Functional
analysis of the C-terminal boundary of the
second nucleotide binding domain of the cystic
fibrosis transmembrane conductance regulator
and structural implications
Heteromultimerization
Modulates P2X Receptor Functions through
Participating Extracellular and C-terminal
Subdomains*
Taka-aki
Koshimizu†§,
Susumu Ueno¶, Akito Tanoue†,
Nobuyuki Yanagihara¶, Stanko
S. Stojilkovic||,
and Gozoh Tsujimoto†** From
the † Department
of Molecular and Cell Pharmacology, || Endocrinology
and Reproduction Research
Branch, NICHD, National Institutes
of Health, Bethesda, Maryland
20892 and the ¶ Department
of Pharmacology, University
of Occupational and Environmental
Health, Japan School of Medicine,
Tokyo 154-8567, Japan
Received for publication, May 29, 2002, and in revised form, September
16, 2002
J. Biol. Chem., Vol. 277, Issue 49, 46891-46899, December 6, 2002 ** To whom correspondence should be
addressed: Dept. of Molecular, Cell Pharmacology, National Research
Institute for Child Healthand Development, 3-35-31, Taishido,
Setagaya-Ku, Tokyo 154, Japan.Tel.: 81-3-3419-2476;
Fax: 81-3-3419-1252; E-mail: gtsujimoto@nch.go.jp. http://www.jbc.org/cgi/content/full/277/49/46891 http://www.jbc.org/cgi/reprint/277/49/46891.pdf
Novel ATPase
of SNF2-like Protein Family Interacts with
Androgen Receptor and Modulates Androgen-dependent
Transcription
Nathalie
Rouleau,* Andrii Domans'kyi,* Mati
Reeben,* Anu-Maarit Moilanen,* Kristina
Havas,† Zhigang
Kang,* Tom Owen-Hughes,† Jorma
J. Palvimo,*† and
Olli A. Jänne*§||
Biomedicum
Helsinki, Institute of Biomedicine, †Institute
of Biotechnology, and §Department
of Clinical Chemistry, University of Helsinki
and Helsinki University Central Hospital,
Fin-00014 Helsinki, Finland; and †Division
of Gene Regulation, The Wellcome Trust
Biocentre, University of Dundee, Dundee
DD1 5EH, Scotland
Submitted October 9, 2001; Revised February 19, 2002; Accepted
March 18, 2002
Monitoring Editor: Keith R. Yamamoto
Molecular Biology of the Cell, Vol. 13, Issue 6, 2106-2119, June 2002 http://www.molbiolcell.org/cgi/content/full/13/6/2106 http://www.molbiolcell.org/cgi/reprint/13/6/2106.pdfVolume
516, Issues 1-3, 10 April 2002, Pages 20-26
Corresponding Author Contact Information Corresponding
author. Fax: (32)-9-33 13597; E-mail: jan.gettemans@rug.ac.be
2001
The Yeast
a-factor Transporter Ste6p, a Member of the
ABC Superfamily, Couples ATP Hydrolysis to
Pheromone Export*
Christian
J. Ketchum†,
Walter K. Schmidt§,
Garnepudi V. Rajendrakumar†,
Susan Michaelis§,
and Peter C. Maloney†¶
From the † Department
of Physiology and the § Department
of Cell Biology and Anatomy, Johns Hopkins
University
School of Medicine,
Baltimore, Maryland 21205
Received for publication, January 29, 2001,
and in revised form, May 23, 2001
J. Biol. Chem., Vol. 276, Issue 31, 29007-29011,
August 3, 2001 ¶ To whom correspondence
should be addressed. Tel.: 410-955-8325; Fax:
410-955-4438; E-mail:
pmaloney@jhmi.edu.
Published, JBC Papers in Press, June 1, 2001
DOI 10.1074/jbc.M100810200 http://www.jbc.org/cgi/content/full/276/31/29007 http://www.jbc.org/cgi/reprint/276/31/29007.pdf
Evidence
for the Vectorial Nature of Drug (Substrate)-stimulated
ATP Hydrolysis by
Human P-glycoprotein
Zuben
E. Sauna, Melissa M. Smith, Marianna Müller,
and Suresh V. Ambudkar†
From the Laboratory of Cell Biology, Center
for Cancer Research, National Cancer Institute,
National Institutes of Health, Bethesda, Maryland
20892-4255
Received for publication, July 2, 2001, and
in revised form, July 11, 2001
J Biol Chem 2001 Sep 7;276(36):33301-4 † To
whom correspondence should be addressed: Tel.:
301-402-4178; E-mail: ambudkar@helix.nih.gov http://www.jbc.org/cgi/content/full/276/36/33301 http://www.jbc.org/cgi/reprint/276/36/33301.pdf
Characterization
of the nucleotide-binding capacity and the
ATPase activity of the PIP3-binding protein
JFC1
Functionally
Similar Vanadate-induced 8-Azidoadenosine
5'-[alpha -32P]Diphosphate-trapped Transition
State Intermediates of Human P-glycoprotein
Are Generated in the Absence and Presence
of ATP Hydrolysis
Zuben
E. Sauna, Melissa M. Smith, Marianna Müller,
and Suresh V. Ambudkar†
From the Laboratory of Cell Biology, Center
for Cancer Research, National Cancer Institute,
National Institutes of Health, Bethesda, Maryland
20892-4255
Received for publication, January 30, 2001
J. Biol. Chem., Vol. 276, Issue 24, 21199-21208,
June 15, 2001 † To whom correspondence should be addressed:
Laboratory of Cell Biology, Center for Cancer
Research, NCI, Bldg. 37, Rm. 1B-22, National
Institutes of Health, 37 Convent Dr., MD 20892-4255.
Tel.: 301-402-4178; Fax: 301-435-8188; E-mail: ambudkar@helix.nih.gov. http://www.pnas.org/cgi/content/full/98/20/11230 http://www.pnas.org/cgi/reprint/98/20/11230.pdf
Modulation of Multidrug Resistance Protein
1 (MRP1/ABCC1) Transport and ATPase Activities
by Interaction with Dietary Flavonoids
Elaine M. Leslie, Qingcheng Mao, Curtis J.
Oleschuk, Roger G. Deeley, and Susan P. C.
Cole
Department of Pharmacology and Toxicology (E.M.L.,
C.J.O., S.P.C.C.) and the Cancer Research Laboratories
(E.M.L., Q.M., C.J.O., R.G.D., S.P.C.C.), Queen's
University, Kingston, Ontario, Canada
Molecular Pharmacology Vol. 59, Issue 5, 1171-1180,
May 2001 Send reprint requests to: Dr. Susan P. C. Cole,
Cancer Research Laboratories, Room 328, Botterell
Hall, Queen's University, Kingston, Ontario,
Canada, K7L 3N6. E-mail: coles@post.queensu.ca http://molpharm.aspetjournals.org/cgi/content/full/59/5/1171 http://molpharm.aspetjournals.org/cgi/reprint/59/5/1171.pdf
Characterization of the Catalytic Cycle of
ATP Hydrolysis by Human P-glycoprotein
THE TWO ATP HYDROLYSIS EVENTS IN A SINGLE
CATALYTIC CYCLE ARE KINETICALLY SIMILAR BUT
AFFECT DIFFERENT FUNCTIONAL OUTCOMES
Zuben
E. Sauna and Suresh V. Ambudkar†
From the Laboratory of Cell Biology, Division
of Basic Sciences, NCI, National Institutes
of Health, Bethesda, Maryland 20892
Received for publication, December 14, 2000,
and in revised form, January 10, 2001 †To whom correspondence should be addressed:
Laboratory of Cell Biology, Division of Basic
Sciences, NCI, Bldg. 37, Rm. 1B-22, National
Institutes of Health, 37 Convent Dr., Bethesda,
MD 20892-4255. Tel.: 301-402-4178; Fax: 301-435-8188;
E-mail: ambudkar@helix.nih.gov
J. Biol. Chem., Vol. 276, Issue 15, 11653-11661,
April 13, 2001 http://www.jbc.org/cgi/content/full/276/15/11653 http://www.jbc.org/cgi/reprint/276/15/11653.pdf
Differential Interactions of Nucleotides
at the Two Nucleotide Binding Domains of
the Cystic Fibrosis Transmembrane Conductance
Regulator
Luba
Aleksandrov, April Mengos, Xiu-bao Chang,
Andrei Aleksandrov,
and John R. Riordan†
From the S. C. Johnson Medical Research Center, Mayo Clinic Scottsdale, Scottsdale,
Arizona 85259
Received for publication, January 18, 2001
J. Biol. Chem., Vol. 276, Issue 16, 12918-12923, April 20, 2001 † To whom correspondence should be addressed: Mayo Clinic Scottsdale,
S. C. Johnson Medical Research Center, 13400 E. Shea Blvd., Scottsdale, AZ
85259. Tel.: 480-301-6206; Fax: 480-301-7017; E-mail: riordan@mayo.edu http://www.jbc.org/cgi/content/full/276/16/12918 http://www.jbc.org/cgi/reprint/276/5/3492.pdf
Mapping of the ATP-binding Sites on Inositol
1,4,5-Trisphosphate Receptor Type 1 and Type
3 Homotetramers by Controlled Proteolysis
and Photoaffinity Labeling
Karlien
Maes§,
Ludwig Missiaen, Jan B. Parys¶,
Patrick De Smet||,
Ilse Sienaert||,
Etienne Waelkens**, Geert Callewaert†,
and Humbert De Smedt†
From the † Laboratorium
voor Fysiologie and the ** Laboratorium voor Biochemie, K.U.Leuven Campus
Gasthuisberg, Herestraat 49, B-3000 Leuven,
Belgium
Received for publication, July 11, 2000, and in revised form, October 11,
2000 § To whom correspondence should be addressed: Tel.: 32-16-345-736; Fax:
32-16-345-991; E-mail: Karlien.Maes@med.kuleuven.ac.be
J. Biol. Chem., Vol. 276, Issue 5, 3492-3497, February 2, 2001 http://www.jbc.org/cgi/content/full/276/5/3492 http://www.jbc.org/cgi/reprint/276/16/12918.pdf
Purification
and characterization of acyl-acyl carrier
protein synthetase from oleaginous yeast
and its role in triacylglycerol biosynthesis
Functional
Analysis of a Mutant Sulfonylurea Receptor,
SUR1-R1420C, That Is Responsible
for Persistent Hyperinsulinemic Hypoglycemia
of Infancy
Michinori
Matsuo†,
Stefan Trapp§,
Yukio Tanizawa¶,
Noriyuki Kioka†,
Teruo Amachi†,
Yoshitomo Oka¶,
Frances M. Ashcroft§,
and Kazumitsu Ueda†||
From the † Department
of Physiology and the § Department of Cell Biology and Anatomy,
Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
Received for publication, January 29, 2001, and in revised form, May 23,
2001
J. Biol. Chem., Vol. 276, Issue 31, 29007-29011, August 3, 2001 ¶ To
whom correspondence should be addressed.
Tel.: 410-955-8325; Fax: 410-955-4438;
E-mail: pmaloney@jhmi.edu.
Published, JBC Papers in Press, June 1, 2001 DOI 10.1074/jbc.M100810200 http://www.jbc.org/cgi/content/full/275/52/41184 http://www.jbc.org/cgi/reprint/275/52/41184.pdf
Comparison
of the Functional Characteristics of the
Nucleotide Binding Domains of Multidrug Resistance
Protein 1
Mian
Gao†§¶, Heng-Ran Cui†,
Douglas W. Loe†,
Caroline E. Grant†,
Kurt C. Almquist†,
Susan P. C. Cole†§||,
and Roger G. Deeley†§**
From the † Cancer
Research Laboratories and the § Department of Pathology, Queen's
University, Kingston, Ontario K7L 3N6, Canada
** Stauffer Research Professor of Queen's University.
To whom correspondence and reprint requests
should be addressed: Cancer Research Laboratories,
Rm. A315, Botterell Hall, Queen's University,
Kingston, Ontario K7L 3N6, Canada. Tel.: 613-533-2981;
Fax: 613-533-6830.
J Biol Chem, Vol. 275, Issue 17, 13098-13108,
April 28, 2000 http://www.jbc.org/cgi/content/full/275/17/13098 http://www.jbc.org/cgi/reprint/275/17/13098.pdf
Allosteric
Interactions between the Two Non-equivalent
Nucleotide Binding Domains of Multidrug Resistance
Protein MRP1
Yue-xian
Hou, Liying Cui, John R. Riordan, and Xiu-bao
Chang†
From the Mayo Foundation, S. C. Johnson Medical
Research Center, Mayo Clinic Scottsdale, Scottsdale,
Arizona 85259
Received for publication, February 9, 2000,
and in revised form, April 6, 2000 † To whom correspondence should be addressed:
Mayo Clinic Scottsdale, S. C. Johnson Medical
Research Center, 13400 E. Shea Blvd., Scottsdale,
AZ 85259. Tel.: 480-301-6206; Fax: 480-301-7017;
E-mail: xbchang@mayo.edu.
J. Biol. Chem., Vol. 275, Issue 27, 20280-20287,
July 7, 2000 http://www.jbc.org/cgi/content/full/275/27/20280 http://www.jbc.org/cgi/reprint/275/27/20280.pdf
Different
Binding Properties and Affinities for ATP
and ADP among Sulfonylurea Receptor Subtypes,
SUR1, SUR2A, and SUR2B
Michinori
Matsuo, Kouichi Tanabe, Noriyuki Kioka,
Teruo Amachi, and Kazumitsu Ueda†
From the Laboratory of Biochemistry, Division
of Applied Life Sciences, Kyoto University
Graduate School of Agriculture, Kyoto 606-8502,
Japan
Received for publication, June 5, 2000, and
in revised form, July 7, 2000 † To whom correspondence should be addressed:
Laboratory of Biochemistry, Division of Applied
Life Sciences, Kyoto University Graduate School
of Agriculture, Kyoto 606-8502, Japan. Tel.:
81-75-753-6105; Fax: 81-75-753-6104; E-mail:
uedak@kais.kyoto-u.ac.jp
J. Biol. Chem., Vol. 275, Issue 37, 28757-28763,
September 15, 2000 http://www.jbc.org/cgi/content/full/275/37/28757 http://www.jbc.org/cgi/reprint/275/37/28757.pdf
Cloning,
characterization and tissue distribution
of the rat ATP-binding cassette (ABC) transporter
ABC2/ABCA2
Li-Xia ZHAO*, Cheng-Ji ZHOU†,
Arowu TANAKA‡, Masanori NAKATA*, Takahiro HIRABAYASHI§,
Teruo AMACHI‡, Seiji SHIODA†, Kazumitsu
UEDA‡ and Nobuya INAGAKI*1
*Department of Physiology, Akita University
School of Medicine, 1-1-1, Hondo, Akita 010-8543,
Japan, †Department of Anatomy, Showa
University School of Medicine, Tokyo 142-8555,
Japan, ‡Laboratory of Biochemistry, Division
of Applied Life Sciences, Kyoto University
Graduate School of Agriculture, Kyoto 606-8502,
Japan, and §Center for Biotechnology,
Showa University, Tokyo 142-8555, Japan 1 To whom correspondence should be addressed
E-mail:
uedak@kais.kyoto-u.ac.jp
Biochem. J. (2000) 350 (865–872) http://www.biochemj.org/bj/350/0865/bj3500865.htm http://www.biochemj.org/bj/350/0865/3500865.pdf
MDR3 P-glycoprotein, a Phosphatidylcholine
Translocase, Transports Several Cytotoxic
Drugs and Directly Interacts with Drugs as
Judged by Interference with Nucleotide Trapping
Alexander J. Smith††§, Ardy van
Helvoort††¶,
Gerrit van Meer¶||,
Katalin Szabó**††, Ervin
Welker**††, Gergely Szakács**,
András Váradi††,
Balázs Sarkadi**§§,
and Piet Borst††¶¶
From the †† Division of Molecular Biology
and Center for Biomedical Genetics, The Netherlands
Cancer Institute, Plesmanlaan 121, 1066 CX
Amsterdam, The Netherlands, the || Laboratory
of Cell Biology and Histology, Academic Medical
Center, University of Amsterdam, Amsterdam,
The Netherlands, ** National Institute of Haematology
and Immunology, Membrane Research Group of
the Hungarian Academy of Sciences, H-1113 Budapest,
Hungary, †† Institute of Enzymology,
Biological Research Center, Hungarian Academy
of Sciences, H-1113 Budapest, Hungary, and ¶ Department
of Cell Biology, Faculty of Medicine and Institute
of Biomembranes, Universiteit Utrecht, 3584
CX Utrecht, The Netherlands ¶¶ To whom correspondence should be addressed:
Division of Molecular Biology, The Netherlands
Cancer Inst., Plesmanlaan 121, 1066 CX Amsterdam,
The Netherlands. Tel.: 31-20-512-2880; Fax:
31-20-669-1383; E-mail: pborst@nki.nl.
Received for publication, November 8, 1999,
and in revised form, April 20, 2000
J. Biol. Chem., Vol. 275, Issue 31, 23530-23539,
August 4, 2000 http://www.jbc.org/cgi/content/full/275/31/23530 http://www.jbc.org/cgi/reprint/275/31/23530.pdf
The Hydrophilic N-terminal Domain Complements
the Membrane-anchored C-terminal Domain of
the Sensor Kinase KdpD of Escherichia coli
Ralf Heermann†, Karlheinz Altendorf, and Kirsten Jung†§
From the Universität Osnabrück, Fachbereich
Biologie/Chemie, Abteilung Mikrobiologie, D-49069
Osnabrück, Germany
Received for publication, January 6, 2000,
and in revised form, March 10, 2000 § To whom correspondence should be addressed:
Universität Osnabrück, Fachbereich
Biologie/Chemie, Abteilung Mikrobiologie, Barbarastr.
11, D-49069 Osnabrück, Germany. Tel.:
49-541-969-2276; Fax: 49-541-969-2870; E-mail:
jung_k@biologie.uni-osnabrueck.de http://www.biochemj.org/bj/350/0865/bj3500865.htm http://www.jbc.org/cgi/reprint/275/22/17080.pdf
Identification of ecto-PKC on surface of
human platelets: role in maintenance of latent
fibrinogen receptors
Anna Babinska1, Michael V. Hogan2,*, Tomasz
Sobocki1,*, Malgorzata B. Sobocka1, Yigal H.
Ehrlich2, and Elizabeth Kornecki1 1 Department of Anatomy and Cell Biology, State
University of New York, Health Science Center
at Brooklyn, Brooklyn 11203; and the 2 College
of Staten Island/Institute for Basic Research
Center for Developmental Neuroscience, City
University of New York, College of Staten Island,
Staten Island, New York 11314
Address for reprint requests and other correspondence:
E. Kornecki, Dept. of Anatomy and Cell Biology,
450 Clarkson Ave., SUNY Health Science Center
at Brooklyn, Brooklyn, NY 11203. E-mail: ekornecki@netmail.hscbklyn.edu
Am J Physiol Heart Circ Physiol 278: H2008-H2019,
2000; Vol. 278, Issue 6, H2008-H2019, June
2000 http://ajpheart.physiology.org/cgi/content/full/278/6/H2008 http://ajpheart.physiology.org/cgi/reprint/278/6/H2008.pdf
Nonequivalent
Nucleotide Trapping in the Two Nucleotide
Binding Folds of the Human Multidrug Resistance
Protein MRP1
Koh Nagata, Masahito Nishitani, Michinori
Matsuo, Noriyuki Kioka, Teruo Amachi, and Kazumitsu
Ueda†
From the Laboratory of Biochemistry, Division
of Applied Life Sciences, Kyoto University
Graduate School of Agriculture, Kyoto 606-8502,
Japan † To whom correspondence should be addressed:
Laboratory of Biochemistry, Dept. of Applied
Life Science, Kyoto University Graduate School
of Agriculture, Kyoto 606-8502, Japan. Tel.:
81-75-753-6105; Fax: 81-75-753-6104; E-mail:
uedak@kais.kyoto-u.ac.jp
Received for publication, January 31, 2000,
and in revised form, March 3, 2000
J. Biol. Chem., Vol. 275, Issue 23, 17626-17630,
June 9, 2000 http://www.jbc.org/cgi/content/full/275/23/17626#FN152 http://www.jbc.org/cgi/reprint/275/23/17626.pdf
Analysis
of a nucleotide-binding site of 5-lipoxygenase
by affinity labelling: binding characteristics
and amino acid sequences
Ying-Yi ZHANG*1, Tove HAMMARBERG†,
Olof RADMARK†, Bengt SAMUELSSON†,
Carol F. NG‡2, Colin D. FUNK§ and
Joseph LOSCALZO*
*Whitaker Cardiovascular Institute, Boston
University School of Medicine, 715 Albany Street,
Boston, MA 02118, U.S.A., †Department
of Medical Biochemistry and Biophysics, Karolinska
Institute, S-17177 Stockholm, Sweden, ‡Department
of Cell Biology, University of Medicine and
Dentistry of New Jersey, Stratford, NJ 08084,
U.S.A., and §Department of Pharmacology,
Center for Experimental Therapeutics, University
of Pennsylvania, Philadelphia, PA 19104, U.S.A. 1 To
whom correspondence should be addressed E-mail: yyzhang@bu.edu
Biochem. J. (2000) 351 (697–707) http://www.biochemj.org/bj/351/0697/bj3510697.htm http://www.biochemj.org/bj/351/0697/3510697.pdf
Different
binding properties and affinities for ATP
and ADP among sulfonylurea receptor subtypes,
SUR1, SUR2A, and SUR2B
J. Biol. Chem, 10:1074
Submitted on June 5, 2000; Revised on July 7, 2000; Accepted on July 11, 2000
Michinori Matsuo, Kouichi Tanabe, Noriyuki Kioka, Teruo Amachi, and Kazumitsu
Ueda
Kyoto University Graduate School of Agriculture, Laboratory of Biochemistry,
Kyoto 606-8502 http://www.jbc.org/cgi/content/abstract/M004818200
Nonequivalent
Nucleotide Trapping in the Two Nucleotide
Binding Folds of the Human Multidrug Resistance
Protein MRP1*
J. Biol. Chem., Vol. 275, Issue 23, 17626-17630,
June 9, 2000
Koh Nagata, Masahito Nishitani, Michinori Matsuo,
Noriyuki Kioka, Teruo Amachi, and Kazumitsu
Ueda
From the Laboratory of Biochemistry, Division
of Applied Life Sciences, Kyoto University
Graduate School of Agriculture, Kyoto 606-8502,
Japan http://www.jbc.org/cgi/content/abstract/275/23/17626
Using photolabile ligands in drug discovery
and development
G. Dormán and
G.D. Prestwich
Trends in Biotechnology 2000, 18:64-77
ComGenex, Budapest, 1027 Bem rkp. 33-34, Hungary
The University of Utah, Department of Medicinal
Chemistry, Salt Lake City, UT 84112-5820, USA. http://reviews.bmn.com/browse/areas/record?uid=TIBTECH.etd00219
Elucidation
of protein–protein interactions
using chemical cross-linking or label transfer
techniques
ATP Binding
Properties of the Nucleotide-binding Folds
of SUR1
Michinori
Matsuo, Noriyuki Kioka, Teruo Amachi, and
Kazumitsu Ueda†
From the Laboratory of Biochemistry, Division
of Applied Life Sciences, Kyoto University
Graduate School of Agriculture, Kyoto 606-8502,
Japan † To whom correspondence should be addressed.
Tel.: 81-75-753-6105; Fax: 81-75-753-6104;
E-mail: uedak@kais.kyoto-u.ac.jp.
J Biol Chem, Vol. 274, Issue 52, 37479-37482,
December 24, 1999 http://www.jbc.org/cgi/content/full/274/52/37479 http://www.jbc.org/cgi/reprint/274/52/37479.pdf
Intrinsic
Nucleoside Diphosphate Kinase-like Activity
Is a Novel Function of the 20 S Proteasome
Photoaffinity
Labeling of Wild-type and Mutant Forms of
the Yeast V-ATPase A Subunit by 2-Azido-[32P]ADP
Kathryn J.
MacLeod†,
Elena Vasilyeva†,
Keith Merdek†,
Pia D. Vogel§,
and Michael Forgac†¶
From the † Department of Physiology, Tufts
University School of Medicine, Boston, Massachusetts
02111 and the § Fachbereich
Chemie/Abteilung Biochemie, Universitaet Kaiserslautern,
D-67653
Kaiserslautern, Germany
J Biol Chem, Vol. 274, Issue 46, 32869-32874,
November 12, 1999 http://www.jbc.org/cgi/content/full/274/46/32869 http://www.jbc.org/cgi/reprint/274/46/32869.pdf
Activation of Go-proteins by Membrane Depolarization
Traced by in Situ Photoaffinity Labeling
of Galpha o-proteins with [32P]GTP-azidoanilide
J Biol Chem, Vol. 274, Issue 11, 7431-7440
March 12, 1999
Yosef Anis, Bernd Nürnberg§, Leonid
Visochek, Nachum Reiss¶,
Zvi Naor¶,
and Malka Cohen-Armon
From the Department of Physiology and The Cardiac
Research Institute, Sackler School of Medicine
and ¶ Department
of Biochemistry, George S. Wise Faculty of
Life Sciences, Tel-Aviv
University, 69978 Tel-Aviv, Israel and § Institut
fur Pharmakologie, Freie Universitat Berlin,
Thielallee 67-73, D-14195 Berlin, Federal Republic
of Germany http://www.jbc.org/cgi/content/abstract/274/11/7431
Metal-dependent
nucleotide binding to the Escherichia coli
rotamase SlyD
Thomas MITTERAUER*, Christian
NANOFF*, Horst AHORN†, Michael FREISSMUTH*1 and Martin HOHENEGGER*
Biochem. J. (1999) 342 (33–39)
*Institute of Pharmacology, University of Vienna,
Währinger Str. 13a, A-1090 Vienna, Austria,
and †Department of Biochemistry, Ernst
Boehringer Institut für Arzneimittelforschung,
A-1120 Vienna, Austria http://www.biochemj.org/bj/342/0033/bj3420033.htm http://www.biochemj.org/bj/342/0033/3420033.pdf
Purification of the human apical conjugate
export pump MRP2. Reconstitution and functional
characterization as substrate-stimulated
ATPase
Wolfgang Hagmann1,
Anne T. Nies1, Jörg
König1, Manfred Frey2, Hanswalter
Zentgraf2 and Dietrich Keppler1 1Division of Tumor Biochemistry and 2Applied
Tumorvirology Program, Deutsches Krebsforschungszentrum,
Heidelberg, Germany
Correspondence to W. Hagmann, Division of Tumor
Biochemistry, Deutsches Krebsforschungszentrum,
D-69120 Heidelberg, Germany. Fax: + 49 6221
422402, Tel.: + 49 6221 422405, E-mail: Hagmann@DKFZ-Heidelberg.de
European Journal of Biochemistry Volume 265
Issue 1 Page 281 - October (I) 1999 http://www.blackwell-synergy.com/links/doi/10.1046/j.1432-1327.1999.00735.x/full/ View/Print
PDF article (619K)
The
role of lysine 185 in the Kir6.2 subunit
of the ATP-sensitive channel in channel inhibition
by ATP
Frank
Reimann, Timothy J. Ryder, Stephen J. Tucker
and Frances M. Ashcroft
University Laboratory of Physiology, Parks Road, Oxford OX1 3PT, UK
Metal-dependent
nucleotide binding to the Escherichia
coli rotamase SlyD
Thomas
MITTERAUER*, Christian NANOFF*, Horst AHORN†,
Michael FREISSMUTH*1
and Martin
HOHENEGGER*
*Institute of Pharmacology,
University of Vienna, Währinger Str. 13a, A-1090
Vienna, Austria, and †Department of Biochemistry,
Ernst Boehringer Institut für Arzneimittelforschung,
A-1120 Vienna, Austria 1 To whom correspondence should
be addressed Email: michael.freissmuth@univie.ac.at
Biochem. J. (1999) Aug
15;342 ( Pt 1):33-9 http://www.biochemj.org/bj/342/0033/bj3420033.htm http://www.biochemj.org/bj/342/0033/3420033.pdf
Monoclonal
Antibodies That Inhibit the Transport Function
of the 190-kDa Multidrug Resistance
Protein, MRP
LOCALIZATION
OF THEIR EPITOPES TO THE NUCLEOTIDE-BINDING
DOMAINS OF THE PROTEIN*
David
R. Hipfner†§¶,
Qingcheng Mao§, Wei Qiu§,
Elaine M. Leslie§**††,
Mian Gao†§§§,
Roger G. Deeley†§¶¶,
and Susan P. C. Cole†§**|| From the Departments of † Pathology
and ** Pharmacology and Toxicology
and the § Cancer Research Laboratories,
Queen's University, Kingston, Ontario K7L 3N6,
Canada || Senior Scientist
of Cancer Care Ontario. To whom correspondence
should be addressed: Cancer Research Laboratories,
BotterellHall, Queen's University, Kingston, Ontario K7L
3N6, Canada. Tel.:613-533-6507; Fax: 613-533-6830; E-mail: coles@post.queensu.ca.
J
Biol Chem, Vol. 274, Issue 22, 15420-15426,
May 28, 1999 http://www.jbc.org/cgi/content/full/274/22/15420 http://www.jbc.org/cgi/reprint/274/22/15420.pdf
The 3 Adrenergic
Receptor Activates Mitogen-activated Protein
Kinase in Adipocytes
through a Gi-dependent Mechanism*
Katalin Szabó†§,
Gergely Szakács†, Tamás
Hegedűs†,
and Balázs
Sarkadi†¶
From the † National
Institute of Haematology and Immunology, Membrane
Research Group of
the Hungarian Academy of Sciences and the § Institute
of Enzymology, Biological Research Center,
Hungarian Academy of Sciences, H-1113 Budapest,
Hungary ¶ Howard
Hughes International Research Scholar. To whom correspondence should be addressed:
National Institute of Haematology and Immunology,
1113 Budapest, Daróczi u. 24, Hungary.
Tel.:/Fax: 36-1-372-4353; E-mail: b.sarkadi@ohvi.hu.
J Biol Chem, Vol. 274, Issue 18, 12209-12212,
April 30, 1999 http://www.jbc.org/cgi/content/full/274/18/12209 http://www.jbc.org/cgi/reprint/274/18/12209.pdf
Direct
Photoaffinity Labeling of the Kir6.2 Subunit
of the ATP-sensitive K+ Channel by 8-Azido-ATP*
J Biol Chem, Vol. 274, Issue
7, 3931-3933, February 12, 1999
Kouichi Tanabe†,
Stephen J. Tucker§¶,
Michinori Matsuo, Peter
Proks§,
Frances M. Ashcroft§,
Susumu Seinoparallel, Teruo Amachi,
and Kazumitsu Ueda**
From the Laboratory of Biochemistry, Division of Applied Life Sciences, Kyoto
University Graduate School of Agriculture, Kyoto 606-8502, Japan, the § University
Laboratory of Physiology, Oxford OX1 3PT, United Kingdom, and the || Department
of Molecular Medicine, Chiba University Graduate School of Medicine, Chuo-ku,
Chiba 260-8670, Japan http://www.jbc.org/cgi/content/full/274/7/3931
Cooperative binding of ATP and MgADP in the
sulfonylurea receptor is modulated by glibenclamide
Kazumitsu Ueda*,†,
Jun Komine*, Michinori Matsuo*, Susumu
Seino†,
and Teruo Amachi*
* Laboratory of Biochemistry, Division of Applied
Life Sciences, Kyoto University Graduate School
of Agriculture, Kyoto 606-8502, Japan; and Department
of Molecular Medicine, Chiba University Graduate
School of Medicine, Chuo-ku,
Chiba 260-8670, Japan
Communicated by Ira Pastan, National Cancer
Institute, Bethesda, MD, December 2, 1998 (received
for review October 24, 1998)
dagger To whom reprint requests should be addressed.
E-mail: uedak@kais.kyoto-u.ac.jp
Proc Natl Acad Sci U S A 1999 Feb 16;96(4):1268-72 http://www.pnas.org/cgi/content/full/96/4/1268 http://www.pnas.org/cgi/reprint/96/4/1268.pdf
Developing a snapshot of the ATP binding domain(s)
of Aminoglycoside Phosphotransferases
Anti-cancer drugs and glutathione stimulate vanadate-induced trapping of
nucleotide in multidrug resistance-associated protein (MRP)
Yoshitomo Taguchi, Aya Yoshida,
Yuko Takada, Tohru Komano and Kazumitsu Ueda*
E-mail: uedak@kais.kyoto-u.ac.jp
Laboratory of Biochemistry, Department of Agricultural
Chemistry, Kyoto University, Kyoto 606-01,
Japan
Received 11 November 1996; revised 25 November
1996. Available online 30 March 1998. FEBS
LettersVolume
401, Issue 1, 13 January
1997, Pages 11-14 http://www.sciencedirect.com/scienceuserid
1993
Photoaffinity labeling of ribulose-1,5-bisphosphate
carboxylase/oxygenase activase with ATP gamma-benzophenone.
Identification of the ATP gamma-phosphate
binding domain.
32P]GTP-azidoanilide
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3 Adrenergic
Receptor Activates Mitogen-activated Protein
Kinase in Adipocytes
through a Gi-dependent Mechanism*
Department
of Molecular Medicine, Chiba University Graduate
School of Medicine, Chuo-ku,
Chiba 260-8670, Japan