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Roles of Rap1 signaling in tumor cell migration and invasion.

Cancer biology & medicine

Zhang YL, Wang RC, Cheng K, Ring BZ, Su L.
PMID: 28443208
Cancer Biol Med. 2017 Feb;14(1):90-99. doi: 10.20892/j.issn.2095-3941.2016.0086.

Ras-associated protein-1 (Rap1), a small GTPase in the Ras-related protein family, is an important regulator of basic cellular functions (e.g., formation and control of cell adhesions and junctions), cellular migration, and polarization. Through its interaction with other proteins, Rap1...

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Zhang YL, Wang RC, Cheng K, et al. Roles of Rap1 signaling in tumor cell migration and invasion. Cancer Biol Med. 2017;14(1):90-99doi: 10.20892/j.issn.2095-3941.2016.0086.
Zhang, Y. L., Wang, R. C., Cheng, K., Ring, B. Z., & Su, L. (2017). Roles of Rap1 signaling in tumor cell migration and invasion. Cancer biology & medicine, 14(1), 90-99. https://doi.org/10.20892/j.issn.2095-3941.2016.0086
Zhang, Yi-Lei, et al. "Roles of Rap1 signaling in tumor cell migration and invasion." Cancer biology & medicine vol. 14,1 (2017): 90-99. doi: https://doi.org/10.20892/j.issn.2095-3941.2016.0086
Zhang YL, Wang RC, Cheng K, Ring BZ, Su L. Roles of Rap1 signaling in tumor cell migration and invasion. Cancer Biol Med. 2017 Feb;14(1):90-99. doi: 10.20892/j.issn.2095-3941.2016.0086. PMID: 28443208; PMCID: PMC5365179.
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Exome sequencing identifies a novel mutation of the GDI1 gene in a Chinese non-syndromic X-linked intellectual disability family.

Genetics and molecular biology

Duan Y, Lin S, Xie L, Zheng K, Chen S, Song H, Zeng X, Gu X, Wang H, Zhang L, Shao H, Hong W, Zhang L, Duan S.
PMID: 28863211
Genet Mol Biol. 2017 Jul-Sep;40(3):591-596. doi: 10.1590/1678-4685-GMB-2016-0249. Epub 2017 Aug 31.

X-linked intellectual disability (XLID) has been associated with various genes. Diagnosis of XLID, especially for non-syndromic ones (NS-XLID), is often hampered by the heterogeneity of this disease. Here we report the case of a Chinese family in which three...

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Duan Y, Lin S, Xie L, et al. Exome sequencing identifies a novel mutation of the GDI1 gene in a Chinese non-syndromic X-linked intellectual disability family. Genet Mol Biol. 2017;40(3):591-596doi: 10.1590/1678-4685-GMB-2016-0249.
Duan, Y., Lin, S., Xie, L., Zheng, K., Chen, S., Song, H., Zeng, X., Gu, X., Wang, H., Zhang, L., Shao, H., Hong, W., Zhang, L., & Duan, S. (2017). Exome sequencing identifies a novel mutation of the GDI1 gene in a Chinese non-syndromic X-linked intellectual disability family. Genetics and molecular biology, 40(3), 591-596. https://doi.org/10.1590/1678-4685-GMB-2016-0249
Duan, Yongheng, et al. "Exome sequencing identifies a novel mutation of the GDI1 gene in a Chinese non-syndromic X-linked intellectual disability family." Genetics and molecular biology vol. 40,3 (2017): 591-596. doi: https://doi.org/10.1590/1678-4685-GMB-2016-0249
Duan Y, Lin S, Xie L, Zheng K, Chen S, Song H, Zeng X, Gu X, Wang H, Zhang L, Shao H, Hong W, Zhang L, Duan S. Exome sequencing identifies a novel mutation of the GDI1 gene in a Chinese non-syndromic X-linked intellectual disability family. Genet Mol Biol. 2017 Jul-Sep;40(3):591-596. doi: 10.1590/1678-4685-GMB-2016-0249. Epub 2017 Aug 31. PMID: 28863211; PMCID: PMC5596370.
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Structure, Function, Pharmacology, and Therapeutic Potential of the G Protein, Gα/q,11.

Frontiers in cardiovascular medicine

Kamato D, Thach L, Bernard R, Chan V, Zheng W, Kaur H, Brimble M, Osman N, Little PJ.
PMID: 26664886
Front Cardiovasc Med. 2015 Mar 24;2:14. doi: 10.3389/fcvm.2015.00014. eCollection 2015.

G protein coupled receptors (GPCRs) are one of the major classes of cell surface receptors and are associated with a group of G proteins consisting of three subunits termed alpha, beta, and gamma. G proteins are classified into four...

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Kamato D, Thach L, Bernard R, et al. Structure, Function, Pharmacology, and Therapeutic Potential of the G Protein, Gα/q,11. Front Cardiovasc Med. 2015;2:14doi: 10.3389/fcvm.2015.00014.
Kamato, D., Thach, L., Bernard, R., Chan, V., Zheng, W., Kaur, H., Brimble, M., Osman, N., & Little, P. J. (2015). Structure, Function, Pharmacology, and Therapeutic Potential of the G Protein, Gα/q,11. Frontiers in cardiovascular medicine, 214. https://doi.org/10.3389/fcvm.2015.00014
Kamato, Danielle, et al. "Structure, Function, Pharmacology, and Therapeutic Potential of the G Protein, Gα/q,11." Frontiers in cardiovascular medicine vol. 2 (2015): 14. doi: https://doi.org/10.3389/fcvm.2015.00014
Kamato D, Thach L, Bernard R, Chan V, Zheng W, Kaur H, Brimble M, Osman N, Little PJ. Structure, Function, Pharmacology, and Therapeutic Potential of the G Protein, Gα/q,11. Front Cardiovasc Med. 2015 Mar 24;2:14. doi: 10.3389/fcvm.2015.00014. eCollection 2015. PMID: 26664886; PMCID: PMC4671355.
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The Atypical Guanylate Kinase MoGuk2 Plays Important Roles in Asexual/Sexual Development, Conidial Septation, and Pathogenicity in the Rice Blast Fungus.

Frontiers in microbiology

Cai X, Zhang X, Li X, Liu M, Liu X, Wang X, Zhang H, Zheng X, Zhang Z.
PMID: 29321770
Front Microbiol. 2017 Dec 11;8:2467. doi: 10.3389/fmicb.2017.02467. eCollection 2017.

Guanylate kinases (GKs), which convert guanosine monophosphate into guanosine diphosphate (GDP), are important for growth and mannose outer chain elongation of cell wall N-linked glycoproteins in yeast. Here, we identified the ortholog of

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Cai X, Zhang X, Li X, et al. The Atypical Guanylate Kinase MoGuk2 Plays Important Roles in Asexual/Sexual Development, Conidial Septation, and Pathogenicity in the Rice Blast Fungus. Front Microbiol. 2017;8:2467doi: 10.3389/fmicb.2017.02467.
Cai, X., Zhang, X., Li, X., Liu, M., Liu, X., Wang, X., Zhang, H., Zheng, X., & Zhang, Z. (2017). The Atypical Guanylate Kinase MoGuk2 Plays Important Roles in Asexual/Sexual Development, Conidial Septation, and Pathogenicity in the Rice Blast Fungus. Frontiers in microbiology, 82467. https://doi.org/10.3389/fmicb.2017.02467
Cai, Xingjia, et al. "The Atypical Guanylate Kinase MoGuk2 Plays Important Roles in Asexual/Sexual Development, Conidial Septation, and Pathogenicity in the Rice Blast Fungus." Frontiers in microbiology vol. 8 (2017): 2467. doi: https://doi.org/10.3389/fmicb.2017.02467
Cai X, Zhang X, Li X, Liu M, Liu X, Wang X, Zhang H, Zheng X, Zhang Z. The Atypical Guanylate Kinase MoGuk2 Plays Important Roles in Asexual/Sexual Development, Conidial Septation, and Pathogenicity in the Rice Blast Fungus. Front Microbiol. 2017 Dec 11;8:2467. doi: 10.3389/fmicb.2017.02467. eCollection 2017. PMID: 29321770; PMCID: PMC5732230.
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Conformational switch that induces GDP release from Gi.

Journal of structural biology

Ham D, Ahn D, Ashim J, Cho Y, Kim HR, Yu W, Chung KY.
PMID: 33418033
J Struct Biol. 2021 Mar;213(1):107694. doi: 10.1016/j.jsb.2020.107694. Epub 2021 Jan 06.

Heterotrimeric guanine nucleotide-binding proteins (G proteins) are composed of α, β, and γ subunits. Gα switches between guanosine diphosphate (GDP)-bound inactive and guanosine triphosphate (GTP)-bound active states, and Gβγ interacts with the GDP-bound state. The GDP-binding regions are composed...

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Ham D, Ahn D, Ashim J, et al. Conformational switch that induces GDP release from Gi. J Struct Biol. 2021;213(1):107694doi: 10.1016/j.jsb.2020.107694.
Ham, D., Ahn, D., Ashim, J., Cho, Y., Kim, H. R., Yu, W., & Chung, K. Y. (2021). Conformational switch that induces GDP release from Gi. Journal of structural biology, 213(1), 107694. https://doi.org/10.1016/j.jsb.2020.107694
Ham, Donghee, et al. "Conformational switch that induces GDP release from Gi." Journal of structural biology vol. 213,1 (2021): 107694. doi: https://doi.org/10.1016/j.jsb.2020.107694
Ham D, Ahn D, Ashim J, Cho Y, Kim HR, Yu W, Chung KY. Conformational switch that induces GDP release from Gi. J Struct Biol. 2021 Mar;213(1):107694. doi: 10.1016/j.jsb.2020.107694. Epub 2021 Jan 06. PMID: 33418033.
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Group translocation as a mechanism for sucrose transfer into vacuoles from sugarcane cells.

Proceedings of the National Academy of Sciences of the United States of America

Thom M, Maretzki A.
PMID: 16593581
Proc Natl Acad Sci U S A. 1985 Jul;82(14):4697-701. doi: 10.1073/pnas.82.14.4697.

Isolated vacuoles from sugarcane cells took up uridine diphosphate glucose (UDP-Glc) from the surrounding medium at a rapid rate. After a 7-min incubation of vacuoles with UDP-[14C]Glc, sucrose and sucrose phosphate were identified in the vacuole extract. UDP-Glc in...

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Thom M, Maretzki A. Group translocation as a mechanism for sucrose transfer into vacuoles from sugarcane cells. Proc Natl Acad Sci U S A. 1985;82(14):4697-701doi: 10.1073/pnas.82.14.4697.
Thom, M., & Maretzki, A. (1985). Group translocation as a mechanism for sucrose transfer into vacuoles from sugarcane cells. Proceedings of the National Academy of Sciences of the United States of America, 82(14), 4697-701. https://doi.org/10.1073/pnas.82.14.4697
Thom, M, and Maretzki, A. "Group translocation as a mechanism for sucrose transfer into vacuoles from sugarcane cells." Proceedings of the National Academy of Sciences of the United States of America vol. 82,14 (1985): 4697-701. doi: https://doi.org/10.1073/pnas.82.14.4697
Thom M, Maretzki A. Group translocation as a mechanism for sucrose transfer into vacuoles from sugarcane cells. Proc Natl Acad Sci U S A. 1985 Jul;82(14):4697-701. doi: 10.1073/pnas.82.14.4697. PMID: 16593581; PMCID: PMC390453.
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Lead identification for the K-Ras protein: virtual screening and combinatorial fragment-based approaches.

OncoTargets and therapy

Pathan AA, Panthi B, Khan Z, Koppula PR, Alanazi MS, Sachchidanand, Parine NR, Chourasia M.
PMID: 27217775
Onco Targets Ther. 2016 May 02;9:2575-84. doi: 10.2147/OTT.S99671. eCollection 2016.

OBJECTIVE: Kirsten rat sarcoma (K-Ras) protein is a member of Ras family belonging to the small guanosine triphosphatases superfamily. The members of this family share a conserved structure and biochemical properties, acting as binary molecular switches. The guanosine triphosphate-bound...

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Pathan AA, Panthi B, Khan Z, et al. Lead identification for the K-Ras protein: virtual screening and combinatorial fragment-based approaches. Onco Targets Ther. 2016;9:2575-84doi: 10.2147/OTT.S99671.
Pathan, A. A., Panthi, B., Khan, Z., Koppula, P. R., Alanazi, M. S., Sachchidanand, Parine, N. R., & Chourasia, M. (2016). Lead identification for the K-Ras protein: virtual screening and combinatorial fragment-based approaches. OncoTargets and therapy, 92575-84. https://doi.org/10.2147/OTT.S99671
Pathan, Akbar Ali Khan, et al. "Lead identification for the K-Ras protein: virtual screening and combinatorial fragment-based approaches." OncoTargets and therapy vol. 9 (2016): 2575-84. doi: https://doi.org/10.2147/OTT.S99671
Pathan AA, Panthi B, Khan Z, Koppula PR, Alanazi MS, Sachchidanand, Parine NR, Chourasia M. Lead identification for the K-Ras protein: virtual screening and combinatorial fragment-based approaches. Onco Targets Ther. 2016 May 02;9:2575-84. doi: 10.2147/OTT.S99671. eCollection 2016. PMID: 27217775; PMCID: PMC4861002.
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Protein-RNA linkage and posttranslational modifications of feline calicivirus and murine norovirus VPg proteins.

PeerJ

Olspert A, Hosmillo M, Chaudhry Y, Peil L, Truve E, Goodfellow I.
PMID: 27375966
PeerJ. 2016 Jun 28;4:e2134. doi: 10.7717/peerj.2134. eCollection 2016.

Members of the Caliciviridae family of positive sense RNA viruses cause a wide range of diseases in both humans and animals. The detailed characterization of the calicivirus life cycle had been hampered due to the lack of robust cell...

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Olspert A, Hosmillo M, Chaudhry Y, et al. Protein-RNA linkage and posttranslational modifications of feline calicivirus and murine norovirus VPg proteins. PeerJ. 2016;4:e2134doi: 10.7717/peerj.2134.
Olspert, A., Hosmillo, M., Chaudhry, Y., Peil, L., Truve, E., & Goodfellow, I. (2016). Protein-RNA linkage and posttranslational modifications of feline calicivirus and murine norovirus VPg proteins. PeerJ, 4e2134. https://doi.org/10.7717/peerj.2134
Olspert, Allan, et al. "Protein-RNA linkage and posttranslational modifications of feline calicivirus and murine norovirus VPg proteins." PeerJ vol. 4 (2016): e2134. doi: https://doi.org/10.7717/peerj.2134
Olspert A, Hosmillo M, Chaudhry Y, Peil L, Truve E, Goodfellow I. Protein-RNA linkage and posttranslational modifications of feline calicivirus and murine norovirus VPg proteins. PeerJ. 2016 Jun 28;4:e2134. doi: 10.7717/peerj.2134. eCollection 2016. PMID: 27375966; PMCID: PMC4928471.
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Endosome-to-Plasma Membrane Recycling of VEGFR2 Receptor Tyrosine Kinase Regulates Endothelial Function and Blood Vessel Formation.

Cells

Jopling HM, Odell AF, Pellet-Many C, Latham AM, Frankel P, Sivaprasadarao A, Walker JH, Zachary IC, Ponnambalam S.
PMID: 24785348
Cells. 2014 Apr 29;3(2):363-85. doi: 10.3390/cells3020363.

Rab GTPases are implicated in endosome-to-plasma membrane recycling, but how such membrane traffic regulators control vascular endothelial growth factor receptor 2 (VEGFR2/KDR) dynamics and function are not well understood. Here, we evaluated two different recycling Rab GTPases, Rab4a and...

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Jopling HM, Odell AF, Pellet-Many C, et al. Endosome-to-Plasma Membrane Recycling of VEGFR2 Receptor Tyrosine Kinase Regulates Endothelial Function and Blood Vessel Formation. Cells. 2014;3(2):363-85doi: 10.3390/cells3020363.
Jopling, H. M., Odell, A. F., Pellet-Many, C., Latham, A. M., Frankel, P., Sivaprasadarao, A., Walker, J. H., Zachary, I. C., & Ponnambalam, S. (2014). Endosome-to-Plasma Membrane Recycling of VEGFR2 Receptor Tyrosine Kinase Regulates Endothelial Function and Blood Vessel Formation. Cells, 3(2), 363-85. https://doi.org/10.3390/cells3020363
Jopling, Helen M, et al. "Endosome-to-Plasma Membrane Recycling of VEGFR2 Receptor Tyrosine Kinase Regulates Endothelial Function and Blood Vessel Formation." Cells vol. 3,2 (2014): 363-85. doi: https://doi.org/10.3390/cells3020363
Jopling HM, Odell AF, Pellet-Many C, Latham AM, Frankel P, Sivaprasadarao A, Walker JH, Zachary IC, Ponnambalam S. Endosome-to-Plasma Membrane Recycling of VEGFR2 Receptor Tyrosine Kinase Regulates Endothelial Function and Blood Vessel Formation. Cells. 2014 Apr 29;3(2):363-85. doi: 10.3390/cells3020363. PMID: 24785348; PMCID: PMC4092869.
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Dysregulation of RalA signaling through dual regulatory mechanisms exerts its oncogenic functions in hepatocellular carcinoma.

Hepatology (Baltimore, Md.)

Tian L, Zhao L, Sze KM, Kam CS, Ming VS, Wang X, Zhang VX, Ho DW, Cheung TT, Chan LK, Ng IO.
PMID: 34767674
Hepatology. 2021 Nov 12; doi: 10.1002/hep.32236. Epub 2021 Nov 12.

BACKGROUND AND AIMS: Ras-like (Ral) small guanosine triphosphatases (GTPases), RalA and RalB, are proto-oncogenes directly downstream of Ras and cycle between the active guanosine triphosphate-bound and inactive guanosine diphosphate-bound forms. RalGTPase-activating protein (RalGAP) complex exerts a negative regulation. Currently,...

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Tian L, Zhao L, Sze KM, et al. Dysregulation of RalA signaling through dual regulatory mechanisms exerts its oncogenic functions in hepatocellular carcinoma. Hepatology. 2021;doi: 10.1002/hep.32236.
Tian, L., Zhao, L., Sze, K. M., Kam, C. S., Ming, V. S., Wang, X., Zhang, V. X., Ho, D. W., Cheung, T. T., Chan, L. K., & Ng, I. O. (2021). Dysregulation of RalA signaling through dual regulatory mechanisms exerts its oncogenic functions in hepatocellular carcinoma. Hepatology (Baltimore, Md.), . https://doi.org/10.1002/hep.32236
Tian, Lu, et al. "Dysregulation of RalA signaling through dual regulatory mechanisms exerts its oncogenic functions in hepatocellular carcinoma." Hepatology (Baltimore, Md.) vol. (2021). doi: https://doi.org/10.1002/hep.32236
Tian L, Zhao L, Sze KM, Kam CS, Ming VS, Wang X, Zhang VX, Ho DW, Cheung TT, Chan LK, Ng IO. Dysregulation of RalA signaling through dual regulatory mechanisms exerts its oncogenic functions in hepatocellular carcinoma. Hepatology. 2021 Nov 12; doi: 10.1002/hep.32236. Epub 2021 Nov 12. PMID: 34767674.
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Guanosine, a guanine-based nucleoside relaxed isolated corpus cavernosum from mice through cGMP accumulation.

Purinergic signalling

de Souza Nicoletti A, Passos GR, Bertollotto GM, Lescano CH, de Oliveira MG, Antunes E, Mónica FZ.
PMID: 32458299
Purinergic Signal. 2020 Jun;16(2):241-249. doi: 10.1007/s11302-020-09702-5. Epub 2020 May 27.

In corpus cavernosum (CC), guanosine triphosphate (GTP) is converted into cyclic guanosine monophosphate (cGMP) to induce erection. The action of cGMP is terminated by phosphodiesterases and efflux transporters, which pump cGMP out of the cell. The nucleotides, GTP, and...

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de Souza Nicoletti A, Passos GR, Bertollotto GM, et al. Guanosine, a guanine-based nucleoside relaxed isolated corpus cavernosum from mice through cGMP accumulation. Purinergic Signal. 2020;16(2):241-249doi: 10.1007/s11302-020-09702-5.
de Souza Nicoletti, A., Passos, G. R., Bertollotto, G. M., Lescano, C. H., de Oliveira, M. G., Antunes, E., & Mónica, F. Z. (2020). Guanosine, a guanine-based nucleoside relaxed isolated corpus cavernosum from mice through cGMP accumulation. Purinergic signalling, 16(2), 241-249. https://doi.org/10.1007/s11302-020-09702-5
de Souza Nicoletti, Aline, et al. "Guanosine, a guanine-based nucleoside relaxed isolated corpus cavernosum from mice through cGMP accumulation." Purinergic signalling vol. 16,2 (2020): 241-249. doi: https://doi.org/10.1007/s11302-020-09702-5
de Souza Nicoletti A, Passos GR, Bertollotto GM, Lescano CH, de Oliveira MG, Antunes E, Mónica FZ. Guanosine, a guanine-based nucleoside relaxed isolated corpus cavernosum from mice through cGMP accumulation. Purinergic Signal. 2020 Jun;16(2):241-249. doi: 10.1007/s11302-020-09702-5. Epub 2020 May 27. PMID: 32458299; PMCID: PMC7367940.
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Heterotrimeric G Proteins in Plants: Canonical and Atypical Gα Subunits.

International journal of molecular sciences

Maruta N, Trusov Y, Jones AM, Botella JR.
PMID: 34769272
Int J Mol Sci. 2021 Oct 31;22(21). doi: 10.3390/ijms222111841.

Heterotrimeric GTP-binding proteins (G proteins), consisting of Gα, Gβ and Gγ subunits, transduce signals from a diverse range of extracellular stimuli, resulting in the regulation of numerous cellular and physiological functions in Eukaryotes. According to the classic G protein...

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Maruta N, Trusov Y, Jones AM, et al. Heterotrimeric G Proteins in Plants: Canonical and Atypical Gα Subunits. Int J Mol Sci. 2021;22(21)doi: 10.3390/ijms222111841.
Maruta, N., Trusov, Y., Jones, A. M., & Botella, J. R. (2021). Heterotrimeric G Proteins in Plants: Canonical and Atypical Gα Subunits. International journal of molecular sciences, 22(21), . https://doi.org/10.3390/ijms222111841
Maruta, Natsumi, et al. "Heterotrimeric G Proteins in Plants: Canonical and Atypical Gα Subunits." International journal of molecular sciences vol. 22,21 (2021). doi: https://doi.org/10.3390/ijms222111841
Maruta N, Trusov Y, Jones AM, Botella JR. Heterotrimeric G Proteins in Plants: Canonical and Atypical Gα Subunits. Int J Mol Sci. 2021 Oct 31;22(21). doi: 10.3390/ijms222111841. PMID: 34769272; PMCID: PMC8584482.
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Showing 1 to 12 of 45 entries