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1
The motif E X E XXX L in the cytosolic tail of the secretory human proprotein convertase PC7 regulates its trafficking and cleavage activity
The motif E X E XXX L in the cytosolic tail of the secretory human proprotein convertase PC7 regulates its trafficking and cleavage activity
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The motif E X E XXX L in the cytosolic tail of the secretory human proprotein convertase PC7 regulates its trafficking and cleavage activity

The Journal of biological chemistry, 2020-02, Vol.295 (7), p.2068 [Peer Reviewed Journal]

2020 Durand et al. ;EISSN: 1083-351X ;PMID: 31915245

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2
Presenilin Transmembrane Domain 8 Conserved AXXXAXXXG Motifs Are Required for the Activity of the γ-Secretase Complex
Presenilin Transmembrane Domain 8 Conserved AXXXAXXXG Motifs Are Required for the Activity of the γ-Secretase Complex
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Presenilin Transmembrane Domain 8 Conserved AXXXAXXXG Motifs Are Required for the Activity of the γ-Secretase Complex

The Journal of biological chemistry, 2015-03, Vol.290 (11), p.7169-7184 [Peer Reviewed Journal]

2015 © 2015 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2015 by The American Society for Biochemistry and Molecular Biology, Inc. ;2015 by The American Society for Biochemistry and Molecular Biology, Inc. 2015 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M114.601286 ;PMID: 25614624

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3
A GxxxG-like Motif within HIV-1 Fusion Peptide Is Critical to Its Immunosuppressant Activity, Structure, and Interaction with the Transmembrane Domain of the T-cell Receptor
A GxxxG-like Motif within HIV-1 Fusion Peptide Is Critical to Its Immunosuppressant Activity, Structure, and Interaction with the Transmembrane Domain of the T-cell Receptor
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A GxxxG-like Motif within HIV-1 Fusion Peptide Is Critical to Its Immunosuppressant Activity, Structure, and Interaction with the Transmembrane Domain of the T-cell Receptor

The Journal of biological chemistry, 2012-09, Vol.287 (40), p.33503-33511 [Peer Reviewed Journal]

2012 © 2012 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2012 by The American Society for Biochemistry and Molecular Biology, Inc. 2012 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M112.370817 ;PMID: 22872636

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4
Amyloidogenic Processing but Not Amyloid Precursor Protein (APP) Intracellular C-terminal Domain Production Requires a Precisely Oriented APP Dimer Assembled by Transmembrane GXXXG Motifs
Amyloidogenic Processing but Not Amyloid Precursor Protein (APP) Intracellular C-terminal Domain Production Requires a Precisely Oriented APP Dimer Assembled by Transmembrane GXXXG Motifs
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Amyloidogenic Processing but Not Amyloid Precursor Protein (APP) Intracellular C-terminal Domain Production Requires a Precisely Oriented APP Dimer Assembled by Transmembrane GXXXG Motifs

The Journal of biological chemistry, 2008-03, Vol.283 (12), p.7733-7744 [Peer Reviewed Journal]

2008 © 2008 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M707142200 ;PMID: 18201969

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5
Regulation of RNF144A E3 Ubiquitin Ligase Activity by Self-association through Its Transmembrane Domain
Regulation of RNF144A E3 Ubiquitin Ligase Activity by Self-association through Its Transmembrane Domain
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Regulation of RNF144A E3 Ubiquitin Ligase Activity by Self-association through Its Transmembrane Domain

The Journal of biological chemistry, 2015-09, Vol.290 (38), p.23026-23038 [Peer Reviewed Journal]

2015 © 2015 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2015 by The American Society for Biochemistry and Molecular Biology, Inc. ;2015 by The American Society for Biochemistry and Molecular Biology, Inc. 2015 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M115.645499 ;PMID: 26216882

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6
A Novel Pex14 Protein-interacting Site of Human Pex5 Is Critical for Matrix Protein Import into Peroxisomes
A Novel Pex14 Protein-interacting Site of Human Pex5 Is Critical for Matrix Protein Import into Peroxisomes
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A Novel Pex14 Protein-interacting Site of Human Pex5 Is Critical for Matrix Protein Import into Peroxisomes

The Journal of biological chemistry, 2014-01, Vol.289 (1), p.437-448 [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. 2014 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M113.499707 ;PMID: 24235149

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7
Conservation and Diversification of Dileucine Signal Recognition by Adaptor Protein (AP) Complex Variants
Conservation and Diversification of Dileucine Signal Recognition by Adaptor Protein (AP) Complex Variants
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Conservation and Diversification of Dileucine Signal Recognition by Adaptor Protein (AP) Complex Variants

The Journal of biological chemistry, 2011-01, Vol.286 (3), p.2022-2030 [Peer Reviewed Journal]

2011 © 2011 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2011 by The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M110.197178 ;PMID: 21097499

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8
The Oligomeric States of the Purified Sigma-1 Receptor Are Stabilized by Ligands
The Oligomeric States of the Purified Sigma-1 Receptor Are Stabilized by Ligands
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The Oligomeric States of the Purified Sigma-1 Receptor Are Stabilized by Ligands

The Journal of biological chemistry, 2014-07, Vol.289 (29), p.20333-20344 [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. ;2014 by The American Society for Biochemistry and Molecular Biology, Inc. 2014 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M113.537993 ;PMID: 24847081

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9
An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1·cartilage-associated protein·cyclophilin B: the CXXXC motif reveals disulfide isomerase activity in vitro
An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1·cartilage-associated protein·cyclophilin B: the CXXXC motif reveals disulfide isomerase activity in vitro
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An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1·cartilage-associated protein·cyclophilin B: the CXXXC motif reveals disulfide isomerase activity in vitro

The Journal of biological chemistry, 2013-11, Vol.288 (44), p.31437-31446 [Peer Reviewed Journal]

2013 by The American Society for Biochemistry and Molecular Biology, Inc. 2013 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M113.498063 ;PMID: 24043621

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10
Human Naa50p (Nat5/San) Displays Both Protein Nα- and Nϵ-Acetyltransferase Activity
Human Naa50p (Nat5/San) Displays Both Protein Nα- and Nϵ-Acetyltransferase Activity
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Human Naa50p (Nat5/San) Displays Both Protein Nα- and Nϵ-Acetyltransferase Activity

The Journal of biological chemistry, 2009-11, Vol.284 (45), p.31122-31129 [Peer Reviewed Journal]

2009 © 2009 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2009 by The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M109.001347 ;PMID: 19744929

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11
Aberrant Amyloid Precursor Protein (APP) Processing in Hereditary Forms of Alzheimer Disease Caused by APP Familial Alzheimer Disease Mutations Can Be Rescued by Mutations in the APP GxxxG Motif
Aberrant Amyloid Precursor Protein (APP) Processing in Hereditary Forms of Alzheimer Disease Caused by APP Familial Alzheimer Disease Mutations Can Be Rescued by Mutations in the APP GxxxG Motif
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Aberrant Amyloid Precursor Protein (APP) Processing in Hereditary Forms of Alzheimer Disease Caused by APP Familial Alzheimer Disease Mutations Can Be Rescued by Mutations in the APP GxxxG Motif

The Journal of biological chemistry, 2010-07, Vol.285 (28), p.21636-21643 [Peer Reviewed Journal]

2010 © 2010 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2010 by The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M109.088005 ;PMID: 20452985

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12
Dimerization and phosphorylation of Lutheran/basal cell adhesion molecule are critical for its function in cell migration on laminin
Dimerization and phosphorylation of Lutheran/basal cell adhesion molecule are critical for its function in cell migration on laminin
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Dimerization and phosphorylation of Lutheran/basal cell adhesion molecule are critical for its function in cell migration on laminin

The Journal of biological chemistry, 2019-10, Vol.294 (41), p.14911-14921 [Peer Reviewed Journal]

2019 © 2019 Guadall et al. ;2019 Guadall et al. ;Distributed under a Creative Commons Attribution 4.0 International License ;2019 Guadall et al. 2019 Guadall et al. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.RA119.007521 ;PMID: 31413112

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13
Structural Basis of p75 Transmembrane Domain Dimerization
Structural Basis of p75 Transmembrane Domain Dimerization
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Structural Basis of p75 Transmembrane Domain Dimerization

The Journal of biological chemistry, 2016-06, Vol.291 (23), p.12346-12357 [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. ;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.M116.723585 ;PMID: 27056327

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14
Inside-out Signaling Promotes Dynamic Changes in the Carcinoembryonic Antigen-related Cellular Adhesion Molecule 1 (CEACAM1) Oligomeric State to Control Its Cell Adhesion Properties
Inside-out Signaling Promotes Dynamic Changes in the Carcinoembryonic Antigen-related Cellular Adhesion Molecule 1 (CEACAM1) Oligomeric State to Control Its Cell Adhesion Properties
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Inside-out Signaling Promotes Dynamic Changes in the Carcinoembryonic Antigen-related Cellular Adhesion Molecule 1 (CEACAM1) Oligomeric State to Control Its Cell Adhesion Properties

The Journal of biological chemistry, 2013-10, Vol.288 (41), p.29654-29669 [Peer Reviewed Journal]

2013 © 2013 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2013 by The American Society for Biochemistry and Molecular Biology, Inc. 2013 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M113.504639 ;PMID: 24005674

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15
A Transmembrane Leucine Zipper Is Required for Activation of the Dimeric Receptor Tyrosine Kinase DDR1
A Transmembrane Leucine Zipper Is Required for Activation of the Dimeric Receptor Tyrosine Kinase DDR1
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A Transmembrane Leucine Zipper Is Required for Activation of the Dimeric Receptor Tyrosine Kinase DDR1

The Journal of biological chemistry, 2006-08, Vol.281 (32), p.22744-22751 [Peer Reviewed Journal]

2006 © 2006 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M603233200 ;PMID: 16774916

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16
Identification of residues critical for topology inversion of the transmembrane protein TM4SF20 through regulated alternative translocation
Identification of residues critical for topology inversion of the transmembrane protein TM4SF20 through regulated alternative translocation
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Identification of residues critical for topology inversion of the transmembrane protein TM4SF20 through regulated alternative translocation

The Journal of biological chemistry, 2019-04, Vol.294 (15), p.6054-6061 [Peer Reviewed Journal]

2019 © 2019 Wang et al. ;2019 Wang et al. ;2019 Wang et al. 2019 Wang et al. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.RA119.007681 ;PMID: 30808712

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17
Structure of Shigella IpgB2 in Complex with Human RhoA: IMPLICATIONS FOR THE MECHANISM OF BACTERIAL GUANINE NUCLEOTIDE EXCHANGE FACTOR MIMICRY
Structure of Shigella IpgB2 in Complex with Human RhoA: IMPLICATIONS FOR THE MECHANISM OF BACTERIAL GUANINE NUCLEOTIDE EXCHANGE FACTOR MIMICRY
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Structure of Shigella IpgB2 in Complex with Human RhoA: IMPLICATIONS FOR THE MECHANISM OF BACTERIAL GUANINE NUCLEOTIDE EXCHANGE FACTOR MIMICRY

The Journal of biological chemistry, 2010-05, Vol.285 (22), p.17197-17208 [Peer Reviewed Journal]

2010 by The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M110.107953 ;PMID: 20363740

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18
Critical residues and motifs for homodimerization of the first transmembrane domain of the plasma membrane glycoprotein CD36
Critical residues and motifs for homodimerization of the first transmembrane domain of the plasma membrane glycoprotein CD36
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Critical residues and motifs for homodimerization of the first transmembrane domain of the plasma membrane glycoprotein CD36

The Journal of biological chemistry, 2017-05, Vol.292 (21), p.8683-8693 [Peer Reviewed Journal]

2017 © 2017 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology ;2017 by The American Society for Biochemistry and Molecular Biology, Inc. ;2017 by The American Society for Biochemistry and Molecular Biology, Inc. 2017 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M117.779595 ;PMID: 28336533

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19
Activation Loop Phosphorylation of ERK3/ERK4 by Group I p21-activated Kinases (PAKs) Defines a Novel PAK-ERK3/4-MAPK-activated Protein Kinase 5 Signaling Pathway
Activation Loop Phosphorylation of ERK3/ERK4 by Group I p21-activated Kinases (PAKs) Defines a Novel PAK-ERK3/4-MAPK-activated Protein Kinase 5 Signaling Pathway
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Activation Loop Phosphorylation of ERK3/ERK4 by Group I p21-activated Kinases (PAKs) Defines a Novel PAK-ERK3/4-MAPK-activated Protein Kinase 5 Signaling Pathway

The Journal of biological chemistry, 2011-02, Vol.286 (8), p.6470-6478 [Peer Reviewed Journal]

2011 © 2011 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2011 by The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M110.181529 ;PMID: 21177870

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20
Essential Role of a GXXXG Motif for Membrane Channel Formation by Helicobacter pylori Vacuolating Toxin
Essential Role of a GXXXG Motif for Membrane Channel Formation by Helicobacter pylori Vacuolating Toxin
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Essential Role of a GXXXG Motif for Membrane Channel Formation by Helicobacter pylori Vacuolating Toxin

The Journal of biological chemistry, 2003-04, Vol.278 (14), p.12101-12108 [Peer Reviewed Journal]

ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M212595200 ;PMID: 12562777

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