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1
The Luteinizing Hormone/Chorionic Gonadotropin Receptor Has Distinct Transmembrane Conductors for cAMP and Inositol Phosphate Signals
The Luteinizing Hormone/Chorionic Gonadotropin Receptor Has Distinct Transmembrane Conductors for cAMP and Inositol Phosphate Signals
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The Luteinizing Hormone/Chorionic Gonadotropin Receptor Has Distinct Transmembrane Conductors for cAMP and Inositol Phosphate Signals

Gilchrist, R L ; Ryu, K S ; Ji, I ; Ji, T H

The Journal of biological chemistry, 1996-08, Vol.271 (32), p.19283-19287 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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2
High Affinity Hormone Binding to the Extracellular N-terminal Exodomain of the Follicle-stimulating Hormone Receptor Is Critically Modulated by Exoloop 3
High Affinity Hormone Binding to the Extracellular N-terminal Exodomain of the Follicle-stimulating Hormone Receptor Is Critically Modulated by Exoloop 3
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High Affinity Hormone Binding to the Extracellular N-terminal Exodomain of the Follicle-stimulating Hormone Receptor Is Critically Modulated by Exoloop 3

Ryu, KiSung ; Gilchrist, Roger L. ; Tung, Chang-Shung ; Ji, Inhae ; Ji, Tae H.

The Journal of biological chemistry, 1998-10, Vol.273 (44), p.28953-28958 [Periódico revisado por pares]

United States: Elsevier Inc

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3
Exoloop 3 of the luteinizing hormone/choriogonadotropin receptor. Lys583 is essential and irreplaceable for human choriogonadotropin (hCG)-dependent receptor activation but not for high affinity hCG binding
Exoloop 3 of the luteinizing hormone/choriogonadotropin receptor. Lys583 is essential and irreplaceable for human choriogonadotropin (hCG)-dependent receptor activation but not for high affinity hCG binding
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Exoloop 3 of the luteinizing hormone/choriogonadotropin receptor. Lys583 is essential and irreplaceable for human choriogonadotropin (hCG)-dependent receptor activation but not for high affinity hCG binding

Ryu, K S ; Gilchrist, R L ; Ji, I ; Kim, S J ; Ji, T H

The Journal of biological chemistry, 1996-03, Vol.271 (13), p.7301 [Periódico revisado por pares]

United States

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4
Exoloop 3 of the luteinizing hormone/choriogonadotropin receptor. LYS super(583) is essential and irreplaceable for human choriogonadotropin (hCG)-dependent receptor activation but not for high affinity hCG binding
Exoloop 3 of the luteinizing hormone/choriogonadotropin receptor. LYS super(583) is essential and irreplaceable for human choriogonadotropin (hCG)-dependent receptor activation but not for high affinity hCG binding
Material Type:
Artigo 		Adicionar ao Meu Espaço

Exoloop 3 of the luteinizing hormone/choriogonadotropin receptor. LYS super(583) is essential and irreplaceable for human choriogonadotropin (hCG)-dependent receptor activation but not for high affinity hCG binding

Ryu, Ki-Sung ; Gilchrist, R L ; Ji, Inhae ; Kim, Seung-Jo ; Ji, Tae H

The Journal of biological chemistry, 1996-01, Vol.271 (13), p.7301-7304 [Periódico revisado por pares]

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5
The luteinizing hormone/chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals
The luteinizing hormone/chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals
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The luteinizing hormone/chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals

Gilchrist, Roger L. ; Ryu, Ki-Sung ; Ji, Inhae ; Ji, Tae H.

The Journal of biological chemistry, 1996-10, Vol.271 (42), p.26444 [Periódico revisado por pares]

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6
Plakoglobin Regulates the Expression of the Anti-apoptotic Protein BCL-2
Plakoglobin Regulates the Expression of the Anti-apoptotic Protein BCL-2
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Plakoglobin Regulates the Expression of the Anti-apoptotic Protein BCL-2

Hakimelahi, Shahram ; Parker, Henry R. ; Gilchrist, Anita J. ; Barry, Michele ; Li, Zhi ; Bleackley, R.Chris ; Pasdar, Manijeh

The Journal of biological chemistry, 2000-04, Vol.275 (15), p.10905-10911 [Periódico revisado por pares]

United States: Elsevier Inc

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7
Interactions between protein kinase CK2 and Pin1. Evidence for phosphorylation-dependent interactions
Interactions between protein kinase CK2 and Pin1. Evidence for phosphorylation-dependent interactions
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Interactions between protein kinase CK2 and Pin1. Evidence for phosphorylation-dependent interactions

Messenger, Moira M ; Saulnier, Ronald B ; Gilchrist, Andrew D ; Diamond, Phaedra ; Gorbsky, Gary J ; Litchfield, David W

The Journal of biological chemistry, 2002-06, Vol.277 (25), p.23054 [Periódico revisado por pares]

United States

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8
Mechanism of Activation of Protein Kinase D2(PKD2) by the CCKB/Gastrin Receptor
Mechanism of Activation of Protein Kinase D2(PKD2) by the CCKB/Gastrin Receptor
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Mechanism of Activation of Protein Kinase D2(PKD2) by the CCKB/Gastrin Receptor

Sturany, Sabine ; Van Lint, Johan ; Gilchrist, Annette ; Vandenheede, Jackie R. ; Adler, Guido ; Seufferlein, Thomas

The Journal of biological chemistry, 2002-08, Vol.277 (33), p.29431-29436 [Periódico revisado por pares]

Elsevier Inc

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9
A Ubiquitin-specific Protease That Efficiently Cleaves the Ubiquitin-Proline Bond
A Ubiquitin-specific Protease That Efficiently Cleaves the Ubiquitin-Proline Bond
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A Ubiquitin-specific Protease That Efficiently Cleaves the Ubiquitin-Proline Bond

Gilchrist, Catherine A. ; Gray, Douglas A. ; Baker, Rohan T.

The Journal of biological chemistry, 1997-12, Vol.272 (51), p.32280-32285 [Periódico revisado por pares]

United States: Elsevier Inc

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10
Thrombin receptors activate G(o) proteins in endothelial cells to regulate intracellular calcium and cell shape changes
Thrombin receptors activate G(o) proteins in endothelial cells to regulate intracellular calcium and cell shape changes
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Thrombin receptors activate G(o) proteins in endothelial cells to regulate intracellular calcium and cell shape changes

Vanhauwe, Jurgen F ; Thomas, Tarita O ; Minshall, Richard D ; Tiruppathi, Chinnaswamy ; Li, Anli ; Gilchrist, Annette ; Yoon, Eun-ja ; Malik, Asrar B ; Hamm, Heidi E

The Journal of biological chemistry, 2002-09, Vol.277 (37), p.34143-34149 [Periódico revisado por pares]

United States

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