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1
Mitochondrial Phosphoenolpyruvate Carboxykinase (PEPCK-M) Is a Pro-survival, Endoplasmic Reticulum (ER) Stress Response Gene Involved in Tumor Cell Adaptation to Nutrient Availability
Mitochondrial Phosphoenolpyruvate Carboxykinase (PEPCK-M) Is a Pro-survival, Endoplasmic Reticulum (ER) Stress Response Gene Involved in Tumor Cell Adaptation to Nutrient Availability
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Mitochondrial Phosphoenolpyruvate Carboxykinase (PEPCK-M) Is a Pro-survival, Endoplasmic Reticulum (ER) Stress Response Gene Involved in Tumor Cell Adaptation to Nutrient Availability

The Journal of biological chemistry, 2014-08, Vol.289 (32), p.22090-22102 [Peer Reviewed Journal]

2014 © 2014 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2014 by The American Society for Biochemistry and Molecular Biology, Inc. ;(c) American Society for Biochemistry and Molecular Biology, 2014 info:eu-repo/semantics/openAccess ;2014 by The American Society for Biochemistry and Molecular Biology, Inc. 2014 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M114.566927 ;PMID: 24973213

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2
Cannabinoid Receptors CB1 and CB2 Form Functional Heteromers in Brain
Cannabinoid Receptors CB1 and CB2 Form Functional Heteromers in Brain
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Cannabinoid Receptors CB1 and CB2 Form Functional Heteromers in Brain

The Journal of biological chemistry, 2012-06, Vol.287 (25), p.20851-20865 [Peer Reviewed Journal]

2012 © 2012 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;(c) American Society for Biochemistry and Molecular Biology, 2012 info:eu-repo/semantics/openAccess ;2012 by The American Society for Biochemistry and Molecular Biology, Inc. 2012 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M111.335273 ;PMID: 22532560

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3
Targeting CB2-GPR55 Receptor Heteromers Modulates Cancer Cell Signaling
Targeting CB2-GPR55 Receptor Heteromers Modulates Cancer Cell Signaling
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Targeting CB2-GPR55 Receptor Heteromers Modulates Cancer Cell Signaling

The Journal of biological chemistry, 2014-08, Vol.289 (32), p.21960-21972 [Peer Reviewed Journal]

2014 © 2014 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2014 by The American Society for Biochemistry and Molecular Biology, Inc. ;(c) American Society for Biochemistry and Molecular Biology, 2014 info:eu-repo/semantics/openAccess ;2014 by The American Society for Biochemistry and Molecular Biology, Inc. 2014 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M114.561761 ;PMID: 24942731

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4
Annexin A6 and Late Endosomal Cholesterol Modulate Integrin Recycling and Cell Migration
Annexin A6 and Late Endosomal Cholesterol Modulate Integrin Recycling and Cell Migration
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Annexin A6 and Late Endosomal Cholesterol Modulate Integrin Recycling and Cell Migration

The Journal of biological chemistry, 2016-01, Vol.291 (3), p.1320-1335 [Peer Reviewed Journal]

2016 © 2016 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2016 by The American Society for Biochemistry and Molecular Biology, Inc. ;(c) American Society for Biochemistry and Molecular Biology, 2016 info:eu-repo/semantics/openAccess ;2016 by The American Society for Biochemistry and Molecular Biology, Inc. 2016 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M115.683557 ;PMID: 26578516

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5
Interactions between Intracellular Domains as Key Determinants of the Quaternary Structure and Function of Receptor Heteromers
Interactions between Intracellular Domains as Key Determinants of the Quaternary Structure and Function of Receptor Heteromers
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Interactions between Intracellular Domains as Key Determinants of the Quaternary Structure and Function of Receptor Heteromers

The Journal of biological chemistry, 2010-08, Vol.285 (35), p.27346-27359 [Peer Reviewed Journal]

2010 © 2010 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;(c) American Society for Biochemistry and Molecular Biology, 2010 info:eu-repo/semantics/openAccess ;2010 by The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M110.115634 ;PMID: 20562103

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6
Coaggregation, cointernalization, and codesensitization of adenosine A2A receptors and dopamine D2 receptors
Coaggregation, cointernalization, and codesensitization of adenosine A2A receptors and dopamine D2 receptors
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Coaggregation, cointernalization, and codesensitization of adenosine A2A receptors and dopamine D2 receptors

The Journal of biological chemistry, 2002-05, Vol.277 (20), p.18091-18097 [Peer Reviewed Journal]

(c) American Society for Biochemistry and Molecular Biology, 2002 info:eu-repo/semantics/openAccess ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M107731200 ;PMID: 11872740

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7
Coregulator Control of Androgen Receptor Action by a Novel Nuclear Receptor-binding Motif
Coregulator Control of Androgen Receptor Action by a Novel Nuclear Receptor-binding Motif
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Coregulator Control of Androgen Receptor Action by a Novel Nuclear Receptor-binding Motif

The Journal of biological chemistry, 2014-03, Vol.289 (13), p.8839-8851 [Peer Reviewed Journal]

2014 © 2014 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;(c) American Society for Biochemistry and Molecular Biology, 2014 info:eu-repo/semantics/openAccess ;2014 by The American Society for Biochemistry and Molecular Biology, Inc. 2014 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M113.534859 ;PMID: 24523409

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8
Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets
Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets
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Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets

The Journal of biological chemistry, 2005-06, Vol.280 (22), p.21522-21530 [Peer Reviewed Journal]

(c) American Society for Biochemistry and Molecular Biology, 2005 info:eu-repo/semantics/openAccess ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M502255200 ;PMID: 15799962

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9
Cellular Redox Systems Impact the Aggregation of Cu,Zn Superoxide Dismutase Linked to Familial Amyotrophic Lateral Sclerosis
Cellular Redox Systems Impact the Aggregation of Cu,Zn Superoxide Dismutase Linked to Familial Amyotrophic Lateral Sclerosis
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Cellular Redox Systems Impact the Aggregation of Cu,Zn Superoxide Dismutase Linked to Familial Amyotrophic Lateral Sclerosis

The Journal of biological chemistry, 2016-08, Vol.291 (33), p.17197-17208 [Peer Reviewed Journal]

2016 © 2016 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2016 by The American Society for Biochemistry and Molecular Biology, Inc. ;(c) American Society for Biochemistry and Molecular Biology, 2016 info:eu-repo/semantics/openAccess ;2016 by The American Society for Biochemistry and Molecular Biology, Inc. 2016 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;ISSN: 1083-351X ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M115.708230 ;PMID: 27261461

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10
Interactions between Calmodulin, Adenosine A2A, and Dopamine D2 Receptors
Interactions between Calmodulin, Adenosine A2A, and Dopamine D2 Receptors
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Interactions between Calmodulin, Adenosine A2A, and Dopamine D2 Receptors

The Journal of biological chemistry, 2009-10, Vol.284 (41), p.28058-28068 [Peer Reviewed Journal]

2009 © 2009 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;(c) American Society for Biochemistry and Molecular Biology, 2009 info:eu-repo/semantics/openAccess ;2009 by The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;ISSN: 1083-351X ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M109.034231 ;PMID: 19632986

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11
The Human Apolipoprotein AV Gene Is Regulated by Peroxisome Proliferator-activated Receptor-α and Contains a Novel Farnesoid X-activated Receptor Response Element
The Human Apolipoprotein AV Gene Is Regulated by Peroxisome Proliferator-activated Receptor-α and Contains a Novel Farnesoid X-activated Receptor Response Element
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The Human Apolipoprotein AV Gene Is Regulated by Peroxisome Proliferator-activated Receptor-α and Contains a Novel Farnesoid X-activated Receptor Response Element

The Journal of biological chemistry, 2003-07, Vol.278 (28), p.25468-25480 [Peer Reviewed Journal]

2003 © 2003 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;(c) American Society for Biochemistry and Molecular Biology, 2003 info:eu-repo/semantics/openAccess ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M301302200 ;PMID: 12709436

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12
Cells Lacking Pfh1, a Fission Yeast Homolog of Mammalian Frataxin Protein, Display Constitutive Activation of the Iron Starvation Response
Cells Lacking Pfh1, a Fission Yeast Homolog of Mammalian Frataxin Protein, Display Constitutive Activation of the Iron Starvation Response
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Cells Lacking Pfh1, a Fission Yeast Homolog of Mammalian Frataxin Protein, Display Constitutive Activation of the Iron Starvation Response

The Journal of biological chemistry, 2012-12, Vol.287 (51), p.43042-43051 [Peer Reviewed Journal]

2012 © 2012 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;American Society for Biochemistry and Molecular Biology (ASBMB) /nThis research was originally published in Journal of biological chemistry. Gabrielli N, Ayté J, Hidalgo E. Cells lacking pfh1, a fission yeast homolog of mammalian frataxin protein, display constitutive activation of the iron starvation response. Journal of biological chemistry. 2012; 287(51): 43042-43051 info:eu-repo/semantics/openAccess ;2012 by The American Society for Biochemistry and Molecular Biology, Inc. 2012 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M112.421735 ;PMID: 23115244

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13
The Adenosine A2A Receptor Interacts with the Actin-binding Protein α-Actinin
The Adenosine A2A Receptor Interacts with the Actin-binding Protein α-Actinin
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The Adenosine A2A Receptor Interacts with the Actin-binding Protein α-Actinin

The Journal of biological chemistry, 2003-09, Vol.278 (39), p.37545-37552 [Peer Reviewed Journal]

2003 © 2003 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;(c) American Society for Biochemistry and Molecular Biology, 2003 info:eu-repo/semantics/openAccess ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M302809200 ;PMID: 12837758

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14
Actin-binding Protein α-Actinin-1 Interacts with the Metabotropic Glutamate Receptor Type 5b and Modulates the Cell Surface Expression and Function of the Receptor
Actin-binding Protein α-Actinin-1 Interacts with the Metabotropic Glutamate Receptor Type 5b and Modulates the Cell Surface Expression and Function of the Receptor
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Actin-binding Protein α-Actinin-1 Interacts with the Metabotropic Glutamate Receptor Type 5b and Modulates the Cell Surface Expression and Function of the Receptor

The Journal of biological chemistry, 2007-04, Vol.282 (16), p.12143-12153 [Peer Reviewed Journal]

2007 © 2007 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;(c) American Society for Biochemistry and Molecular Biology, 2007 info:eu-repo/semantics/openAccess ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M608880200 ;PMID: 17311919

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15
Thyroid Hormone Regulates the Hypotriglyceridemic Gene APOA5
Thyroid Hormone Regulates the Hypotriglyceridemic Gene APOA5
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Thyroid Hormone Regulates the Hypotriglyceridemic Gene APOA5

The Journal of biological chemistry, 2005-07, Vol.280 (30), p.27533-27543 [Peer Reviewed Journal]

2005 © 2005 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;(c) American Society for Biochemistry and Molecular Biology, 2005 info:eu-repo/semantics/openAccess ;Distributed under a Creative Commons Attribution 4.0 International License ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M503139200 ;PMID: 15941710

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16
Peroxisome proliferator-activated receptor mediates induction of the mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase gene by fatty acids
Peroxisome proliferator-activated receptor mediates induction of the mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase gene by fatty acids
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Peroxisome proliferator-activated receptor mediates induction of the mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase gene by fatty acids

The Journal of biological chemistry, 1994-07, Vol.269 (29), p.18767-18772 [Peer Reviewed Journal]

1994 INIST-CNRS ;(c) American Society for Biochemistry and Molecular Biology, 1994 info:eu-repo/semantics/openAccess ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1016/s0021-9258(17)32234-2 ;PMID: 7913466 ;CODEN: JBCHA3

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17
Myogenin Protein Stability Is Decreased by BMP-2 through a Mechanism Implicating Id1
Myogenin Protein Stability Is Decreased by BMP-2 through a Mechanism Implicating Id1
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Myogenin Protein Stability Is Decreased by BMP-2 through a Mechanism Implicating Id1

The Journal of biological chemistry, 2004-10, Vol.279 (44), p.45766-45772 [Peer Reviewed Journal]

(c) American Society for Biochemistry and Molecular Biology, 2004 info:eu-repo/semantics/openAccess ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M408059200 ;PMID: 15322112

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