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1. Full Text DOTA-amide lanthanide tag for reliable generation of pseudocontact shifts in protein NMR spectra
by Graham, Bim and Loh, Choy Theng and Swarbrick, James David and Ung, Phuc and Shin, James and Yagi, Hiromasa and Jia, Xinying and Chhabra, Sandeep and Barlow, Nicholas and Pintacuda, Guido and Huber, Thomas and Otting, Gottfried
Bioconjugate Chemistry, ISSN 1043-1802, 10/2011, Volume 22, Issue 10, pp. 2118 - 2125
Structural studies of proteins and protein-ligand complexes by nuclear magnetic resonance (NMR) spectroscopy can be greatly enhanced by site-specific... 
DISTANCE | DESIGN | ACID | SERIES | LIGAND COMPLEXES | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | CHEMISTRY, ORGANIC | WATER EXCHANGE | CHEMISTRY, MULTIDISCIPLINARY | SPECTROSCOPY | BINDING TAG | MAGNETIC-SUSCEPTIBILITY | PARAMAGNETIC NMR | Repressor Proteins - chemistry | Humans | Ubiquitin - chemistry | Models, Molecular | Ubiquitin - genetics | Cysteine - chemistry | Escherichia coli - chemistry | Lanthanoid Series Elements - chemistry | Heterocyclic Compounds, 1-Ring - chemistry | Nuclear Magnetic Resonance, Biomolecular - methods | Protein Conformation | Mutation | Proteins - chemistry | Escherichia coli Proteins - chemistry | Ubiquitin | Analytical chemistry | Lanthanoid Series Elements | Cysteine | Escherichia coli | Repressor Proteins | Biochemistry, Molecular Biology | Heterocyclic Compounds, 1-Ring | Chemical Sciences | Proteins | Life Sciences | Escherichia coli Proteins | Nuclear Magnetic Resonance, Biomolecular | Biomolecules | Molecular biology
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2. Full Text Atomic structure of the APC/C and its mechanism of protein ubiquitination
by Chang, Leifu and Zhang, Ziguo and Yang, Jing and McLaughlin, Stephen H and Barford, David
Nature, ISSN 0028-0836, 06/2015, Volume 522, Issue 7557, pp. 450 - 454
The anaphase-promoting complex (APC/C) is a multimeric RING E3 ubiquitin ligase that controls chromosome segregation and mitotic exit. Its regulation by... 
E3 LIGASE | SPINDLE CHECKPOINT | ANAPHASE-PROMOTING COMPLEX | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | MITOTIC REGULATION | EM STRUCTURE DETERMINATION | CRYO-EM | ELECTRON-MICROSCOPY | CONJUGATING ENZYME | CHAIN ELONGATION | Phosphorylation | Ubiquitin - ultrastructure | Cadherins - metabolism | Humans | Apc11 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Ubiquitin - metabolism | Cell Cycle Proteins - ultrastructure | Substrate Specificity | Apc10 Subunit, Anaphase-Promoting Complex-Cyclosome - ultrastructure | Structure-Activity Relationship | Anaphase-Promoting Complex-Cyclosome - ultrastructure | Protein Subunits - metabolism | Ubiquitin-Conjugating Enzymes - chemistry | Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Cell Cycle Proteins - chemistry | Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Ubiquitination | Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Cadherins - chemistry | Cytoskeletal Proteins - metabolism | Lysine - metabolism | Anaphase-Promoting Complex-Cyclosome - chemistry | Cadherins - ultrastructure | Apc10 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Catalytic Domain | F-Box Proteins - metabolism | Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | F-Box Proteins - chemistry | Cell Cycle Proteins - metabolism | Ubiquitin - chemistry | Models, Molecular | Ubiquitin-Conjugating Enzymes - ultrastructure | Cytoskeletal Proteins - chemistry | Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Cryoelectron Microscopy | F-Box Proteins - ultrastructure | Ubiquitin-Conjugating Enzymes - metabolism | Protein Binding | Protein Subunits - chemistry | Apc10 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Anaphase-Promoting Complex-Cyclosome - metabolism | Apc11 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome - ultrastructure | Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome - ultrastructure | Ubiquitin | Physiological aspects | Structure | Ubiquitin-proteasome system | Ligases | Proteins | Peptides | Molecular structure | Cyclin-dependent kinases | Cell division | Kinases | Gene expression
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3. Full Text Jasmonate perception by inositol-phosphate-potentiated COI1-JAZ co-receptor
by Sheard, Laura B and Tan, Xu and Mao, Haibin and Withers, John and Ben-Nissan, Gili and Hinds, Thomas R and Kobayashi, Yuichi and Hsu, Fong-Fu and Sharon, Michal and Browse, John and He, Sheng Yang and Rizo, Josep and Howe, Gregg A and Zheng, Ning
Nature, ISSN 0028-0836, 11/2010, Volume 468, Issue 7322, pp. 400 - 407
Jasmonates are a family of plant hormones that regulate plant growth, development and responses to stress. The F-box protein CORONATINE INSENSITIVE 1 (COI1)... 
CORONATINE | ACID | MECHANISM | RECOGNITION | REPRESSION | MULTIDISCIPLINARY SCIENCES | ISOLEUCINE | BOX PROTEIN TIR1 | ARABIDOPSIS | REGULATED DEFENSE | AUXIN RECEPTOR | Indenes - metabolism | Amino Acids - chemistry | Molecular Sequence Data | Crystallography, X-Ray | Cyclopentanes - chemistry | Indenes - chemistry | Arabidopsis Proteins - metabolism | Plant Growth Regulators - chemistry | Amino Acids - metabolism | Isoleucine - chemistry | Inositol Phosphates - metabolism | Binding Sites | Repressor Proteins - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Arabidopsis - chemistry | Signal Transduction | F-Box Proteins - metabolism | F-Box Proteins - chemistry | Models, Molecular | Arabidopsis - metabolism | Isoleucine - metabolism | Oxylipins - metabolism | Peptide Fragments - chemistry | Arabidopsis Proteins - chemistry | Isoleucine - analogs & derivatives | Protein Binding | Cyclopentanes - metabolism | Plant Growth Regulators - metabolism | Oxylipins - chemistry | Ubiquitin | Inositol | Research | Jasmonates | Growth (Plants) | Proteins | Studies | Phosphates | Data collection | Mass spectrometry | Crystal structure
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4. Full Text Enzyme-Friendly, Mass Spectrometry-Compatible Surfactant for In-Solution Enzymatic Digestion of Proteins
by Yu, Ying-Qing and Gilar, Martin and Lee, Peter J and Bouvier, Edouard S. P and Gebler, John C
Analytical Chemistry, ISSN 0003-2700, 11/2003, Volume 75, Issue 21, pp. 6023 - 6028
Improved in-solution tryptic digestion of proteins in terms of speed and peptide coverage was achieved with the aid of a novel acid-labile anionic surfactant... 
MIXTURES | CHEMISTRY, ANALYTICAL | PEPTIDES | POLYACRYLAMIDE-GEL ELECTROPHORESIS | LIQUID-CHROMATOGRAPHY | SEPARATION | IDENTIFICATION | Myoglobin - metabolism | Chymotrypsin - metabolism | Ubiquitin - metabolism | Myoglobin - chemistry | Chromatography, High Pressure Liquid | Arginine - analogs & derivatives | Urea - chemistry | Neurotensin - metabolism | Ovalbumin - metabolism | Neurotensin - chemistry | Spectrometry, Mass, Electrospray Ionization | Membrane Proteins - metabolism | Molecular Structure | Ovalbumin - chemistry | Endopeptidases - metabolism | Angiotensin II - metabolism | Muramidase - chemistry | Solubility | Ubiquitin - chemistry | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods | Muramidase - metabolism | Trypsin - metabolism | Dioxolanes - chemistry | Arginine - chemistry | Angiotensin II - chemistry | Proteins - metabolism | Membrane Proteins - chemistry | Alkanesulfonates - chemistry | Sodium Dodecyl Sulfate - chemistry | Bacteriorhodopsins - metabolism | Hydrophobic and Hydrophilic Interactions | Surface-Active Agents - chemistry | Proteins - chemistry | Bacteriorhodopsins - chemistry | Arginine - metabolism | Hydrogen-Ion Concentration | Enzymes | Usage | Composition | Chemistry, Analytic | Solution (Chemistry) | Liquid chromatography | Research | Chemical compounds | Proteins | Trypsin | Surface active agents | Acids | Proteolysis | Analysis | Mass spectrometry
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5. Full Text Structural Insights into the Assembly and Function of the SAGA Deubiquitinating Module
by Nadine L. Samara and Ajit B. Datta and Christopher E. Berndsen and Xiangbin Zhang and Tingting Yao and Robert E. Cohen and Cynthia Wolberger
Science, ISSN 0036-8075, 5/2010, Volume 328, Issue 5981, pp. 1025 - 1029
SAGA is a transcriptional coactivator complex that is conserved across eukaryotes and performs multiple functions during transcriptional activation and... 
Proteins | Yeasts | Active sites | Ubiquitins | REPORTS | Histones | Atoms | Amino acids | Nucleosomes | Aldehydes | Zinc | COMPLEX | DOMAIN | UBP8 | CHROMATIN | NUCLEAR-PORE | UBIQUITIN | MULTIDISCIPLINARY SCIENCES | SUS1 | DEUBIQUITYLATION | MESSENGER-RNA EXPORT | ASSOCIATION | Transcription Factors - chemistry | Histone Acetyltransferases - chemistry | Nucleosomes - chemistry | Zinc - metabolism | Ubiquitin - metabolism | Crystallography, X-Ray | Ubiquitins - chemistry | Aldehydes - metabolism | Trans-Activators - chemistry | Zinc - chemistry | Endopeptidases - chemistry | Ubiquitination | Histone Acetyltransferases - metabolism | Ubiquitinated Proteins - metabolism | Ubiquitins - metabolism | Protein Structure, Tertiary | Endopeptidases - metabolism | Zinc Fingers | RNA-Binding Proteins - chemistry | Ubiquitin - chemistry | Models, Molecular | Nucleosomes - metabolism | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Transcription Factors - metabolism | Models, Biological | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Protein Conformation | Trans-Activators - metabolism | Histones - metabolism | RNA-Binding Proteins - metabolism | Aldehydes - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Ubiquitin | Physiological aspects | Transcription factors | Research | Eukaryotes | Biochemistry | Cellular biology | Proteases | Crystal structure | Modules | Mathematical models | Assembly | Elongation
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6. Full Text Mechanistic Insight into the Allosteric Activation of a Ubiquitin-Conjugating Enzyme by RING-Type Ubiquitin Ligases
by Engin Özkan and Hongtao Yu and Johann Deisenhofer and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2005, Volume 102, Issue 52, pp. 18890 - 18895
Ubiquitin-conjugating enzymes (E2s) collaborate with the ubiquitin-activating enzyme (E1) and ubiquitin ligases (E3s) to attach ubiquitin to target proteins.... 
Proteins | Enzymes | Biological Sciences | Active sites | Mutagenesis | rev genes | Ubiquitins | Kinetics | Causal covariation | Cyclins | E3 enzymes | E2 enzymes | Mechanism | ANAPHASE-PROMOTING COMPLEX | DETERMINANTS | MULTIDISCIPLINARY SCIENCES | PROTEIN LIGASE | IDENTIFICATION | APC11 | FAMILY | FINGER | PROTEASOME | DEGRADATION | mechanism | SUBUNIT | Ubiquitin-Activating Enzymes - chemistry | Humans | Ligases - chemistry | Cyclin B1 | Ubiquitin-Conjugating Enzymes - chemistry | Time Factors | Esters - chemistry | Escherichia coli - metabolism | Binding Sites | Protein Structure, Tertiary | Magnetic Resonance Spectroscopy | Peptides - chemistry | Ubiquitin - chemistry | Models, Molecular | Cysteine - chemistry | Ubiquitin-Protein Ligases - chemistry | Ubiquitin-Protein Ligase Complexes - chemistry | Allosteric Site | Protein Binding | Cyclin B - chemistry | Protein Conformation | Mutation | Cluster Analysis
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7. Full Text A chemical biology route to site-specific authentic protein modifications
by Yang, Aerin and Ha, Sura and Ahn, Jihye and Kim, Rira and Kim, Sungyoon and Lee, Younghoon and Kim, Jaehoon and Söll, Dieter and Lee, Hee-Yoon and Park, Hee-Sung
Science, ISSN 0036-8075, 11/2016, Volume 354, Issue 6312, pp. 623 - 626
Many essential biological processes are controlled by posttranslational protein modifications. The inability to synthetically attain the diversity enabled by... 
GENETIC-CODE | MULTIDISCIPLINARY SCIENCES | PHOSPHOSERINE | CHEMISTRY | BOND FORMATION | CYSTEINE | POSTTRANSLATIONAL MODIFICATIONS | RECOMBINANT HISTONES | LYSINE ANALOGS | METHYL-LYSINE | PEPTIDE | Protein Biosynthesis | Protein Engineering - methods | Histones - chemistry | Xenopus laevis | Ubiquitin - chemistry | Histones - biosynthesis | Recombinant Proteins - chemistry | Alanine - chemistry | Iodides - chemistry | Recombinant Proteins - biosynthesis | Zinc - chemistry | Xenopus Proteins - chemistry | Alanine - analogs & derivatives | Animals | Copper - chemistry | Green Fluorescent Proteins - biosynthesis | Xenopus Proteins - biosynthesis | Protein Processing, Post-Translational | Acetylation | Green Fluorescent Proteins - chemistry | Methylation | Ubiquitin - biosynthesis | Phosphoserine - chemistry | Post-translational modification | Protein research | Research | Proteins | Chemicals | Biological activity | Biological diversity | Carbon-carbon composites | Histones | Copper | Zinc | Functional groups | Radicals | Recombinant
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8. Full Text Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases
by Zhuang, Min and Calabrese, Matthew F and Liu, Jiang and Waddell, M. Brett and Nourse, Amanda and Hammel, Michal and Miller, Darcie J and Walden, Helen and Duda, David M and Seyedin, Steven N and Hoggard, Timothy and Harper, J. Wade and White, Kevin P and Schulman, Brenda A and Argonne National Lab. (ANL), Argonne, IL (United States)
Molecular Cell, ISSN 1097-2765, 10/2009, Volume 36, Issue 1, pp. 39 - 50
In the largest E3 ligase subfamily, Cul3 binds a BTB domain, and an associated protein-interaction domain such as MATH recruits substrates for ubiquitination.... 
PROTEINS | E3 LIGASE | OXIDATIVE STRESS | PROTEIN SPOP | NRF2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCF | ADAPTER | DEGRADATION | BTB DOMAIN | F-BOX | TRANSCRIPTION FACTOR | CELL BIOLOGY | Transcription Factors - chemistry | Humans | Crystallography, X-Ray | Drosophila Proteins - metabolism | Mutation - physiology | Protein Multimerization - physiology | Protein Structure, Quaternary - physiology | Ubiquitination - physiology | Peptide Fragments - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Nuclear Proteins - chemistry | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Cullin Proteins - chemistry | Peptide Fragments - chemistry | Phosphoprotein Phosphatases - genetics | Consensus Sequence - physiology | Recombinant Fusion Proteins - genetics | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Drosophila melanogaster | Phosphoprotein Phosphatases - chemistry | Protein Binding - physiology | Adaptor Proteins, Signal Transducing - chemistry | Histones - chemistry | Protein Interaction Domains and Motifs - physiology | Phosphoprotein Phosphatases - metabolism | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Cullin Proteins - metabolism | Nuclear Proteins - genetics | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Nuclear Proteins - metabolism | Drosophila Proteins - chemistry | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Cullin Proteins - genetics | Transcription Factors - metabolism | Animals | Histones - genetics | Adaptor Proteins, Signal Transducing - genetics | Drosophila Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin | Chromatin | Phosphatases | Ligases | CHROMATIN | BASIC BIOLOGICAL SCIENCES | SUBSTRATES | FLEXIBILITY | GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE | LIGASES | DIMERIZATION | DIMERS | PHOSPHATASES
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9. Full Text Lanthanide tags for site-specific ligation to an unnatural amino acid and generation of pseudocontact shifts in proteins
by Loh, Choy Theng and Ozawa, Kiyoshi and Tuck, Kellie L and Barlow, Nicholas and Huber, Thomas and Otting, Gottfried and Graham, Bim
Bioconjugate Chemistry, ISSN 1043-1802, 02/2013, Volume 24, Issue 2, pp. 260 - 268
Pseudocontact shifts (PCS) from paramagnetic lanthanide ions present powerful long-range structural restraints for structural biology by NMR spectroscopy, but... 
RESIDUAL DIPOLAR COUPLINGS | COMPLEX | METAL-ION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | BIOCHEMICAL RESEARCH METHODS | CHEMISTRY, ORGANIC | WEAK ALIGNMENT | CHEMISTRY, MULTIDISCIPLINARY | PARAMAGNETIC NMR-SPECTROSCOPY | GENETIC-CODE | BIOCONJUGATION | BINDING TAG | PROBE | Phenylalanine - analogs & derivatives | Click Chemistry | Humans | Oligopeptides - genetics | Ubiquitin - chemistry | Histidine - genetics | Models, Molecular | Recombinant Proteins - chemistry | Alkynes - chemistry | Recombinant Proteins - genetics | Ubiquitin - genetics | Azides - chemistry | Cycloaddition Reaction | Proteins - genetics | Copper - chemistry | Lanthanoid Series Elements - chemistry | Heterocyclic Compounds - chemistry | Escherichia coli - genetics | Phenylalanine - genetics | Nuclear Magnetic Resonance, Biomolecular | Catalysis | Proteins - chemistry | Histidine - chemistry | Oligopeptides - chemistry
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10. Full Text Copper-triggered aggregation of ubiquitin
by Arnesano, Fabio and Scintilla, Simone and Calò, Vincenza and Bonfrate, Elena and Ingrosso, Chiara and Losacco, Maurizio and Pellegrino, Teresa and Rizzarelli, Enrico and Natile, Giovanni
PLoS ONE, ISSN 1932-6203, 09/2009, Volume 4, Issue 9, pp. e7052 - e7052
Neurodegenerative disorders share common features comprising aggregation of misfolded proteins, failure of the ubiquitin-proteasome system, and increased... 
BIOLOGY | Protein Structure, Tertiary | Protein Structure, Secondary | Microscopy, Electron, Transmission - methods | Solvents - chemistry | Humans | Molecular Conformation | Chelating Agents - chemistry | Ubiquitin - chemistry | Ubiquitin - metabolism | Spectroscopy, Fourier Transform Infrared | Copper - chemistry | Alzheimer Disease - metabolism | Copper - metabolism | Microscopy, Atomic Force | Protein Binding | Cell Membrane - metabolism | Proteasome Endopeptidase Complex - metabolism | Electrochemistry - methods | Oligomers | Ubiquitin | Development and progression | Nervous system diseases | Analysis | Electric properties | Brain | Atomic force microscopy | Parkinson's disease | Aluminum | Disorders | Conglomerates | Risk factors | Proteins | Ring structures | Particle physics | Dichroism | Chelation | Copper | Alzheimer's disease | Movement disorders | Cadmium | Dielectric constant | Trifluoroethanol | Neurodegenerative diseases | Infrared spectra | Electron microscopy | Fatty acids | Substrates | Circular dichroism | Studies | Aggregates | Proteasomes | Dismantling | Parkinsons disease | Chain branching | Lipids | Agglomeration | Infrared analysis | Protein folding | Spectrum analysis | Amyloid | Incubation | Gel electrophoresis | Health risks | Particulates | Amyotrophic lateral sclerosis | Clustering | Phosphocholine | Zinc | Coalescing | Transmission electron microscopy | N-Terminus | Nickel | Dimers | Liposomes | Alzheimers disease | Coalescence | Index Medicus
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11. Full Text Compositional Control of Phase-Separated Cellular Bodies
by Banani, Salman F and Rice, Allyson M and Peeples, William B and Lin, Yuan and Jain, Saumya and Parker, Roy and Rosen, Michael K
Cell, ISSN 0092-8674, 07/2016, Volume 166, Issue 3, pp. 651 - 663
Cellular bodies such as P bodies and PML nuclear bodies (PML NBs) appear to be phase-separated liquids organized by multivalent interactions among proteins and... 
PROTEIN | RNA | LOW-COMPLEXITY DOMAINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | PML NUCLEAR-BODIES | DYNAMICS | LIQUID DROPLETS | BODY FORMATION | SACCHAROMYCES-CEREVISIAE | BINDING | STRESS GRANULES | CELL BIOLOGY | Body Composition | Organelles - chemistry | Cell Line | Yeasts | Humans | Ubiquitins - chemistry | Amino Acid Motifs | Polypyrimidine Tract-Binding Protein - chemistry | Cell Compartmentation | Artificial Cells - chemistry | Protein Engineering | Electrochemistry | Carrier Proteins - chemistry | Cell Nucleus - chemistry | Molecular Structure | HeLa Cells | Proteins - chemistry | In Vitro Techniques | Cytoplasm | Proteins | Physiological aspects | Analysis | Yuan (China)
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12. Full Text Effects of Select Anions from the Hofmeister Series on the Gas-Phase Conformations of Protein Ions Measured with Traveling-Wave Ion Mobility Spectrometry/Mass Spectrometry
by Merenbloom, Samuel I and Flick, Tawnya G and Daly, Michael P and Williams, Evan R
Journal of The American Society for Mass Spectrometry, ISSN 1044-0305, 11/2011, Volume 22, Issue 11, pp. 1978 - 1990
The gas-phase conformations of ubiquitin, cytochrome c, lysozyme, and α-lactalbumin ions, formed by electrospray ionization (ESI) from aqueous solutions... 
Biotechnology | Chemistry | Analytical Chemistry | Ion mobility | Hofmeister series | Adduction | Proteomics | Bioinformatics | Mass spectrometry | Organic Chemistry | Conformation | RAY-ABSORPTION SPECTROSCOPY | CHEMISTRY, ANALYTICAL | UBIQUITIN IONS | BIOCHEMICAL RESEARCH METHODS | CHEMISTRY, PHYSICAL | AQUEOUS-SOLUTION | CYTOCHROME-C | BULK WATER | SPECTROSCOPY | LIQUID WATER | STRUCTURAL TRANSITIONS | IONIZATION MASS-SPECTROMETRY | ELECTROSPRAY-IONIZATION | BIOLOGICAL-SYSTEMS | Cytochromes c - chemistry | Gases - chemistry | Iodine Compounds - chemistry | Acids - chemistry | Muramidase - chemistry | Spectrometry, Mass, Electrospray Ionization - methods | Lactalbumin - chemistry | Ubiquitin - chemistry | Sulfuric Acids - chemistry | Anions - chemistry | Proteins - chemistry | Perchlorates - chemistry | Proteins | Cytochrome | Spectroscopy | Anions | Aqueous solutions | Ionization | Ionic mobility | Ions | Scientific imaging | Lysozyme
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