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1. Full Text BMP signalling permits population expansion by preventing premature myogenic differentiation in muscle satellite cells
by Ono, Y and Calhabeu, F and Morgan, J.E and Katagiri, T and Amthor, H and Zammit, P.S
Cell Death and Differentiation, ISSN 1350-9047, 02/2011, Volume 18, Issue 2, pp. 222 - 234
Satellite cells are the resident stem cells of adult skeletal muscle, supplying myonuclei for homoeostasis, hypertrophy and repair. In this study, we have... 
Noggin | Smad | satellite cell | BMP | skeletal muscle | Id1 | STEM-CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | C2C12 MYOBLASTS | SELF-RENEWAL | RECEPTOR | IDENTIFICATION | CELL BIOLOGY | INHIBITION | PROTEINS | EXPRESSION | FATES | Bone Morphogenetic Proteins - antagonists & inhibitors | Phosphorylation | Cell Proliferation | Bone Morphogenetic Proteins - physiology | Bone Morphogenetic Protein 4 - genetics | Bone Morphogenetic Protein 4 - metabolism | Bone Morphogenetic Proteins - metabolism | RNA Interference | Carrier Proteins - pharmacology | Cell Differentiation | Pyrazoles - pharmacology | Recombinant Proteins - metabolism | Signal Transduction | Satellite Cells, Skeletal Muscle - cytology | Bone Morphogenetic Protein Receptors, Type I - genetics | Smad Proteins - genetics | Recombinant Proteins - genetics | Pyrimidines - pharmacology | Recombinant Proteins - pharmacology | Bone Morphogenetic Protein Receptors, Type I - metabolism | Bone Morphogenetic Protein 4 - pharmacology | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Mice | Smad Proteins - metabolism | RNA, Small Interfering - metabolism | Index Medicus | Original Paper
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2. Full Text Efficient cell-specific uptake of binding proteins into the cytoplasm through engineered modular transport systems
by Verdurmen, Wouter P.R and Luginbühl, Manuel and Honegger, Annemarie and Plückthun, Andreas
Journal of Controlled Release, ISSN 0168-3659, 02/2015, Volume 200, pp. 13 - 22
Through advances in protein scaffold engineering and selection technologies, highly specific binding proteins, which fold under reducing conditions, can be... 
Protein engineering | Cytoplasmic delivery | Biotin ligase | Anthrax toxin | Designed ankyrin repeat protein | Pseudomonas exotoxin A | TRANSLOCATION | ANKYRIN REPEAT PROTEIN | PSEUDOMONAS-AERUGINOSA EXOTOXIN | CRYSTAL-STRUCTURE | DARPINS | MAMMALIAN-CELLS | CANCER | CHEMISTRY, MULTIDISCIPLINARY | LETHAL FACTOR | PHARMACOLOGY & PHARMACY | PENETRATING PEPTIDES | Cell Line | Humans | Cytoplasm - metabolism | Ankyrin Repeat | Exotoxins - pharmacology | Repressor Proteins - pharmacology | Biological Transport | MCF-7 Cells | Bacterial Toxins - pharmacology | ADP Ribose Transferases - pharmacology | Carrier Proteins - pharmacology | Escherichia coli Proteins - pharmacology | Carbon-Nitrogen Ligases - pharmacology | Protein Engineering | Virulence Factors - pharmacology | Binding proteins | Protein binding | Index Medicus
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3. Full Text An alginate-based hybrid system for growth factor delivery in the functional repair of large bone defects
by Kolambkar, Yash M and Dupont, Kenneth M and Boerckel, Joel D and Huebsch, Nathaniel and Mooney, David J and Hutmacher, Dietmar W and Guldberg, Robert E
Biomaterials, ISSN 0142-9612, 2010, Volume 32, Issue 1, pp. 65 - 74
Abstract The treatment of challenging fractures and large osseous defects presents a formidable problem for orthopaedic surgeons. Tissue... 
Advanced Basic Science | Dentistry | Drug delivery | Alginate | Bone morphogenetic protein | Scaffold | Bone regeneration | Nanofiber mesh | POLYCAPROLACTONE SCAFFOLDS | POLY(L-LACTIDE) MEMBRANE | MICROCOMPUTED TOMOGRAPHY | HYDROGELS | MATERIALS SCIENCE, BIOMATERIALS | ENGINEERING, BIOMEDICAL | RESORBABLE POLYMERIC MEMBRANES | TISSUE REGENERATION | BIODEGRADABLE CARRIER | CONTROLLED SCAFFOLD DEGRADATION | IN-VIVO | MORPHOGENETIC PROTEIN-2 | Femur - pathology | Angiography | Humans | Femur - diagnostic imaging | X-Ray Microtomography | Biomechanical Phenomena - drug effects | Bone Morphogenetic Proteins - pharmacology | Wound Healing - drug effects | Alginates - pharmacology | Bone Regeneration - drug effects | Nanofibers - ultrastructure | Bone Morphogenetic Proteins - administration & dosage | Implants, Experimental | Bone Morphogenetic Protein 2 | Rats | Recombinant Proteins - pharmacology | Femur - physiopathology | Recombinant Proteins - administration & dosage | Transforming Growth Factor beta - pharmacology | Glucuronic Acid - pharmacology | Animals | Transforming Growth Factor beta - administration & dosage | Kinetics | Drug Delivery Systems - methods | Hexuronic Acids - pharmacology | Finite element method | Biomedical materials | Nanocomposites | Nanomaterials | Bones | Nanostructure | Repair | Growth factors | Defects | Index Medicus
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4. Full Text A family of helminth molecules that modulate innate cell responses via molecular mimicry of host antimicrobial peptides
by Robinson, Mark W and Donnelly, Sheila and Hutchinson, Andrew T and To, Joyce and Taylor, Nicole L and Norton, Raymond S and Perugini, Matthew A and Dalton, John P
PLoS Pathogens, ISSN 1553-7366, 05/2011, Volume 7, Issue 5, pp. e1002042 - e1002042
Over the last decade a significant number of studies have highlighted the central role of host antimicrobial (or defence) peptides in modulating the response... 
IMMUNE-RESPONSE | PROTEIN SECONDARY STRUCTURE | ENTERIC NEMATODE | PATHOGEN FASCIOLA-HEPATICA | MICROBIOLOGY | DEFENSE PEPTIDES | SIZE-DISTRIBUTION ANALYSIS | CIRCULAR-DICHROISM SPECTRA | ALTERNATIVELY ACTIVATED MACROPHAGES | VIROLOGY | CATHELICIDIN FAMILY | LIPOPOLYSACCHARIDE-BINDING | PARASITOLOGY | Helminth Proteins - pharmacology | Membrane Glycoproteins - metabolism | Anti-Infective Agents - metabolism | Humans | Helminth Proteins - chemistry | Lipopolysaccharides - metabolism | Molecular Sequence Data | Antimicrobial Cationic Peptides - metabolism | Anti-Infective Agents - immunology | Inflammation - metabolism | Molecular Mimicry | Fasciola hepatica - chemistry | Fascioliasis - parasitology | Sepsis - metabolism | Carrier Proteins - pharmacology | Endotoxemia - immunology | Toll-Like Receptors - metabolism | Helminth Proteins - metabolism | Fasciola hepatica - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Sepsis - immunology | Acute-Phase Proteins - metabolism | Antimicrobial Cationic Peptides - chemistry | Membrane Glycoproteins - pharmacology | Toll-Like Receptors - immunology | Antimicrobial Cationic Peptides - pharmacology | Helminth Proteins - genetics | Inflammation - immunology | Recombinant Proteins - genetics | Recombinant Proteins - pharmacology | Immunity, Innate | Fasciola hepatica - immunology | Animals | Carrier Proteins - metabolism | Fascioliasis - immunology | Lipopolysaccharides - pharmacology | Mice | Mice, Inbred BALB C | Endotoxemia - metabolism | Acute-Phase Proteins - pharmacology | Proteolysis | Antimicrobial peptides | Worms, Intestinal and parasitic | Physiological aspects | Research | Health aspects | Helminths | Medical research | Peptides | Cytokines | Rodents | Immune system | Index Medicus
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5. Full Text VDAC2 Inhibits BAK Activation and Mitochondrial Apoptosis
by Emily H. -Y. Cheng and Tatiana V. Sheiko and Jill K. Fisher and William J. Craigen and Stanley J. Korsmeyer
Science, ISSN 0036-8075, 7/2003, Volume 301, Issue 5632, pp. 513 - 517
The multidomain proapoptotic molecules BAK or BAX are required to initiate the mitochondrial pathway of apoptosis. How cells maintain the potentially lethal... 
Proteins | Protein isoforms | Molecules | Mitochondria | Cell death | Cell lines | Cytochromes | Reports | Liver cells | Cells | Apoptosis | CYTOCHROME-C | DEPENDENT ANION CHANNEL | BCL-X-L | PROTEIN | RESPIRATION | MULTIDISCIPLINARY SCIENCES | DEATH | RELEASE | DYSFUNCTION | PERMEABILITY TRANSITION | FAMILY | Mitochondria, Liver - metabolism | Humans | BH3 Interacting Domain Death Agonist Protein | Porins - metabolism | Voltage-Dependent Anion Channel 2 | Biopolymers | Carrier Proteins - pharmacology | Porins - isolation & purification | Membrane Proteins - metabolism | Voltage-Dependent Anion Channels | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Cell Line | Porins - genetics | Jurkat Cells | Membrane Proteins - genetics | Mice, Inbred C57BL | Cells, Cultured | Etoposide - pharmacology | Mitochondria - metabolism | Recombinant Proteins - pharmacology | bcl-2-Associated X Protein | Animals | Carrier Proteins - metabolism | Membrane Proteins - chemistry | bcl-2 Homologous Antagonist-Killer Protein | Protein Binding | Voltage-Dependent Anion Channel 1 | Protein Conformation | Mice | Proto-Oncogene Proteins c-bcl-2 | Intracellular Membranes - metabolism | Staurosporine - pharmacology | Cellular biology | Genetics | Index Medicus
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6. Full Text Characterisation of plasmalemmal shedding of vesicles induced by the cholesterol/sphingomyelin binding protein, ostreolysin A-mCherry
by Skočaj, Matej and Yu, Yang and Grundner, Maja and Resnik, Nataša and Bedina Zavec, Apolonija and Leonardi, Adrijana and Križaj, Igor and Guella, Graziano and Maček, Peter and Kreft, Mateja Erdani and Frangež, Robert and Veranič, Peter and Sepčić, Kristina
BBA - Biomembranes, ISSN 0005-2736, 11/2016, Volume 1858, Issue 11, pp. 2882 - 2893
Ostreolysin A (OlyA) is a 15-kDa protein that binds selectively to cholesterol/sphingomyelin membrane nanodomains. This binding induces the production of... 
Extracellular vesicles | Ostreolysin A | Vesiculation | Aegerolysin proteins | CELLS | CHOLESTEROL | BIOCHEMISTRY & MOLECULAR BIOLOGY | MASS-SPECTROMETRY | DETERGENT-RESISTANT MEMBRANES | A/PLEUROTOLYSIN B | BIOPHYSICS | STREPTOLYSIN-O | PORE-FORMING PROTEINS | CURVATURE | OYSTER MUSHROOM | Metabolomics | Hemolysin Proteins - pharmacology | Recombinant Fusion Proteins - pharmacology | Calcium - metabolism | Hemolysin Proteins - genetics | Cell-Derived Microparticles - chemistry | Recombinant Fusion Proteins - metabolism | Luminescent Proteins - pharmacology | Cell Membrane - chemistry | Cholesterol - chemistry | Sphingomyelins - isolation & purification | Cell-Derived Microparticles - drug effects | Carrier Proteins - pharmacology | Madin Darby Canine Kidney Cells | Ion Transport | Pancreatic Elastase - genetics | Pancreatic Elastase - pharmacology | Cell Membrane - drug effects | Cell Survival - drug effects | Cholesterol - isolation & purification | Pancreatic Elastase - metabolism | Fungal Proteins - genetics | Lysophosphatidylcholines - isolation & purification | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Dogs | Protein Binding | Recombinant Fusion Proteins - genetics | Luminescent Proteins - genetics | Sphingomyelins - chemistry | Fungal Proteins - pharmacology | Lysophosphatidylcholines - chemistry | Hemolysin Proteins - metabolism | Fungal Proteins - metabolism | Luminescent Proteins - metabolism | Proteins | Mass spectrometry | Analysis | Protein binding | Cells | Index Medicus
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7. Full Text Characterization of Rictor Phosphorylation Sites Reveals Direct Regulation of mTOR Complex 2 by S6K1
by Christian C. Dibble and John M. Asara and Brendan D. Manning
Molecular and Cellular Biology, ISSN 0270-7306, 11/2009, Volume 29, Issue 21, pp. 5657 - 5670
Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
MAMMALIAN TARGET | TSC1-TSC2 COMPLEX | BINDING PARTNER | AKT/PROTEIN-KINASE-B | PROTEIN-KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | HYDROPHOBIC MOTIF PHOSPHORYLATION | TUBEROUS SCLEROSIS | CELL-GROWTH | INSULIN-RECEPTOR SUBSTRATE-1 | RAPAMYCIN COMPLEX-1 | CELL BIOLOGY | Humans | Molecular Sequence Data | Amino Acid Substitution - drug effects | Ribosomal Protein S6 Kinases, 90-kDa - metabolism | Mass Spectrometry | Chromatography, Liquid | Conserved Sequence | Carrier Proteins - chemistry | Phosphorylation - drug effects | Proto-Oncogene Proteins c-akt - metabolism | Binding Sites | Rapamycin-Insensitive Companion of mTOR Protein | Amino Acid Sequence | Insulin - pharmacology | Phosphoserine - metabolism | Sirolimus - pharmacology | Phosphothreonine - metabolism | 14-3-3 Proteins - metabolism | Animals | Carrier Proteins - metabolism | Intercellular Signaling Peptides and Proteins - pharmacology | Models, Biological | Mice | HeLa Cells | Vertebrates - metabolism | Index Medicus
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8. Full Text The non-specific lipid transfer protein, Ara h 9, is an important allergen in peanut
by Lauer, I and Dueringer, N and Pokoj, S and Rehm, S and Zoccatelli, G and Reese, G and Miguel-Moncin, M. S and Cistero-Bahima, A and Enrique, E and Lidholm, J and Vieths, S and Scheurer, S
Clinical & Experimental Allergy, ISSN 0954-7894, 09/2009, Volume 39, Issue 9, pp. 1427 - 1437
Summary Background Plant food allergy in the Mediterranean area is mainly caused by non-specific lipid transfer proteins (nsLTP). The aim of this study was to... 
Ara h 9 | food allergy | lipid transfer protein | Pru p 3 | peanut allergen | Food allergy | Peanut allergen | Lipid transfer protein | HAZELNUT | PREVALENCE | IMMUNOLOGY | IN-VITRO DIAGNOSIS | MAJOR ALLERGEN | DIGESTION | ALLERGY | PEACH | PURIFICATION | CROSS-REACTIVITY | RECOMBINANT ALLERGENS | EXPRESSION | Humans | Male | Histamine - immunology | Antigens, Plant - chemistry | Glycoproteins - pharmacology | Immunoglobulin E - blood | Immunoglobulin E - immunology | Peanut Hypersensitivity - blood | Allergens - immunology | Plant Proteins - chemistry | Protein Isoforms - chemistry | Carrier Proteins - pharmacology | Allergens - chemistry | Basophils - immunology | Carrier Proteins - chemistry | Female | Glycoproteins - chemistry | Circular Dichroism | Carrier Proteins - immunology | Rabbits | Plant Proteins - pharmacology | Protein Structure, Secondary | Recombinant Proteins - chemistry | Antigens, Plant - immunology | Plant Proteins - immunology | Antigens, Plant - pharmacology | Peanut Hypersensitivity - immunology | Recombinant Proteins - pharmacology | Spain | Protein Isoforms - pharmacology | Glycoproteins - immunology | Animals | Recombinant Proteins - immunology | Allergens - pharmacology | Structural Homology, Protein | Protein Isoforms - immunology | Antigen-antibody reactions | Allergens | Histamine | Analysis | Immunoglobulin E | Amino acids | Recombinant proteins | Index Medicus
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9. Full Text Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization
by Youle, Richard J and Sharpe, Juanita C and Karbowski, Mariusz and Cecconi, Francesco and Gaume, Brigitte and Arnoult, Damien
The EMBO Journal, ISSN 0261-4189, 09/2003, Volume 22, Issue 17, pp. 4385 - 4399
Mitochondrial outer‐membrane permeabilization by pro‐apoptotic Bcl‐2 family members plays a crucial role in apoptosis induction. However, whether this directly... 
cytochrome | c | Diablo | HtrA2 | Omi | Smac | EndoG | AIF | Cytochrome c | APOPTOSIS-INDUCING FACTOR | OUTER-MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BAX OLIGOMERIZATION | CELL BIOLOGY | PROGRAMMED CELL-DEATH | CAENORHABDITIS-ELEGANS | DNA | SERINE-PROTEASE | cytochrome c | CYTOCHROME-C RELEASE | PROTEINS | ENDONUCLEASE-G | Apoptosis Inducing Factor | Humans | BH3 Interacting Domain Death Agonist Protein | Caspases - metabolism | Mitochondrial Proteins - metabolism | Carrier Proteins - pharmacology | DNA Fragmentation | Endodeoxyribonucleases - metabolism | Membrane Proteins - metabolism | Proto-Oncogene Proteins - metabolism | Proto-Oncogene Proteins - pharmacology | Caenorhabditis elegans - metabolism | Flavoproteins - metabolism | Intracellular Signaling Peptides and Proteins | Mitochondria - metabolism | Permeability | Recombinant Proteins - pharmacology | bcl-2-Associated X Protein | Cytochrome c Group - metabolism | High-Temperature Requirement A Serine Peptidase 2 | Animals | Caenorhabditis elegans - cytology | Carrier Proteins - metabolism | bcl-2 Homologous Antagonist-Killer Protein | Mice | Serine Endopeptidases - metabolism | Enzyme Activation | HeLa Cells | Proto-Oncogene Proteins c-bcl-2 | In Vitro Techniques | Staurosporine - pharmacology | Apoptosis | Bak protein | Smac protein | HtrA2 protein | endonuclease G | Diablo protein | Omi protein | apoptosis-inducing factor | Index Medicus
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10. Full Text Effects of protein dose and delivery system on BMP-mediated bone regeneration
by Boerckel, Joel D and Kolambkar, Yash M and Dupont, Kenneth M and Uhrig, Brent A and Phelps, Edward A and Stevens, Hazel Y and García, Andrés J and Guldberg, Robert E
Biomaterials, ISSN 0142-9612, 2011, Volume 32, Issue 22, pp. 5241 - 5251
Abstract Delivery of recombinant proteins is a proven therapeutic strategy to promote endogenous repair mechanisms and tissue regeneration. Bone morphogenetic... 
Advanced Basic Science | Dentistry | Drug release | Alginate | Bone tissue engineering | Hydrogel | BMP (bone morphogenetic protein) | Collagen | MATERIALS SCIENCE, BIOMATERIALS | GROWTH-FACTOR DELIVERY | ENGINEERING, BIOMEDICAL | SPINAL-FUSION | CONTROLLED SCAFFOLD DEGRADATION | CLINICAL-APPLICATIONS | IN-VIVO | BIOLOGICAL-ACTIVITY | EXTRACELLULAR-MATRIX | MARROW STROMAL CELLS | MORPHOGENETIC PROTEIN-2 | LUMBAR FUSION | Nanofibers - chemistry | Recombinant Proteins - metabolism | Bone Regeneration - drug effects | Bone Regeneration - physiology | Drug Carriers - metabolism | Rats | Recombinant Proteins - chemistry | Stress, Mechanical | Collagen - chemistry | Materials Testing | Recombinant Proteins - genetics | Recombinant Proteins - pharmacology | Rats, Sprague-Dawley | X-Ray Microtomography | Drug Carriers - chemistry | Drug Delivery Systems | Dose-Response Relationship, Drug | Intercellular Signaling Peptides and Proteins - metabolism | Bone Morphogenetic Proteins - metabolism | Animals | Alginates - chemistry | Bone Morphogenetic Proteins - chemistry | Bone Morphogenetic Proteins - genetics | Bone Morphogenetic Proteins - pharmacology | Index Medicus
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