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humans (6) 6
animals (5) 5
cell biology (4) 4
molecular sequence data (4) 4
amino acid sequence (3) 3
protein structure, tertiary (3) 3
abc transporter (2) 2
atp-binding cassette, sub-family b, member 1 - chemistry (2) 2
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endocytosis (2) 2
expression (2) 2
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1. Full Text Secretory lysosomes
by Griffiths, Gillian M and Blott, Emma J
Nature Reviews Molecular Cell Biology, ISSN 1471-0072, 02/2002, Volume 3, Issue 2, pp. 122 - 131
Regulated secretion of stored secretory products is important in many cell types. In contrast to professional secretory cells, which store their secretory... 
NATURAL-KILLER-CELLS | DENDRITIC CELLS | CELL-SURFACE EXPRESSION | MAST-CELLS | MEMBRANE-PROTEIN | CLASS-II MOLECULES | CA2+-DEPENDENT EXOCYTOSIS | CHEDIAK-HIGASHI-SYNDROME | CYTOTOXIC T-LYMPHOCYTES | SMALL GTPASE | CELL BIOLOGY | Membrane Fusion | Membrane Glycoproteins - metabolism | Humans | Exocytosis | Lysosomes - physiology | Biological Evolution | Fas Ligand Protein | Lysosomes - secretion | Endocytosis | Animals | Proteins - metabolism | Models, Biological | Genetic Diseases, Inborn - physiopathology
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2. Full Text Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail
by Blott, E.J and Bossi, G and Clark, R and Zvelebil, M and Griffiths, G.M
Journal of Cell Science, ISSN 0021-9533, 2001, Volume 114, Issue 13, pp. 2405 - 2416
Fas ligand (FasL) induces apoptosis through its cell surface receptor Fas. T lymphocytes and natural killer cells sort newly synthesised FasL to secretory... 
SH3 domain | Fas ligand | Proline-rich domain | Secretory lysosomes | Sorting motif | CELLS | ENDOCYTIC PATHWAY | DI-LEUCINE MOTIF | MEMBRANE | DOWN-REGULATION | GLYCOPROTEINS | IDENTIFICATION | CELL BIOLOGY | secretory lysosomes | proline-rich domain | PEPTIDES | sorting motif | EXPRESSION | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Humans | Membrane Glycoproteins - chemistry | Molecular Sequence Data | Proline | Cytoplasm - metabolism | Protein Transport | src Homology Domains | Fas Ligand Protein | Endocytosis | Membrane Glycoproteins - physiology | Animals | Lysosomes - metabolism | Models, Biological | Mice | Mutation
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3. Full Text Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation
by Zuccato, Elisabetta and Blott, Emma J and Holt, Oliver and Sigismund, Sara and Shaw, Michael and Bossi, Giovanna and Griffiths, Gillian M
Journal of Cell Science, ISSN 0021-9533, 01/2007, Volume 120, Issue 1, pp. 191 - 199
Fas ligand (FasL), a potent mediator of apoptosis expressed by CTL and NK cells, is sorted into the inner vesicles of secretory lysosomes for release via... 
Fas ligand | Multivesicular bodies | Phosphorylation | Ubiquitylation | Sorting | KINASE-ACTIVITY | NATURAL-KILLER-CELLS | DOWN-REGULATION | MICROVESICLES | HUMAN T-CELLS | CELL BIOLOGY | GROWTH-FACTOR RECEPTOR | multivesicular bodies | INTERNALIZATION | MULTIVESICULAR-BODY | sorting | ubiquitylation | phosphorylation | EXPRESSION | C-SRC | Fas Ligand Protein - metabolism | Humans | Secretory Vesicles - metabolism | Ubiquitin - metabolism | Molecular Sequence Data | Protein Transport - physiology | Proto-Oncogene Proteins - chemistry | Endosomes - metabolism | Proto-Oncogene Proteins c-fyn - genetics | Lysosomes - metabolism | src-Family Kinases - metabolism | Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - chemistry | Proto-Oncogene Proteins c-fyn - chemistry | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | Jurkat Cells | Rats | Proto-Oncogene Proteins - genetics | Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - metabolism | src Homology Domains - physiology | Animals | Fas Ligand Protein - chemistry | Proto-Oncogene Proteins c-fyn - metabolism | Signal Transduction - physiology | HeLa Cells | Leukemia, Basophilic, Acute | Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - genetics | Fas Ligand Protein - genetics | src-Family Kinases - chemistry | src-Family Kinases - genetics
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4. Cysteine-scanning mutagenesis provides no evidence for the extracellular accessibility of the nucleotide-binding domains of the multidrug resistance transporter P-glycoprotein
by Emma J. Blott and Christopher F. Higgins and Kenneth J. Linton
EMBO Journal, ISSN 0261-4189, 12/1999, Volume 18, Issue 23, p. 6800
  Multidrug resistance of cancer cells is, at least in part, conferred by overexpression of P-glycoprotein (P-gp), a member of the ATP-binding cassette (ABC)... 
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5. Full Text Cysteine‐scanning mutagenesis provides no evidence for the extracellular accessibility of the nucleotide‐binding domains of the multidrug resistance transporter P‐glycoprotein
by Blott, Emma J and Higgins, Christopher F and Linton, Kenneth J
The EMBO Journal, ISSN 0261-4189, 12/1999, Volume 18, Issue 23, pp. 6800 - 6808
Multidrug resistance of cancer cells is, at least in part, conferred by overexpression of P‐glycoprotein (P‐gp), a member of the ATP‐binding cassette (ABC)... 
multidrug resistance | cysteine‐scanning mutagenesis | P‐glycoprotein | ABC transporter | nucleotide‐binding domain | P-glycoprotein | Cysteine scanning mutagenesis | Nucleotide-binding domain | Multidrug resistance | cysteine-scanning mutagenesis | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SECA PROTEIN | IDENTIFICATION | ATP-BINDING | CELL BIOLOGY | TRANSMEMBRANE CONDUCTANCE REGULATOR | COLI PREPROTEIN TRANSLOCASE | CASSETTE TRANSPORTER | CYSTIC-FIBROSIS | PERIPLASM | nucleotide-binding domain | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Endopeptidases - metabolism | Mutagenesis, Site-Directed | Humans | ATP-Binding Cassette, Sub-Family B, Member 1 - metabolism | Models, Molecular | Molecular Sequence Data | Glycosylation | Cysteine - chemistry | Blotting, Western | Sequence Homology, Amino Acid | ATP-Binding Cassette Transporters - chemistry | Animals | Flow Cytometry | ATP-Binding Cassette Transporters - metabolism | Protein Binding | ATP-Binding Cassette, Sub-Family B, Member 1 - chemistry | Mice | 3T3 Cells
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6. Full Text Adaptor protein 3-dependent microtubule-mediated movement of lytic granules to the immunological synapse
by Booth, Sarah and Davies, E Graham and Blott, Emma and Griffiths, Gillian M and Stinchcombe, Jane C and Clark, Richard H and Day, Anna and Hamblin, Terry and Bossi, Giovanna
Nature Immunology, ISSN 1529-2908, 11/2003, Volume 4, Issue 11, pp. 1111 - 1120
Hermansky-Pudlak syndrome (HPS) is a rare autosomal recessive disease characterized by platelet defects and oculocutaneous albinism. Individuals with HPS type... 
BIOGENESIS | VESICLE FORMATION | BETA-3A SUBUNIT | CHEDIAK-HIGASHI-SYNDROME | LYSOSOME-RELATED ORGANELLES | COMPLEX AP-3 | IMMUNOLOGY | MANNOSE-6-PHOSPHATE RECEPTOR | HERMANSKY-PUDLAK-SYNDROME | CYTOTOXIC T-LYMPHOCYTES | AP-3 ADAPTER | Hermanski-Pudlak Syndrome - metabolism | Humans | Molecular Sequence Data | Adaptor Protein Complex beta Subunits | Adaptor Protein Complex 3 - metabolism | Antigens, CD - metabolism | Microtubules - metabolism | Proteins - metabolism | Tetraspanin 30 | Cytoplasmic Granules - ultrastructure | T-Lymphocytes, Cytotoxic - metabolism | Immune System - metabolism | Base Sequence | Cytoplasmic Granules - metabolism | Membrane Transport Proteins | Platelet Membrane Glycoproteins - metabolism | Adaptor Protein Complex 3 - genetics | Immune System - immunology | Adaptor Protein Complex 3 - deficiency | Mutation | T-Lymphocytes, Cytotoxic - ultrastructure
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7. Full Text Detailed characterization of cysteine‐less P‐glycoprotein reveals subtle pharmacological differences in function from wild‐type protein
by Taylor, Andrew M and Storm, Janet and Soceneantu, Loredana and Linton, Kenneth J and Gabriel, Mark and Martin, Catherine and Woodhouse, James and Blott, Emma and Higgins, Christopher F and Callaghan, Richard
British Journal of Pharmacology, ISSN 0007-1188, 12/2001, Volume 134, Issue 8, pp. 1609 - 1618
Subtle alterations in the coupling of drug binding to nucleotide hydrolysis were observed following mutation of all seven endogenous cysteine residues to... 
drug binding | ATP hydrolysis | cysteine scanning mutagenesis | recombinant expression | P‐glycoprotein | purification and reconstitution | Trichoplusia ni (High Five) cells | ABC transporter | P-glycoprotein | Recombinant expression | Purification and reconstitution | Drug binding | Cysteine scanning mutagenesis | CELLS | STIMULATED ATPASE ACTIVITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | HYDROLYSIS | VINBLASTINE | SCANNING MUTAGENESIS | REVERSE MULTIDRUG-RESISTANCE | DRUG-BINDING-SITES | NUCLEOTIDE | AZIDOPINE | TRANSPORT | PHARMACOLOGY & PHARMACY | Drug Resistance, Multiple | Humans | ATP-Binding Cassette, Sub-Family B, Member 1 - metabolism | Spodoptera - virology | Baculoviridae - genetics | Dihydropyridines - metabolism | Cysteine - genetics | Dose-Response Relationship, Drug | Adenosine Triphosphate - metabolism | Inhibitory Concentration 50 | ATP-Binding Cassette, Sub-Family B, Member 1 - chemistry | Cell Membrane - metabolism | Nicardipine - pharmacology | Azides - metabolism | Binding Sites | Cross-Linking Reagents - chemistry | Cells, Cultured | Adenosine Triphosphatases - metabolism | Serine - genetics | ATP-Binding Cassette, Sub-Family B, Member 1 - physiology | Photoaffinity Labels - metabolism | Animals | Mutagenesis | ATP-Binding Cassette, Sub-Family B, Member 1 - genetics | Vinblastine - pharmacology | Kinetics | Papers
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8. Full Text Under water-colored skies // Lititz, Terre Hill art shows attract plenty of potential patrons
by Zachariah Blott
Sunday News, 07/1997
  "We've come for about the last 25 years," said Donna and Al Olah of Lititz, who were at the Lititz show, "and it's always a nice day." "I'll tell you one... 
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