECHNOLOGY | CHEMISTRY, MULTIDISCIPLINARY | IMMOBILIZATION | CYTOCHROME-C | FLUORESCENCE | HYDROGEN-PEROXIDE | SINGLE-ENZYME | Cytochromes c - chemistry | Immobilized Proteins - chemistry | Biosensing Techniques | Immobilized Proteins - metabolism | Peroxides - analysis | Models, Molecular | Peroxides - metabolism | Organometallic Compounds - chemistry | Proteins | Organic peroxides | Surface chemistry | Nanomaterials | Nanostructure | Explosions | Biological | Metal-organic frameworks | Coprecipitation
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11. 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
Journal of Biological Chemistry, ISSN 0021-9258, 08/2015, Volume 290, Issue 35, pp. 21498 - 21509
Cell division in Escherichia coli involves a set of essential proteins that assembles at midcell to form the so-called divisome. The divisome regulates the... 
BIOCHEMISTRY & MOLECULAR BIOLOGY | Escherichia coli (E | coli | cell division | surface plasmon resonance (SPR) | DIVIB | MASS-SPECTROMETRY | DIVISOME | analytical ultracentrifugation | SEPTAL LOCALIZATION | OF-FLIGHT INSTRUMENT | SEQUENCE DATABASES | BACILLUS-SUBTILIS | FTSQ PROTEIN | SIGNAL RECOGNITION PARTICLE | protein-protein interaction | MEMBRANE-PROTEINS | protein cross-linking | mass spectrometry (MS) | 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 | Microbiology | Escherichia coli (E. coli)
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12. Full Text Acceleration of the sliding movement of actin filaments with the use of a non-motile mutant myosin in in vitro motility assays driven by skeletal muscle heavy meromyosin
by Iwase, Kohei and Tanaka, Masateru and Hirose, Keiko and Uyeda, Taro Q. P and Honda, Hajime
PLoS ONE, ISSN 1932-6203, 07/2017, Volume 12, Issue 7, p. e0181171
We examined the movement of an actin filament sliding on a mixture of normal and genetically modified myosin molecules that were attached to a glass surface.... 
REACTIVE THIOL REGION | F-ACTIN | INHIBITION | FORCE GENERATION | MULTIDISCIPLINARY SCIENCES | MOTOR DOMAIN | SURFACE | ACTOMYOSIN | FIXED H-MEROMYOSIN | ATP | G680V | Actins - metabolism | Multiprotein Complexes - genetics | Muscle, Skeletal - metabolism | Protozoan Proteins - genetics | Molecular Motor Proteins - genetics | Recombinant Fusion Proteins - metabolism | Multiprotein Complexes - metabolism | Movement - physiology | Protozoan Proteins - metabolism | Myosin Type II - metabolism | Actins - chemistry | Molecular Motor Proteins - metabolism | Protozoan Proteins - chemistry | Myosin Type II - genetics | Microscopy, Electron, Transmission | Rabbits | Immobilized Proteins - chemistry | Myosin Subfragments - metabolism | Mutant Proteins - genetics | Mutant Proteins - metabolism | Myosin Subfragments - chemistry | Recombinant Fusion Proteins - chemistry | Molecular Motor Proteins - chemistry | Multiprotein Complexes - chemistry | Animals | Mutant Proteins - chemistry | Immobilized Proteins - metabolism | Dictyostelium - genetics | Recombinant Fusion Proteins - genetics | Dictyostelium - metabolism | In Vitro Techniques | Myosin Type II - chemistry | Dictyostelium | Actin | Analysis | Myosin | Muscles | Research | Health aspects | Bioengineering | Biomedical research | Motility | Glass | Sliding | Biochemistry | Copolymerization | Motor task performance | Assaying | ADP | Velocity | Skeletal muscle | Proteins | Musculoskeletal system | Chemistry | Hypotheses | Filaments | Mutation | Fusion protein | Acceleration | In vitro methods and tests | Genetic modification
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13. Full Text Immobilization of lipases on hydrophobic supports involves the open form of the enzyme
by Manoel, Evelin A and dos Santos, José C.S and Freire, Denise M.G and Rueda, Nazzoly and Fernandez-Lafuente, Roberto
Enzyme and Microbial Technology, ISSN 0141-0229, 04/2015, Volume 71, pp. 53 - 57
The lipases from and have been immobilized on octyl and cyanogen bromide (CNBr) agarose beads. The immobilization on octyl-agarose is slowed with increasing... 
Octyl-agarose | Interfacial activation | Detergents | Ionic strength | Irreversible inhibition | Lipase immobilization | BIOTECHNOLOGY | CELLS | COMPLEX | CRYSTAL-STRUCTURE | PERFORMANCE | MICROBIAL LIPASES | CATALYTIC-PROPERTIES | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PURIFICATION | Fungal Proteins - chemistry | Bacterial Proteins - antagonists & inhibitors | Enzymes, Immobilized - chemistry | Enzymes, Immobilized - metabolism | Sepharose - analogs & derivatives | Bacterial Proteins - chemistry | Ascomycota - enzymology | Fungal Proteins - antagonists & inhibitors | Lipase - metabolism | Lipase - chemistry | Osmolar Concentration | Lipase - antagonists & inhibitors | Hydrophobic and Hydrophilic Interactions | Bacterial Proteins - metabolism | Burkholderia cepacia - enzymology | Enzymes, Immobilized - antagonists & inhibitors | Protein Conformation | Kinetics | Cyanogen Bromide | Fungal Proteins - metabolism | Lipase | Catalysis
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