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index medicus (77) 77
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amino acid sequence (34) 34
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cysteine (20) 20
cyclotides (19) 19
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cystine-knot miniproteins - chemistry (17) 17
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kalata b1 (15) 15
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article (13) 13
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cyclotides - metabolism (9) 9
cystine-knot (9) 9
expression (9) 9
momordica-cochinchinensis (9) 9
plant proteins - chemistry (9) 9
plant sciences (9) 9
protein engineering (9) 9
biotechnology & applied microbiology (8) 8
cyclotides - genetics (8) 8
cystine-knot miniproteins - metabolism (8) 8
in-vitro (8) 8
in-vivo (8) 8
inhibitors (8) 8
multidisciplinary sciences (8) 8
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physiological aspects (8) 8
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agouti-related protein (7) 7
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cyclotides - pharmacology (7) 7
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gene expression (7) 7
genetic aspects (7) 7
mice, nude (7) 7
protein structure, secondary (7) 7
protein structure, tertiary (7) 7
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biochemistry, general (6) 6
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cystine-knot miniproteins - genetics (6) 6
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1. Full Text Engineered knottin peptide enables noninvasive optical imaging of intracranial medulloblastoma
by Sarah J. Moore and Melanie G. Hayden Gephart and Jamie M. Bergen and YouRong S. Su and Helen Rayburn and Matthew P. Scott and Jennifer R. Cochran
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2013, Volume 110, Issue 36, pp. 14598 - 14603
Central nervous system tumors carry grave clinical prognoses due to limited effectiveness of surgical resection, radiation, and chemotherapy. Thus, improved... 
Neuroimaging | Molecular imaging | Molecules | Dyes | Imaging | Medulloblastoma | Brain neoplasms | Tumors | Integrins | Cancer | Protein engineering | Tumor targeting | Miniprotein | Hedgehog pathway | tumor targeting | GLIOBLASTOMA-MULTIFORME | MULTIDISCIPLINARY SCIENCES | MOLECULAR-SIZE | BLOOD-BRAIN-BARRIER | MALIGNANT GLIOMA | LIVING SUBJECTS | protein engineering | TUMOR XENOGRAFTS | IN-VIVO | 5-AMINOLEVULINIC ACID | THERAPEUTIC TARGETS | miniprotein | INTEGRIN ALPHA(V)BETA ANTAGONISTS | Cystine-Knot Miniproteins - metabolism | Cerebellar Neoplasms - diagnosis | Fluorescent Dyes - metabolism | Cystine-Knot Miniproteins - genetics | Male | Green Fluorescent Proteins - genetics | Diagnostic Imaging - methods | Sensitivity and Specificity | Protein Engineering | Cystine-Knot Miniproteins - chemistry | Female | Patched Receptors | Medulloblastoma - genetics | Cerebellar Neoplasms - metabolism | Fluorescent Dyes - chemistry | Green Fluorescent Proteins - metabolism | Medulloblastoma - diagnosis | Receptors, Cell Surface - metabolism | Mice, Transgenic | Molecular Imaging - methods | Medulloblastoma - metabolism | Cerebellar Neoplasms - genetics | Mice, Knockout | Animals | Mice, Nude | Protein Binding | Mice | Integrin alpha5beta1 - metabolism | Microscopy, Fluorescence | Receptors, Cell Surface - genetics | Physiological aspects | Diagnostic imaging | Diagnosis | Research | Methods | Hedgehog proteins | Tissue | Chemotherapy | Peptides | Brain cancer | Rodents | Nervous system | Index Medicus | Biological Sciences
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2. Full Text Cyclic Peptides Arising by Evolutionary Parallelism via Asparaginyl-Endopeptidase—Mediated Biosynthesis
by Joshua S. Mylne and Lai Yue Chan and Aurelie H. Chanson and Norelle L. Daly and Hanno Schaefer and Timothy L. Bailey and Philip Nguyencong and Laura Cascales and David J. Craik
The Plant Cell, ISSN 1040-4651, 7/2012, Volume 24, Issue 7, pp. 2765 - 2778
The cyclic miniprotein Momordica cochinchinensis Trypsin Inhibitor II (MCoTI-II) (34 amino acids) is a potent trypsin inhibitor (TI) and a favored scaffold for... 
Proteins | Polymerase chain reaction | Cyclic peptides | DNA | Squashes | Protein precursors | Amino acids | Biosynthesis | Open reading frames | Free energy | CIRCULAR PROTEINS | CYSTINE KNOT MOTIF | ARABIDOPSIS-THALIANA | BACKBONE CYCLIZATION | MOMORDICA-COCHINCHINENSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | VACUOLAR PROCESSING ENZYME | STRUCTURAL MOTIFS | INHIBITOR MCOTI-II | PLANT SCIENCES | CELL BIOLOGY | PLANT CYCLOTIDES | TRYPSIN-INHIBITOR | Cyclotides - chemistry | Cystine-Knot Miniproteins - metabolism | Molecular Sequence Data | Cystine-Knot Miniproteins - genetics | Phylogeny | Peptides, Cyclic - chemistry | Peptides, Cyclic - metabolism | Cysteine Endopeptidases - metabolism | Peptides, Cyclic - genetics | Cystine-Knot Miniproteins - chemistry | DNA, Plant - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Models, Molecular | Momordica - metabolism | Cyclotides - genetics | Arabidopsis - metabolism | Arabidopsis - genetics | Sequence Homology, Amino Acid | Sequence Alignment | Gene Amplification | Cyclotides - metabolism | Momordica - genetics | Protein Conformation | Evolution, Molecular | Arabidopsis thaliana | Synthesis | Peptides | Plant genetics | Genetic aspects | Research | Observations | Index Medicus
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3. Full Text Combinatorial Optimization of Cystine-Knot Peptides towards High-Affinity Inhibitors of Human Matriptase-1
by Glotzbach, Bernhard and Reinwarth, Michael and Weber, Niklas and Fabritz, Sebastian and Tomaszowski, Michael and Fittler, Heiko and Christmann, Andreas and Avrutina, Olga and Kolmar, Harald
PLoS ONE, ISSN 1932-6203, 10/2013, Volume 8, Issue 10, pp. e76956 - e76956
Cystine-knot miniproteins define a class of bioactive molecules with several thousand natural members. Their eponymous motif comprises a rigid structured core... 
MOMORDICA-COCHINCHINENSIS | PLATELET-AGGREGATION | ELATERIUM TRYPSIN-INHIBITOR | FACTOR ACTIVATOR INHIBITOR-1 | MULTIDISCIPLINARY SCIENCES | ENVELOPE GLYCOPROTEIN | SELECTIVE INHIBITORS | SERINE-PROTEASE MATRIPTASE | YEAST SURFACE DISPLAY | ALPHA(V)BETA INTEGRIN | PLASMINOGEN ACTIVATION | Cell Line | Urokinase-Type Plasminogen Activator - antagonists & inhibitors | Cystine-Knot Miniproteins - metabolism | Humans | Enzyme Inhibitors - pharmacology | Trypsin Inhibitors - pharmacology | Models, Molecular | Peptide Library | Enzyme Activation - drug effects | Two-Hybrid System Techniques | Trypsin Inhibitors - chemistry | Enzyme Inhibitors - chemistry | Cystine-Knot Miniproteins - chemistry | Protein Binding | Protein Conformation | Serine Endopeptidases - metabolism | Cystine-Knot Miniproteins - pharmacology | Thrombin | Cysteine | Trypsin | Peptides | Proteolysis | Cystine | Trypsin inhibitors | Yeast | Serine | Amino acids | Metastasis | Optimization | Cell adhesion & migration | Proteins | Tomography | Chemical bonds | Growth factors | Biodegradation | Antigens | Enzymes | Medical imaging | Medical screening | Biological activity | Molecular chains | Inhibitors | Serine proteinase | Combinatorial analysis | Cancer | Conformation | Index Medicus
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4. Full Text The insecticidal neurotoxin Aps III is an atypical knottin peptide that potently blocks insect voltage-gated sodium channels
by Bende, Niraj S and Kang, Eunji and Herzig, Volker and Bosmans, Frank and Nicholson, Graham M and Mobli, Mehdi and King, Glenn F
Biochemical Pharmacology, ISSN 0006-2952, 05/2013, Volume 85, Issue 10, pp. 1542 - 1554
One of the most potent insecticidal venom peptides described to date is Aps III from the venom of the trapdoor spider . Aps III is highly neurotoxic to... 
Spider-venom peptide | Gating modifier | Inhibitor cystine knot | Pore blocker | Neurotoxin | Voltage-gated sodium channel | STRUCTURAL MOTIF | ESCHERICHIA-COLI | NA+ CHANNELS | ALPHA-TOXIN BINDING | FUNNEL-WEB SPIDERS | CA-V CHANNELS | CALCIUM-CHANNELS | PHARMACOLOGY & PHARMACY | DELTA-ATRACOTOXINS | CYSTINE KNOT | SPIDER-VENOM PEPTIDES | Cystine-Knot Miniproteins - metabolism | Molecular Sequence Data | Neurons - cytology | Spider Venoms - pharmacology | Diptera - metabolism | Periplaneta - drug effects | Disulfides - chemistry | Cystine-Knot Miniproteins - chemistry | Neurons - metabolism | Spider Venoms - metabolism | Neurons - drug effects | Insect Proteins - metabolism | Spider Venoms - chemistry | Spiders - chemistry | Spiders - physiology | Membrane Potentials - drug effects | Recombinant Proteins - metabolism | Amino Acid Sequence | Neurotoxins - chemistry | Protein Structure, Secondary | Models, Molecular | Recombinant Proteins - chemistry | Sodium Channel Blockers - metabolism | Sodium Channel Blockers - pharmacology | Recombinant Proteins - pharmacology | Insect Proteins - antagonists & inhibitors | Periplaneta - metabolism | Neurotoxins - pharmacology | Patch-Clamp Techniques | Animals | Escherichia coli - genetics | Insect Proteins - chemistry | Diptera - drug effects | Neurotoxins - metabolism | Voltage-Gated Sodium Channels - chemistry | Sodium Channel Blockers - chemistry | Kinetics | Primary Cell Culture | Cystine-Knot Miniproteins - pharmacology | Voltage-Gated Sodium Channels - metabolism | Peptides | Index Medicus | neurotoxin | pore blocker | inhibitor cystine knot | gating modifier | voltage-gated sodium channel | spider-venom peptide
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5. Full Text PET imaging of tumor neovascularization in a transgenic mouse model with a novel 64Cu-DOTA-knottin peptide
by Nielsen, Carsten H and Kimura, Richard H and Withofs, Nadia and Tran, Phuoc T and Miao, Zheng and Cochran, Jennifer R and Cheng, Zhen and Felsher, Dean and Kjær, Andreas and Willmann, Juergen K and Gambhir, Sanjiv S
Cancer research, ISSN 0008-5472, 11/2010, Volume 70, Issue 22, pp. 9022 - 9030
Due to the high mortality of lung cancer, there is a critical need to develop diagnostic procedures enabling early detection of the disease while at a curable... 
Neovascularization, Pathologic - diagnosis | Cystine-Knot Miniproteins - metabolism | Radiopharmaceuticals - pharmacokinetics | Proto-Oncogene Proteins p21(ras) - genetics | Platelet Endothelial Cell Adhesion Molecule-1 - analysis | Tomography, X-Ray Computed - methods | Mice, Transgenic | Neoplasms - blood supply | Neoplasms - diagnosis | Positron-Emission Tomography - methods | Copper Radioisotopes - pharmacokinetics | Integrins - metabolism | Proto-Oncogene Proteins c-myc - metabolism | Tissue Distribution | Animals | Neoplasms - genetics | Sensitivity and Specificity | Fluorescent Antibody Technique | Neovascularization, Pathologic - genetics | Mice | Neovascularization, Pathologic - metabolism | Proto-Oncogene Proteins c-myc - genetics | Mutation | Proto-Oncogene Proteins p21(ras) - metabolism | Index Medicus | Animal models | Translation | Lung nodules | Lung cancer | Mortality | Transgenic mice | Thorax | Kidney | Angiogenesis | Computed tomography | vascularization | Positron emission tomography | Integrins | Tracers | Tumors
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6. Full Text Preliminary evaluation of (177)Lu-labeled knottin peptides for integrin receptor-targeted radionuclide therapy
by Jiang, Lei and Miao, Zheng and Kimura, Richard H and Liu, Hongguang and Cochran, Jennifer R and Culter, Cathy S and Bao, Ande and Li, Peiyong and Cheng, Zhen
European journal of nuclear medicine and molecular imaging, 04/2011, Volume 38, Issue 4, pp. 613 - 622
Cystine knot peptides (knottins) 2.5D and 2.5F were recently engineered to bind integrin receptors with high affinity and specificity. These receptors are... 
Amino Acid Sequence | Cystine-Knot Miniproteins - metabolism | Radioisotopes - therapeutic use | Humans | Gene Expression Regulation, Neoplastic | Models, Molecular | Molecular Sequence Data | Male | Radiation Dosage | Integrins - metabolism | Cystine-Knot Miniproteins - therapeutic use | Animals | Heterocyclic Compounds, 1-Ring - chemistry | Cell Transformation, Neoplastic | Platelet Membrane Glycoproteins - metabolism | Radiochemistry | Radiotherapy - methods | Cell Line, Tumor | Cystine-Knot Miniproteins - chemistry | Cystine-Knot Miniproteins - pharmacokinetics | Adult | Protein Conformation | Mice | Lutetium - therapeutic use | Index Medicus
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7. Full Text Distribution and Evolution of Circular Miniproteins in Flowering Plants
by Christian W. Gruber and Alysha G. Elliott and David C. Ireland and Piero G. Delprete and Steven Dessein and Ulf Göransson and Manuela Trabi and Conan K. Wang and Andrew B. Kinghorn and Elmar Robbrecht and David J. Craik and Medicinska och farmaceutiska vetenskapsområdet and Institutionen för läkemedelskemi and Uppsala universitet and Farmaceutiska fakulteten and Avdelningen för farmakognosi
The Plant Cell, ISSN 1040-4651, 9/2008, Volume 20, Issue 9, pp. 2471 - 2483
Cyclotides are disulfide-rich miniproteins with the unique structural features of a circular backbone and knotted arrangement of three conserved disulfide... 
Proteins | Botanical gardens | Flowering plants | Cyclotides | Amino acids | Evolution | Plants | Sequencing | Violas | Angiosperms | COFFEE FAMILY RUBIACEAE | OLDENLANDIA-AFFINIS | PROTEIN SEQUENCES | STRUCTURAL MOTIF | BIOCHEMISTRY & MOLECULAR BIOLOGY | PLANT SCIENCES | CELL BIOLOGY | CHASSALIA-PARVIFOLIA | CYCLIC CYSTINE KNOT | MACROCYCLIC PEPTIDES | CYCLOTIDE KALATA B1 | PHYLOGENETIC-RELATIONSHIPS | SEED PLANTS | Cyclotides - classification | Amino Acid Sequence | Cyclotides - chemistry | Molecular Sequence Data | Magnoliopsida - genetics | Cyclotides - genetics | Phylogeny | Magnoliopsida - metabolism | Plant Proteins - genetics | Plant Proteins - classification | Models, Biological | Plant Proteins - chemistry | Evolution, Molecular | Index Medicus | s | Medical and Health Sciences | MEDICINE | Medicin och hälsovetenskap | MEDICIN
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8. Cystine-knot peptides: Emerging tools for cancer imaging and therapy
by Ackerman, Shelley E and Currier, Nicolas V and Bergen, Jamie M and Cochran, Jennifer R
Expert Review of Proteomics, ISSN 1478-9450, 10/2014, Volume 11, Issue 5, pp. 561 - 572
Cystine-knot miniproteins, also known as knottins, constitute a large family of structurally related peptides with diverse amino acid sequences and biological... 
disulfide-rich peptides | protein engineering | therapeutics | tumor targeting | knottin | drug discovery | miniprotein | molecular imaging | DESIGN | INTEGRIN | BIOCHEMICAL RESEARCH METHODS | FAMILY | AGOUTI-RELATED PROTEIN | TUMOR PAINT | MINIPROTEINS | MCOTI-II | AFFINITY | CHLOROTOXIN | SCAFFOLD | Neoplasms - metabolism | Chronic Pain - drug therapy | Cystine-Knot Miniproteins - metabolism | Humans | Irritable Bowel Syndrome - drug therapy | Molecular Imaging - methods | Antineoplastic Agents - therapeutic use | Neoplasms - diagnosis | Neoplasms - drug therapy | Antineoplastic Agents - metabolism | Cystine-Knot Miniproteins - therapeutic use | Radiopharmaceuticals - metabolism | Animals | Protein Engineering | Biomarkers, Tumor - metabolism | Cyclotides - therapeutic use
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9. Full Text A cystine‐knot miniprotein from tomato fruit inhibits endothelial cell migration and angiogenesis by affecting vascular endothelial growth factor receptor (VEGFR) activation and nitric oxide production
by Treggiari, Davide and Zoccatelli, Gianni and Molesini, Barbara and Degan, Maurizio and Rotino, Giuseppe Leonardo and Sala, Tea and Cavallini, Chiara and MacRae, Calum A and Minuz, Pietro and Pandolfini, Tiziana
Molecular Nutrition & Food Research, ISSN 1613-4125, 11/2015, Volume 59, Issue 11, pp. 2255 - 2266
Scope: Cystine-knot miniproteins are bioactive molecules with a broad range of potential therapeutic applications. Recently, it was demonstrated that two... 
Cystine‐knot protein | Angiogenesis | VEGFA signaling | Cell migration | Tomato fruit | Cystine-knot protein | PROTEIN | FOOD SCIENCE & TECHNOLOGY | PROSTATE-CANCER RISK | ANTITUMOR-ACTIVITY | POTATO CARBOXYPEPTIDASE INHIBITOR | FAMILY | SYNTHASE | CYCLOTIDES | LYCOPENE | EVOLUTION | SEQUENCE | Human Umbilical Vein Endothelial Cells | Nitric Oxide - biosynthesis | Receptors, Vascular Endothelial Growth Factor - physiology | Cystine-Knot Miniproteins - isolation & purification | Phosphorylation | Plant Proteins - pharmacology | Fruit - chemistry | Humans | Cells, Cultured | Angiogenesis Inhibitors - pharmacology | Zebrafish | Cell Movement - drug effects | Animals | Lycopersicon esculentum - chemistry | Proto-Oncogene Proteins c-akt - metabolism | Cystine-Knot Miniproteins - pharmacology | Endothelial Cells - physiology | Endothelial Cells - drug effects | Antioxidants | Cysteine | Fruit | Analysis | Nitric oxide | Vascular endothelial growth factor | Lycopene | Cystine | Index Medicus
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10. Full Text Grafting of thrombopoietin‐mimetic peptides into cystine knot miniproteins yields high‐affinity thrombopoietin antagonists and agonists
by Krause, Sebastian and Schmoldt, Hans‐Ulrich and Wentzel, Alexander and Ballmaier, Matthias and Friedrich, Karlheinz and Kolmar, Harald
FEBS Journal, ISSN 1742-464X, 01/2007, Volume 274, Issue 1, pp. 86 - 95
Thrombopoietin is the primary regulator of platelet production. We exploited two naturally occurring miniproteins of the inhibitor cystine knot family as... 
thrombopoietin mimetics | c‐Mpl receptor | cystine knot proteins | peptide agonist | thrombocytopenia | Thrombocytopenia | Cystine knot proteins | Peptide agonist | Thrombopoietin mimetics | c-Mpl receptor | BIOCHEMISTRY & MOLECULAR BIOLOGY | MONOCLONAL-ANTIBODY | MEGAKARYOCYTE GROWTH | RECEPTOR-BINDING DOMAIN | AGOUTI-RELATED PROTEIN | SQUASH INHIBITORS | NMR STRUCTURE | CHEMICAL-SYNTHESIS | STRUCTURAL SCAFFOLD | TRYPSIN-INHIBITOR | Cystine Knot Motifs | Peptides - chemistry | Humans | Cells, Cultured | Thrombopoietin - antagonists & inhibitors | Receptors, Thrombopoietin - metabolism | Recombinant Fusion Proteins - metabolism | Peptides - pharmacology | Thrombopoietin - agonists | Animals | Transfection | Recombinant Fusion Proteins - genetics | Mice | Megakaryocytes - cytology | Megakaryocytes - metabolism | Dimerization | Bone Marrow Cells - metabolism | Peptides | Proteins | Pharmacology | Antagonist drugs | Rodents | Index Medicus
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11. Full Text Tissue-Specific Expression of Head-to-Tail Cyclized Miniproteins in Violaceae and Structure Determination of the Root Cyclotide Viola hederacea Root cyclotide1
by Manuela Trabi and David J. Craik
The Plant Cell, ISSN 1040-4651, 8/2004, Volume 16, Issue 8, pp. 2204 - 2216
The plant cyclotides are a family of 28 to 37 amino acid miniproteins characterized by their head-to-tail cyclized peptide backbone and six absolutely... 
Trypsin inhibitors | Bracelets | Aerial roots | Plant anatomy | Disulfides | Plant roots | Cyclotides | Amino acids | Plants | Violas | CIRCULAR PROTEINS | CYSTINE KNOT MOTIF | OLDENLANDIA-AFFINIS | MOMORDICA-COCHINCHINENSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | KALATA B1 | PLANT SCIENCES | CELL BIOLOGY | 3-DIMENSIONAL STRUCTURE | CHASSALIA-PARVIFOLIA | PLANT CYCLOTIDES | MACROCYCLIC PEPTIDES | TRYPSIN-INHIBITOR | Disulfides - metabolism | Violaceae - anatomy & histology | Amino Acid Sequence | Plant Roots - metabolism | Violaceae - metabolism | Viola - metabolism | Models, Molecular | Molecular Sequence Data | Gene Expression Profiling | Peptides, Cyclic - metabolism | Tissue Distribution | Sequence Alignment | Violaceae - chemistry | Peptides, Cyclic - genetics | Plant Roots - chemistry | Protein Conformation | Viola - anatomy & histology | Viola - chemistry | Index Medicus
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12. Full Text Biochemical and MALDI-TOF mass spectrometric characterization of a novel native and recombinant cystine knot miniprotein from Solanum tuberosum subsp. andigenum cv. Churqueña
by Cotabarren, Juliana and Tellechea, Mariana Edith and Tanco, Sebastián Martín and Lorenzo, Julia and Garcia-Pardo, Javier and Avilés, Francesc Xavier and Obregón, Walter David
International Journal of Molecular Sciences, ISSN 1661-6596, 03/2018, Volume 19, Issue 3, p. 678
Cystine-knot miniproteins (CKMPs) are an intriguing group of cysteine-rich molecules that combine the characteristics of proteins and peptides. Typically,... 
Carboxypeptidase inhibitor | Andean potatoes | Protease | Solanum tuberosum | Cystine-knot miniproteins | Plant inhibitor | TOMATO FRUIT | plant inhibitor | PROTEIN | METALLOCARBOXYPEPTIDASE INHIBITOR | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | cystine-knot miniproteins | CHEMISTRY, MULTIDISCIPLINARY | PEPTIDE | POTATO CARBOXYPEPTIDASE INHIBITOR | ANNELID SABELLASTARTE-MAGNIFICA | protease | AMINO-ACID-SEQUENCE | carboxypeptidase inhibitor | CDNA CLONING | BINDING | Protease Inhibitors - analysis | Cystine-Knot Miniproteins - genetics | Recombinant Proteins | Protease Inhibitors - pharmacology | Protease Inhibitors - isolation & purification | Cattle | Plant Proteins - chemistry | Swine | Cystine-Knot Miniproteins - analysis | Cloning, Molecular | Cystine-Knot Miniproteins - chemistry | Solanum tuberosum - metabolism | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Proteomics - methods | Solanum tuberosum - genetics | Plant Proteins - isolation & purification | Amino Acid Sequence | Cystine-Knot Miniproteins - isolation & purification | Carboxypeptidases - antagonists & inhibitors | Protease Inhibitors - chemistry | Plant Proteins - analysis | Enzyme Activation - drug effects | Sequence Analysis, DNA | Plant Proteins - genetics | Animals | Solanum tuberosum - chemistry | Kinetics | Disulfide bonds | Peptides | Pharmacology | Molecular weight | Weight | Cystine | Proteins | Tubers | Organic chemistry | Spectrometry | Proteolysis | N-Terminus | Mass spectra | Scaffolds | Recombinant | Index Medicus
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13. Full Text The cyclic cystine knot miniprotein MCoTI-II is internalized into cells by macropinocytosis
by Greenwood, Kathryn P and Daly, Norelle L and Brown, Darren L and Stow, Jennifer L and Craik, David J
International Journal of Biochemistry and Cell Biology, ISSN 1357-2725, 2007, Volume 39, Issue 12, pp. 2252 - 2264
The cyclotides are macrocyclic knotted proteins characterized by a compact topology and exceptional stability. Accordingly it has been hypothesized that they... 
MCoTI-II | Protein engineering | Cyclotides | Cyclic cystine knot | Cell-penetrating peptides | CIRCULAR PROTEINS | STRUCTURAL MOTIF | MOMORDICA-COCHINCHINENSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | DRUG DESIGN | ANTIMICROBIAL PEPTIDES | CELL BIOLOGY | HUMAN IMMUNODEFICIENCY VIRUS | protein engineering | PLANT CYCLOTIDES | MACROCYCLIC PEPTIDES | cell-penetrating peptides | CYCLOTIDES KALATA B1 | cyclotides | cyclic cystine knot | PENETRATING PEPTIDES | Temperature | Cyclotides - chemistry | Lysosomes - chemistry | Humans | Molecular Sequence Data | Rhodamines - metabolism | Endosomes - metabolism | Membrane Proteins - analysis | Lysosomes - metabolism | Seeds - chemistry | Cyclotides - pharmacology | Lysosome-Associated Membrane Glycoproteins - analysis | Momordica - chemistry | Vesicular Transport Proteins - analysis | Dextrans - metabolism | Amino Acid Sequence | Cell Line | Cell Survival - drug effects | Biotinylation | Magnetic Resonance Spectroscopy | Macrophages - cytology | Sequence Homology, Amino Acid | Macrophages - metabolism | Animals | Pinocytosis - physiology | Cell Line, Tumor | Endosomes - chemistry | Cyclotides - metabolism | Microscopy, Fluorescence | Index Medicus
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14. Full Text Pharmacokinetically stabilized cystine knot peptides that bind Alpha-v-Beta-6 integrin with single-digit nanomolar affinities for detection of pancreatic cancer
by Kimura, Richard H and Teed, Robert and Hackel, Benjamin J and Pysz, Marybeth A and Chuang, Courtney Z and Sathirachinda, Ataya and Willmann, Jürgen K and Gambhir, Sanjiv S
Clinical Cancer Research, ISSN 1078-0432, 02/2012, Volume 18, Issue 3, pp. 839 - 849
Purpose: Detection of pancreatic cancer remains a high priority and effective diagnostic tools are needed for clinical applications. Many cancer cells... 
POSITRON-EMISSION-TOMOGRAPHY | OLDENLANDIA-AFFINIS | PROTEIN | RECOGNITION | ONCOLOGY | MOUTH-DISEASE | IN-VIVO | SQUAMOUS-CELL CARCINOMA | YEAST SURFACE DISPLAY | EXPRESSION | AFFIBODY | Bioengineering | Pancreatic Neoplasms - metabolism | Radiopharmaceuticals - pharmacokinetics | Biomarkers, Tumor - analysis | Pancreatic Neoplasms - diagnosis | Humans | Positron-Emission Tomography - methods | Cystine-Knot Miniproteins - chemical synthesis | Integrins - metabolism | Radiopharmaceuticals - chemical synthesis | Tissue Distribution | Animals | Mice, Nude | Antigens, Neoplasm - metabolism | Cystine-Knot Miniproteins - chemistry | Cystine-Knot Miniproteins - pharmacokinetics | Protein Binding | Female | Mice | Index Medicus
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