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1
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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2
A group of novel VEGF splice variants as alternative therapeutic targets in renal cell carcinoma
A group of novel VEGF splice variants as alternative therapeutic targets in renal cell carcinoma
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A group of novel VEGF splice variants as alternative therapeutic targets in renal cell carcinoma

Montemagno, Christopher ; Durivault, Jérôme ; Gastaldi, Cécile ; Dufies, Maeva ; Vial, Valérie ; He, Xingkang ; Ambrosetti, Damien ; Kamenskaya, Anna ; Negrier, Sylvie ; Bernhard, Jean‐Christophe ; Borchiellini, Delphine ; Cao, Yihai ; Pagès, Gilles

Molecular oncology, 2023-07, Vol.17 (7), p.1379-1401 [Periódico revisado por pares]

United States: John Wiley & Sons, Inc

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3
Access of hydrogen-radicals to the peptide-backbone as a measure for estimating the flexibility of proteins using matrix-assisted laser desorption/ionization mass spectrometry
Access of hydrogen-radicals to the peptide-backbone as a measure for estimating the flexibility of proteins using matrix-assisted laser desorption/ionization mass spectrometry
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Access of hydrogen-radicals to the peptide-backbone as a measure for estimating the flexibility of proteins using matrix-assisted laser desorption/ionization mass spectrometry

Takayama, Mitsuo ; Nagoshi, Keishiro ; Iimuro, Ryunosuke ; Inatomi, Kazuma

International journal of molecular sciences, 2014-05, Vol.15 (5), p.8428-8442 [Periódico revisado por pares]

Switzerland: MDPI AG

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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
Hormonal signal amplification mediates environmental conditions during development and controls an irreversible commitment to adulthood
Hormonal signal amplification mediates environmental conditions during development and controls an irreversible commitment to adulthood
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Hormonal signal amplification mediates environmental conditions during development and controls an irreversible commitment to adulthood

Schaedel, Oren N ; Gerisch, Birgit ; Antebi, Adam ; Sternberg, Paul W Ruvkun, Gary

PLoS Biology, 2012-04, Vol.10 (4), p.e1001306-e1001306 [Periódico revisado por pares]

United States: Public Library of Science

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6
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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7
Molecular Pharmacology of VEGF-A Isoforms: Binding and Signalling at VEGFR2
Molecular Pharmacology of VEGF-A Isoforms: Binding and Signalling at VEGFR2
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Molecular Pharmacology of VEGF-A Isoforms: Binding and Signalling at VEGFR2

Peach, Chloe J ; Mignone, Viviane W ; Arruda, Maria Augusta ; Alcobia, Diana C ; Hill, Stephen J ; Kilpatrick, Laura E ; Woolard, Jeanette

International journal of molecular sciences, 2018-04, Vol.19 (4), p.1264 [Periódico revisado por pares]

Switzerland: MDPI AG

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8
Functional effects of blocking VEGF/VEGFR2 signaling in the rat urinary bladder in acute and chronic CYP-induced cystitis
Functional effects of blocking VEGF/VEGFR2 signaling in the rat urinary bladder in acute and chronic CYP-induced cystitis
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Functional effects of blocking VEGF/VEGFR2 signaling in the rat urinary bladder in acute and chronic CYP-induced cystitis

Tooke, Katharine ; Girard, Beatrice ; Vizzard, Margaret A

American journal of physiology. Renal physiology, 2019-07, Vol.317 (7), p.F43-F51 [Periódico revisado por pares]

United States: American Physiological Society

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9
Acetylproteomic Analysis Reveals Functional Implications of Lysine Acetylation in Human Spermatozoa (sperm)[S]
Acetylproteomic Analysis Reveals Functional Implications of Lysine Acetylation in Human Spermatozoa (sperm)[S]
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Acetylproteomic Analysis Reveals Functional Implications of Lysine Acetylation in Human Spermatozoa (sperm)[S]

Yu, Heguo ; Diao, Hua ; Wang, Chunmei ; Lin, Yan ; Yu, Fudong ; Lu, Hui ; Xu, Wei ; Li, Zheng ; Shi, Huijuan ; Zhao, Shimin ; Zhou, Yuchuan ; Zhang, Yonglian

Molecular & cellular proteomics, 2015-04, Vol.14 (4), p.1009-1023 [Periódico revisado por pares]

United States: Elsevier Inc

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10
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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