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Refinado por: Base de dados/Biblioteca: BACON - Mir@bel - GLOBAL_LIBRESACCES remover xxx: xxx remover xxx remover The Journal Of Biological Chemistry remover
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1
Purine N-oxides. XXX. Biochemical studies of the oncogen 3-hydroxyxanthine
Purine N-oxides. XXX. Biochemical studies of the oncogen 3-hydroxyxanthine
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Purine N-oxides. XXX. Biochemical studies of the oncogen 3-hydroxyxanthine

Myles, A ; Brown, G B

The Journal of biological chemistry, 1969-08, Vol.244 (15), p.4072 [Periódico revisado por pares]

United States

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2
Biosynthesis of the purines. XXX. Isolation and characterization of formylglycinamide ribonucleotide amidotransferase-glutamyl complex
Biosynthesis of the purines. XXX. Isolation and characterization of formylglycinamide ribonucleotide amidotransferase-glutamyl complex
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Biosynthesis of the purines. XXX. Isolation and characterization of formylglycinamide ribonucleotide amidotransferase-glutamyl complex

Mizobuchi, K ; Buchanan, J M

The Journal of biological chemistry, 1968-09, Vol.243 (18), p.4853 [Periódico revisado por pares]

United States

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3
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

Marinangeli, Claudia ; Tasiaux, Bernadette ; Opsomer, Rémi ; Hage, Salim ; Sodero, Alejandro O. ; Dewachter, Ilse ; Octave, Jean Noël ; Smith, Steven O. ; Constantinescu, Stefan N. ; Kienlen-Campard, Pascal

The Journal of biological chemistry, 2015-03, Vol.290 (11), p.7169-7184 [Periódico revisado por pares]

United States: Elsevier Inc

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4
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

Faingold, Omri ; Cohen, Tomer ; Shai, Yechiel

The Journal of biological chemistry, 2012-09, Vol.287 (40), p.33503-33511 [Periódico revisado por pares]

United States: Elsevier Inc

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5
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

Kienlen-Campard, Pascal ; Tasiaux, Bernadette ; Van Hees, Joanne ; Li, Mingli ; Huysseune, Sandra ; Sato, Takeshi ; Fei, Jeffrey Z. ; Aimoto, Saburo ; Courtoy, Pierre J. ; Smith, Steven O. ; Constantinescu, Stefan N. ; Octave, Jean-Noël

The Journal of biological chemistry, 2008-03, Vol.283 (12), p.7733-7744 [Periódico revisado por pares]

United States: Elsevier Inc

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6
Phosphoproteomics reveals that glycogen synthase kinase-3 phosphorylates multiple splicing factors and is associated with alternative splicing
Phosphoproteomics reveals that glycogen synthase kinase-3 phosphorylates multiple splicing factors and is associated with alternative splicing
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Phosphoproteomics reveals that glycogen synthase kinase-3 phosphorylates multiple splicing factors and is associated with alternative splicing

Shinde, Mansi Y. ; Sidoli, Simone ; Kulej, Katarzyna ; Mallory, Michael J. ; Radens, Caleb M. ; Reicherter, Amanda L. ; Myers, Rebecca L. ; Barash, Yoseph ; Lynch, Kristen W. ; Garcia, Benjamin A. ; Klein, Peter S.

The Journal of biological chemistry, 2017-11, Vol.292 (44), p.18240-18255 [Periódico revisado por pares]

United States: Elsevier Inc

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7
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

Gromek, Katarzyna A. ; Suchy, Fabian P. ; Meddaugh, Hannah R. ; Wrobel, Russell L. ; LaPointe, Loren M. ; Chu, Uyen B. ; Primm, John G. ; Ruoho, Arnold E. ; Senes, Alessandro ; Fox, Brian G.

The Journal of biological chemistry, 2014-07, Vol.289 (29), p.20333-20344 [Periódico revisado por pares]

United States: Elsevier Inc

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8
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

Ishikawa, Yoshihiro ; Bächinger, Hans Peter

The Journal of biological chemistry, 2013-11, Vol.288 (44), p.31437-31446 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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9
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

Guadall, Anna ; Cochet, Sylvie ; Renaud, Olivier ; Colin, Yves ; Le Van Kim, Caroline ; de Brevern, Alexandre G. ; El Nemer, Wassim

The Journal of biological chemistry, 2019-10, Vol.294 (41), p.14911-14921 [Periódico revisado por pares]

United States: Elsevier Inc

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10
Interaction between the SifA Virulence Factor and Its Host Target SKIP Is Essential for Salmonella Pathogenesis
Interaction between the SifA Virulence Factor and Its Host Target SKIP Is Essential for Salmonella Pathogenesis
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Interaction between the SifA Virulence Factor and Its Host Target SKIP Is Essential for Salmonella Pathogenesis

Diacovich, Lautaro ; Dumont, Audrey ; Lafitte, Daniel ; Soprano, Elodie ; Guilhon, Aude-Agnès ; Bignon, Christophe ; Gorvel, Jean-Pierre ; Bourne, Yves ; Méresse, Stéphane

The Journal of biological chemistry, 2009-11, Vol.284 (48), p.33151-33160 [Periódico revisado por pares]

United States: Elsevier Inc

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