Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues
Reexamination Certificate
2007-08-14
2007-08-14
Andres, Janet L. (Department: 1649)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
C530S300000, C530S329000, C536S023500, C435S007210, C435S069100, C435S252300, C435S320100, C436S501000
Reexamination Certificate
active
11586208
ABSTRACT:
The invention provides human high affinity choline transporter polynucleotides and polypeptides and compositions comprising human high affinity choline transporter polynucleotides and polypeptides.
REFERENCES:
patent: 5756102 (1998-05-01), Paolettie et al.
Accession No. AB030947, published Feb. 3, 2000.
GenBank Accession No. CAC03717 published Aug. 16, 2000.
Alexander, et al., “Altering the antigenicity of proteins”, Proc. Natl. Acad. Sci. 89(3352-3356) 1992.
Guo-HH et al., “Protein tolerance to random amino acid change”, PNAS 101(25)9205-9210, 2004.
Bowie et al., “Deciphering the message in protein sequences: tolerance to amino acid substitutions”, Science 247:1306-1310, 1990.
Happe & Martin, “High Affinity Choline Transport Sites' Use of [3H]Hemicholinium-3 as a Quantitative Marker”, Neurochem, 60:1191-1201 (1993); Raven Press, Ltd. New York.
Rylett et al., “Affinity Labelling and Identification of the High-Affinity Choline Carrier from Synaptic Membranes of Torpedo Electromotor Nerve Terminals with [3H]Choline Mustard”. J. Neurochem 51:1942-5 (1988).
Knipper et al., “Isolation and Reconstitution of the High-Affinity Choline Carrier”, FEBS Lett. 245:235-237 (1989).
Knipper et al., “Hemicholinum-3 Biding Sites in the Nervous Tissue of Insects” Neurochem, Int. 14:211-215 (1989).
Knipper et al., “Purification and Reconstitution of the High Affinity Choline Transporter”, Biochem. Biophys. Acta, 1065:107-113 (1991).
O'Regan et al., Regulation of Hemicholinium-3 Sensitive Choline Uptake inXenopus laevisOocytes by the Second C2 Domain of Synaptotagmin., Mol. Brain Res. 32:135-42 (1994).
Mayser et al., “Primary Structure and Functional Expression of a Choline Transporter Expressed in the Rat Nervous System,” FEBS Lett. 305:31-36 (1992).
Apparsundaram et al., Molecular Cloning of a Human, Hemicholinium-3-Sensitive Choline Transporter, Biochem. Biophys. Res. Comm. 276:862-867 (2000).
Okuda et al., “Identification and characterization of the High-Affinity Choline Transporter”, Natl. Neurosci. 31:120-5 (2000).
Kanai & Hediger, Primary Structure and Functional Characterization of a high-affinity Glutamate Transporter, Nature, 360:467 (1992).
NCBI Accession No. AB030947, Okuda, et al., Feb. 3, 2000, National Center for Biotechnology Information, Bethesda, MD.
NCBI Accession No. AB030946, Okuda, et al., Feb. 3, 2000, National Center for Biotechnology Information, Bethesda, MD.
NCBI Accession No. BB422667; Hayashizaki, Jul. 16, 2000, National Center for Biotechnology Information, Bethesda, MD.
NCBI Accession No. BB192558; Hayashizaki, Jun. 30, 2000, National Center for Biotechnology Information, Bethesda, MD.
NCBI Accession No. AF276871; Apparsundaram, et al., Oct. 25, 2000, National Center for Biotechnology Information, Bethesda, MD.
NCBI Accession No. AJ401467; Weiland et al., Aug. 16, 2000; National Center for Biotechnology Information, Bethesda, MD.
NCBI Accession No. AJ401466; Weiland et al., Aug. 16, 2000; National Center for Biotechnology Information, Bethesda, MD.
Gu Yunrong
He Yun-Ju
Millard William James
Wu Dong-Hai
Andres Janet L.
Brannock Michael
McDonnell Boehnen & Hulbert & Berghoff LLP
University of Florida Research Foundation
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