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Showing 1 to 12 of 123 entries
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Professor Frank McCormick: K-Ras proteins offer new opportunities for therapeutic intervention against human cancers.

Annals of translational medicine

He MC.
PMID: 25568879
Ann Transl Med. 2014 Dec;2(12):126. doi: 10.3978/j.issn.2305-5839.2014.11.10.

No abstract available.

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He MC. Professor Frank McCormick: K-Ras proteins offer new opportunities for therapeutic intervention against human cancers. Ann Transl Med. 2014;2(12):126doi: 10.3978/j.issn.2305-5839.2014.11.10.
He, M. C. (2014). Professor Frank McCormick: K-Ras proteins offer new opportunities for therapeutic intervention against human cancers. Annals of translational medicine, 2(12), 126. https://doi.org/10.3978/j.issn.2305-5839.2014.11.10
He, Melanie C. "Professor Frank McCormick: K-Ras proteins offer new opportunities for therapeutic intervention against human cancers." Annals of translational medicine vol. 2,12 (2014): 126. doi: https://doi.org/10.3978/j.issn.2305-5839.2014.11.10
He MC. Professor Frank McCormick: K-Ras proteins offer new opportunities for therapeutic intervention against human cancers. Ann Transl Med. 2014 Dec;2(12):126. doi: 10.3978/j.issn.2305-5839.2014.11.10. PMID: 25568879; PMCID: PMC4260056.
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Non-Substrate Based, Small Molecule Inhibitors of the Human Isoprenylcysteine Carboxyl Methyltransferase.

MedChemComm

Butler KV, Bohn K, Hrycyna CA, Jin J.
PMID: 27547295
Medchemcomm. 2016 May 01;7(5):1016-1021. doi: 10.1039/C6MD00130K. Epub 2016 Apr 14.

Activating mutations of human K-Ras proteins are among the most common oncogenic mutations, present in approximately 30% of all human cancers. Posttranslational modifications to K-Ras guide it to the plasma membrane and disruption of this localization inhibits the growth...

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Butler KV, Bohn K, Hrycyna CA, et al. Non-Substrate Based, Small Molecule Inhibitors of the Human Isoprenylcysteine Carboxyl Methyltransferase. Medchemcomm. 2016;7(5):1016-1021doi: 10.1039/C6MD00130K.
Butler, K. V., Bohn, K., Hrycyna, C. A., & Jin, J. (2016). Non-Substrate Based, Small Molecule Inhibitors of the Human Isoprenylcysteine Carboxyl Methyltransferase. MedChemComm, 7(5), 1016-1021. https://doi.org/10.1039/C6MD00130K
Butler, Kyle V, et al. "Non-Substrate Based, Small Molecule Inhibitors of the Human Isoprenylcysteine Carboxyl Methyltransferase." MedChemComm vol. 7,5 (2016): 1016-1021. doi: https://doi.org/10.1039/C6MD00130K
Butler KV, Bohn K, Hrycyna CA, Jin J. Non-Substrate Based, Small Molecule Inhibitors of the Human Isoprenylcysteine Carboxyl Methyltransferase. Medchemcomm. 2016 May 01;7(5):1016-1021. doi: 10.1039/C6MD00130K. Epub 2016 Apr 14. PMID: 27547295; PMCID: PMC4990076.
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Molecular docking and simulation of Curcumin with Geranylgeranyl Transferase1 (GGTase1) and Farnesyl Transferase (FTase).

Bioinformation

Subramani PA, Narala VR, Michael RD, Lomada D, Reddy MC.
PMID: 26124569
Bioinformation. 2015 May 28;11(5):248-53. doi: 10.6026/97320630011248. eCollection 2015.

Protein prenylation is a posttranslational modification that is indispensable for translocation of membrane GTPases like Ras, Rho, Ras etc. Proteins of Ras family undergo farnesylation by FTase while Rho family goes through geranylgeranylation by GGTase1. There is only an...

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Subramani PA, Narala VR, Michael RD, et al. Molecular docking and simulation of Curcumin with Geranylgeranyl Transferase1 (GGTase1) and Farnesyl Transferase (FTase). Bioinformation. 2015;11(5):248-53doi: 10.6026/97320630011248.
Subramani, P. A., Narala, V. R., Michael, R. D., Lomada, D., & Reddy, M. C. (2015). Molecular docking and simulation of Curcumin with Geranylgeranyl Transferase1 (GGTase1) and Farnesyl Transferase (FTase). Bioinformation, 11(5), 248-53. https://doi.org/10.6026/97320630011248
Subramani, Parasuraman Aiya, et al. "Molecular docking and simulation of Curcumin with Geranylgeranyl Transferase1 (GGTase1) and Farnesyl Transferase (FTase)." Bioinformation vol. 11,5 (2015): 248-53. doi: https://doi.org/10.6026/97320630011248
Subramani PA, Narala VR, Michael RD, Lomada D, Reddy MC. Molecular docking and simulation of Curcumin with Geranylgeranyl Transferase1 (GGTase1) and Farnesyl Transferase (FTase). Bioinformation. 2015 May 28;11(5):248-53. doi: 10.6026/97320630011248. eCollection 2015. PMID: 26124569; PMCID: PMC4464541.
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ras and p53 in the prediction of survival in Dukes' stage B colorectal carcinoma.

Clinical molecular pathology

Bennett MA, Kay EW, Mulcahy H, O'flaherty L, O'donoghue DP, Leader M, Croke DT.
PMID: 16696029
Clin Mol Pathol. 1995 Dec;48(6):M310-5. doi: 10.1136/mp.48.6.m310.

Aims-To determine possible associations between p53 allelic deletion, c-Ki-ras mutational activation, immunohistochemical detection of p53 and ras proteins, various clinicopathological variables, and patient outcome in 168 Dukes' stage B colorectal carcinomas.Methods-Allelic deletion at the p53 tumour suppressor gene locus...

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Bennett MA, Kay EW, Mulcahy H, et al. ras and p53 in the prediction of survival in Dukes' stage B colorectal carcinoma. Clin Mol Pathol. 1995;48(6):M310-5doi: 10.1136/mp.48.6.m310.
Bennett, M. A., Kay, E. W., Mulcahy, H., O'flaherty, L., O'donoghue, D. P., Leader, M., & Croke, D. T. (1995). ras and p53 in the prediction of survival in Dukes' stage B colorectal carcinoma. Clinical molecular pathology, 48(6), M310-5. https://doi.org/10.1136/mp.48.6.m310
Bennett, M A, et al. "ras and p53 in the prediction of survival in Dukes' stage B colorectal carcinoma." Clinical molecular pathology vol. 48,6 (1995): M310-5. doi: https://doi.org/10.1136/mp.48.6.m310
Bennett MA, Kay EW, Mulcahy H, O'flaherty L, O'donoghue DP, Leader M, Croke DT. ras and p53 in the prediction of survival in Dukes' stage B colorectal carcinoma. Clin Mol Pathol. 1995 Dec;48(6):M310-5. doi: 10.1136/mp.48.6.m310. PMID: 16696029; PMCID: PMC407996.
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CaM interaction and Ser181 phosphorylation as new K-Ras signaling modulators.

Small GTPases

Alvarez-Moya B, Barceló C, Tebar F, Jaumot M, Agell N.
PMID: 21776410
Small GTPases. 2011 Mar;2(2):99-103. doi: 10.4161/sgtp.2.2.15555.

The small G-protein Ras was the first oncogene to be identified and has a very important contribution to human cancer development (20-23% prevalence). K-RasB, one of the members of the Ras family, is the one that is most mutated...

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Alvarez-Moya B, Barceló C, Tebar F, et al. CaM interaction and Ser181 phosphorylation as new K-Ras signaling modulators. Small GTPases. 2011;2(2):99-103doi: 10.4161/sgtp.2.2.15555.
Alvarez-Moya, B., Barceló, C., Tebar, F., Jaumot, M., & Agell, N. (2011). CaM interaction and Ser181 phosphorylation as new K-Ras signaling modulators. Small GTPases, 2(2), 99-103. https://doi.org/10.4161/sgtp.2.2.15555
Alvarez-Moya, Blanca, et al. "CaM interaction and Ser181 phosphorylation as new K-Ras signaling modulators." Small GTPases vol. 2,2 (2011): 99-103. doi: https://doi.org/10.4161/sgtp.2.2.15555
Alvarez-Moya B, Barceló C, Tebar F, Jaumot M, Agell N. CaM interaction and Ser181 phosphorylation as new K-Ras signaling modulators. Small GTPases. 2011 Mar;2(2):99-103. doi: 10.4161/sgtp.2.2.15555. PMID: 21776410; PMCID: PMC3136912.
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Mice Lacking Ras-GRF1 Show Contextual Fear Conditioning but not Spatial Memory Impairments: Convergent Evidence from Two Independently Generated Mouse Mutant Lines.

Frontiers in behavioral neuroscience

d'Isa R, Clapcote SJ, Voikar V, Wolfer DP, Giese KP, Brambilla R, Fasano S.
PMID: 22164138
Front Behav Neurosci. 2011 Dec 06;5:78. doi: 10.3389/fnbeh.2011.00078. eCollection 2011.

Ras-GRF1 is a neuronal specific guanine exchange factor that, once activated by both ionotropic and metabotropic neurotransmitter receptors, can stimulate Ras proteins, leading to long-term phosphorylation of downstream signaling. The two available reports on the behavior of two independently...

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d'Isa R, Clapcote SJ, Voikar V, et al. Mice Lacking Ras-GRF1 Show Contextual Fear Conditioning but not Spatial Memory Impairments: Convergent Evidence from Two Independently Generated Mouse Mutant Lines. Front Behav Neurosci. 2011;5:78doi: 10.3389/fnbeh.2011.00078.
d'Isa, R., Clapcote, S. J., Voikar, V., Wolfer, D. P., Giese, K. P., Brambilla, R., & Fasano, S. (2011). Mice Lacking Ras-GRF1 Show Contextual Fear Conditioning but not Spatial Memory Impairments: Convergent Evidence from Two Independently Generated Mouse Mutant Lines. Frontiers in behavioral neuroscience, 578. https://doi.org/10.3389/fnbeh.2011.00078
d'Isa, Raffaele, et al. "Mice Lacking Ras-GRF1 Show Contextual Fear Conditioning but not Spatial Memory Impairments: Convergent Evidence from Two Independently Generated Mouse Mutant Lines." Frontiers in behavioral neuroscience vol. 5 (2011): 78. doi: https://doi.org/10.3389/fnbeh.2011.00078
d'Isa R, Clapcote SJ, Voikar V, Wolfer DP, Giese KP, Brambilla R, Fasano S. Mice Lacking Ras-GRF1 Show Contextual Fear Conditioning but not Spatial Memory Impairments: Convergent Evidence from Two Independently Generated Mouse Mutant Lines. Front Behav Neurosci. 2011 Dec 06;5:78. doi: 10.3389/fnbeh.2011.00078. eCollection 2011. PMID: 22164138; PMCID: PMC3230787.
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Crystal Structure of a Human K-Ras G12D Mutant in Complex with GDP and the Cyclic Inhibitory Peptide KRpep-2d.

ACS medicinal chemistry letters

Sogabe S, Kamada Y, Miwa M, Niida A, Sameshima T, Kamaura M, Yonemori K, Sasaki S, Sakamoto JI, Sakamoto K.
PMID: 28740607
ACS Med Chem Lett. 2017 May 10;8(7):732-736. doi: 10.1021/acsmedchemlett.7b00128. eCollection 2017 Jul 13.

The Ras proteins play roles in cell differentiation, proliferation, and survival. Aberrant signaling through Ras-mediated pathways in tumor cells occurs as a result of several types of mutational damage, which most frequently affects the amino acids G12, G13, and...

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Sogabe S, Kamada Y, Miwa M, et al. Crystal Structure of a Human K-Ras G12D Mutant in Complex with GDP and the Cyclic Inhibitory Peptide KRpep-2d. ACS Med Chem Lett. 2017;8(7):732-736doi: 10.1021/acsmedchemlett.7b00128.
Sogabe, S., Kamada, Y., Miwa, M., Niida, A., Sameshima, T., Kamaura, M., Yonemori, K., Sasaki, S., Sakamoto, J. I., & Sakamoto, K. (2017). Crystal Structure of a Human K-Ras G12D Mutant in Complex with GDP and the Cyclic Inhibitory Peptide KRpep-2d. ACS medicinal chemistry letters, 8(7), 732-736. https://doi.org/10.1021/acsmedchemlett.7b00128
Sogabe, Satoshi, et al. "Crystal Structure of a Human K-Ras G12D Mutant in Complex with GDP and the Cyclic Inhibitory Peptide KRpep-2d." ACS medicinal chemistry letters vol. 8,7 (2017): 732-736. doi: https://doi.org/10.1021/acsmedchemlett.7b00128
Sogabe S, Kamada Y, Miwa M, Niida A, Sameshima T, Kamaura M, Yonemori K, Sasaki S, Sakamoto JI, Sakamoto K. Crystal Structure of a Human K-Ras G12D Mutant in Complex with GDP and the Cyclic Inhibitory Peptide KRpep-2d. ACS Med Chem Lett. 2017 May 10;8(7):732-736. doi: 10.1021/acsmedchemlett.7b00128. eCollection 2017 Jul 13. PMID: 28740607; PMCID: PMC5512123.
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A Photochemical Switch for Controlling Protein-Protein Interactions.

Angewandte Chemie (International ed. in English)

Pollitt SK, Schultz PG.
PMID: 29711048
Angew Chem Int Ed Engl. 1998 Aug 17;37(15):2104-2107. doi: 10.1002/(SICI)1521-3773(19980817)37:15<2104::AID-ANIE2104>3.0.CO;2-Z.

Incorporation of an unnatural amino acid containing a photolabile group in the side chain allows specific interactions between two proteins to be prevented. The photocaged ras protein in which Asp 38 has been substituted by its β-nitrobenzyl ester (Nb)...

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Pollitt SK, Schultz PG. A Photochemical Switch for Controlling Protein-Protein Interactions. Angew Chem Int Ed Engl. 1998;37(15):2104-2107doi: 10.1002/(SICI)1521-3773(19980817)37:15<2104::AID-ANIE2104>3.0.CO;2-Z.
Pollitt, S. K., & Schultz, P. G. (1998). A Photochemical Switch for Controlling Protein-Protein Interactions. Angewandte Chemie (International ed. in English), 37(15), 2104-2107. https://doi.org/10.1002/(SICI)1521-3773(19980817)37:15<2104::AID-ANIE2104>3.0.CO;2-Z
Pollitt, Sonia K, and Schultz, Peter G. "A Photochemical Switch for Controlling Protein-Protein Interactions." Angewandte Chemie (International ed. in English) vol. 37,15 (1998): 2104-2107. doi: https://doi.org/10.1002/(SICI)1521-3773(19980817)37:15<2104::AID-ANIE2104>3.0.CO;2-Z
Pollitt SK, Schultz PG. A Photochemical Switch for Controlling Protein-Protein Interactions. Angew Chem Int Ed Engl. 1998 Aug 17;37(15):2104-2107. doi: 10.1002/(SICI)1521-3773(19980817)37:15<2104::AID-ANIE2104>3.0.CO;2-Z. PMID: 29711048.
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Aminoacylase 3 Is a New Potential Marker and Therapeutic Target in Hepatocellular Carcinoma.

Journal of Cancer

Tsirulnikov K, Duarte S, Ray A, Datta N, Zarrinpar A, Hwang L, Faull K, Pushkin A, Kurtz I.
PMID: 29290764
J Cancer. 2018 Jan 01;9(1):1-12. doi: 10.7150/jca.21747. eCollection 2018.

Ras proteins (HRas, KRas and NRas) are common oncogenes that require membrane association for activation. Previous approaches to block/inhibit Ras membrane association were unsuccessful for cancer treatment in human clinical studies. In the present study we utilized a new...

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Tsirulnikov K, Duarte S, Ray A, et al. Aminoacylase 3 Is a New Potential Marker and Therapeutic Target in Hepatocellular Carcinoma. J Cancer. 2018;9(1):1-12doi: 10.7150/jca.21747.
Tsirulnikov, K., Duarte, S., Ray, A., Datta, N., Zarrinpar, A., Hwang, L., Faull, K., Pushkin, A., & Kurtz, I. (2018). Aminoacylase 3 Is a New Potential Marker and Therapeutic Target in Hepatocellular Carcinoma. Journal of Cancer, 9(1), 1-12. https://doi.org/10.7150/jca.21747
Tsirulnikov, Kirill, et al. "Aminoacylase 3 Is a New Potential Marker and Therapeutic Target in Hepatocellular Carcinoma." Journal of Cancer vol. 9,1 (2018): 1-12. doi: https://doi.org/10.7150/jca.21747
Tsirulnikov K, Duarte S, Ray A, Datta N, Zarrinpar A, Hwang L, Faull K, Pushkin A, Kurtz I. Aminoacylase 3 Is a New Potential Marker and Therapeutic Target in Hepatocellular Carcinoma. J Cancer. 2018 Jan 01;9(1):1-12. doi: 10.7150/jca.21747. eCollection 2018. PMID: 29290764; PMCID: PMC5743706.
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Pharmacological or genetic inhibition of hypoxia signaling attenuates oncogenic RAS-induced cancer phenotypes.

Disease models & mechanisms

Zhu JY, Huang X, Fu Y, Wang Y, Zheng P, Liu Y, Han Z.
PMID: 34580712
Dis Model Mech. 2022 Feb 01;15(2). doi: 10.1242/dmm.048953. Epub 2021 Nov 19.

Oncogenic Ras mutations are highly prevalent in hematopoietic malignancies. However, it is difficult to directly target oncogenic RAS proteins for therapeutic intervention. We have developed a Drosophila acute myeloid leukemia model induced by human KRASG12V, which exhibits a dramatic...

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Zhu JY, Huang X, Fu Y, et al. Pharmacological or genetic inhibition of hypoxia signaling attenuates oncogenic RAS-induced cancer phenotypes. Dis Model Mech. 2021;15(2)doi: 10.1242/dmm.048953.
Zhu, J. Y., Huang, X., Fu, Y., Wang, Y., Zheng, P., Liu, Y., & Han, Z. (2022). Pharmacological or genetic inhibition of hypoxia signaling attenuates oncogenic RAS-induced cancer phenotypes. Disease models & mechanisms, 15(2), . https://doi.org/10.1242/dmm.048953
Zhu, Jun-Yi, et al. "Pharmacological or genetic inhibition of hypoxia signaling attenuates oncogenic RAS-induced cancer phenotypes." Disease models & mechanisms vol. 15,2 (2022). doi: https://doi.org/10.1242/dmm.048953
Zhu JY, Huang X, Fu Y, Wang Y, Zheng P, Liu Y, Han Z. Pharmacological or genetic inhibition of hypoxia signaling attenuates oncogenic RAS-induced cancer phenotypes. Dis Model Mech. 2022 Feb 01;15(2). doi: 10.1242/dmm.048953. Epub 2021 Nov 19. PMID: 34580712; PMCID: PMC8617310.
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Early-stage structure-based drug discovery for small GTPases by NMR spectroscopy.

Pharmacology & therapeutics

Yin G, Lv G, Zhang J, Jiang H, Lai T, Yang Y, Ren Y, Wang J, Yi C, Chen H, Huang Y, Xiao C.
PMID: 35007659
Pharmacol Ther. 2022 Jan 07;108110. doi: 10.1016/j.pharmthera.2022.108110. Epub 2022 Jan 07.

Small GTPase or Ras superfamily, including Ras, Rho, Rab, Ran and Arf, are fundamental in regulating a wide range of cellular processes such as growth, differentiation, migration and apoptosis. They share structural and functional similarities for binding guanine nucleotides...

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Yin G, Lv G, Zhang J, et al. Early-stage structure-based drug discovery for small GTPases by NMR spectroscopy. Pharmacol Ther. 2022;108110doi: 10.1016/j.pharmthera.2022.108110.
Yin, G., Lv, G., Zhang, J., Jiang, H., Lai, T., Yang, Y., Ren, Y., Wang, J., Yi, C., Chen, H., Huang, Y., & Xiao, C. (2022). Early-stage structure-based drug discovery for small GTPases by NMR spectroscopy. Pharmacology & therapeutics, 108110. https://doi.org/10.1016/j.pharmthera.2022.108110
Yin, Guowei, et al. "Early-stage structure-based drug discovery for small GTPases by NMR spectroscopy." Pharmacology & therapeutics vol. (2022): 108110. doi: https://doi.org/10.1016/j.pharmthera.2022.108110
Yin G, Lv G, Zhang J, Jiang H, Lai T, Yang Y, Ren Y, Wang J, Yi C, Chen H, Huang Y, Xiao C. Early-stage structure-based drug discovery for small GTPases by NMR spectroscopy. Pharmacol Ther. 2022 Jan 07;108110. doi: 10.1016/j.pharmthera.2022.108110. Epub 2022 Jan 07. PMID: 35007659.
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Ras signaling in yeast.

Genes & cancer

Tamanoi F.
PMID: 21779494
Genes Cancer. 2011 Mar;2(3):210-5. doi: 10.1177/1947601911407322.

Since the study of yeast RAS and adenylate cyclase in the early 1980s, yeasts including budding and fission yeasts contributed significantly to the study of Ras signaling. First, yeast studies provided insights into how Ras activates downstream signaling pathways....

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Tamanoi F. Ras signaling in yeast. Genes Cancer. 2011;2(3):210-5doi: 10.1177/1947601911407322.
Tamanoi, F. (2011). Ras signaling in yeast. Genes & cancer, 2(3), 210-5. https://doi.org/10.1177/1947601911407322
Tamanoi, Fuyuhiko. "Ras signaling in yeast." Genes & cancer vol. 2,3 (2011): 210-5. doi: https://doi.org/10.1177/1947601911407322
Tamanoi F. Ras signaling in yeast. Genes Cancer. 2011 Mar;2(3):210-5. doi: 10.1177/1947601911407322. PMID: 21779494; PMCID: PMC3128628.
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Showing 1 to 12 of 123 entries