ras GENES

A genetic model for colorectal tumorigenesis

Fearon, E. R., & Vogelstein, B. (1990) · Cell · doi:10.1016/0092-8674(90)90186-i · Cited by 12,132 · see citing works

p53 Mutations in Human Cancers

Hollstein, M., Sidransky, D., Vogelstein, B., & Harris, C. C. (1991) · Science · doi:10.1126/science.1905840 · Cited by 8,018 · see citing works

Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a

Serrano, M., Lin, A. W., McCurrach, M. E., Beach, D., & Lowe, S. W. (1997) · Cell · doi:10.1016/s0092-8674(00)81902-9 · Cited by 5,178 · see citing works

The GTPase superfamily: conserved structure and molecular mechanism

Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392 · see citing works

The Clinical KRAS(G12C) Inhibitor AMG 510 Drives Anti-Tumour Immunity

Canon, J., Rex, K., Saiki, A. Y., Mohr, C., Cooke, K., Bagal, D., Gaida, K., Holt, T., Knutson, C. G., Koppada, N., et al. (2019) · Nature · doi:10.1038/s41586-019-1694-1 · Cited by 2,277 · see citing works

G ₁ Events and Regulation of Cell Proliferation

Pardee, A. B. (1989) · Science · doi:10.1126/science.2683075 · Cited by 2,182 · see citing works

A role for sunlight in skin-cancer – UV-induced p53 mutations in squamous-cell carcinoma

Brash, D. E., Rudolph, J. A., Simon, J. A., Lin, A., McKenna, G. J., Baden, H. P., Halperin, A. J., & Pontén, J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.22.10124 · Cited by 1,959 · see citing works

Toxic effects of ultraviolet radiation on the skin

Matsumura, Y., & Ananthaswamy, H. N. (2004) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2003.08.019 · Cited by 1,270 · see citing works

KRAS Mutation: From Undruggable to Druggable in Cancer

Huang, L., Guo, Z., Wang, F., & Fu, L. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00780-4 · Cited by 1,127 · see citing works

The NF1 locus encodes a protein functionally related to mammalian GAP and yeast IRA proteins.

Ballester, R., Marchuk, D., Boguski, M., Saulino, A., Letcher, R., Wigler, M., & Collins, F. (1990) · Cell · doi:10.1016/0092-8674(90)90151-4 · Cited by 847 · see citing works

Dragging ras back in the ring

Stephen, A. G., Esposito, D., Bagni, R. K., & McCormick, F. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.02.017 · Cited by 795 · see citing works

JunD Reduces Tumor Angiogenesis by Protecting Cells from Oxidative Stress

Gerald, D., Berra, E., Frapart, Y. M., Chan, D. A., Giaccia, A. J., Mansuy, D., Pouysségur, J., Yaniv, M., & Mechta-Grigoriou, F. (2004) · Cell · doi:10.1016/j.cell.2004.08.025 · Cited by 588 · see citing works

Abnormal regulation of mammalian p21ras contributes to malignant tumor growth in von Recklinghausen (type 1) neurofibromatosis

DeClue, J. E., Papageorge, A. G., Fletcher, J. A., Diehl, S. R., Ratner, N., Vass, W. C., & Lowy, D. R. (1992) · Cell · doi:10.1016/0092-8674(92)90407-4 · Cited by 580 · see citing works

The current state of the art and future trends in RAS-targeted cancer therapies

Punekar, S. R., Velcheti, V., Neel, B. G., & Wong, K.-K. (2022) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-022-00671-9 · Cited by 549 · see citing works

Cellular commitment to oncogene-induced transformation or apoptosis is dependent on the transcription factor IRF-1

Tanaka, N., Ishihara, M., Kitagawa, M., Harada, H., Kimura, T., Matsuyama, T., Lamphier, M. S., Aizawa, S., Mak, T. W., & Taniguchi, T. (1994) · Cell · doi:10.1016/0092-8674(94)90132-5 · Cited by 491 · see citing works

The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glycoprotein)-related ATP-binding protein superfamily.

Kamijo, K., Taketani, S., Yokota, S., Osumi, T., & Hashimoto, T. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39595-x · Cited by 391 · see citing works

A model for RAS mutation patterns in cancers: finding the sweet spot

Li, S., Balmain, A., & Counter, C. M. (2018) · Nature Reviews Cancer · doi:10.1038/s41568-018-0076-6 · Cited by 384 · see citing works

Interaction between RasV12 and scribbled clones induces tumour growth and invasion

Wu, M., Pastor-Pareja, J. C., & Xu, T. (2010) · Nature · doi:10.1038/nature08702 · Cited by 388 · see citing works

Sequential Activation of the MEK-Extracellular Signal-Regulated Kinase and MKK3/6-p38 Mitogen-Activated Protein Kinase Pathways Mediates Oncogenic <i>ras</i> -Induced Premature Senescence

Wang, W., Chen, J. X., Liao, R., Deng, Q., Zhou, J. J., Huang, S., & Sun, P. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.10.3389-3403.2002 · Cited by 376 · see citing works

Ras Conformational Ensembles, Allostery, and Signaling

Lu, S., Jang, H., Muratcioglu, S., Gursoy, A., Keskin, O., Nussinov, R., & Zhang, J. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00542 · Cited by 355 · see citing works

Ras-Mediated Phosphorylation of a Conserved Threonine Residue Enhances the Transactivation Activities of c-Ets1 and c-Ets2

Yang, B.-S., Hauser, C. A., Henkel, G., Colman, M. S., Beveren, C. V., Stacey, K. J., Hume, D. A., Maki, R. A., & Ostrowski, M. C. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.2.538 · Cited by 333 · see citing works

Therapeutic Targeting of Oncogenic K‐Ras by a Covalent Catalytic Site Inhibitor

Lim, S. M., Westover, K. D., Ficarro, S. B., Harrison, R. A., Choi, H. G., Pacold, M. E., Carrasco, M., Hunter, J., Kim, N. D., Xie, T., et al. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201307387 · Cited by 300 · see citing works

Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator.

Hofer, F., Fields, S., Schneider, C., & Martin, G. S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.11089 · Cited by 287 · see citing works

KRAS: From undruggable to a druggable Cancer Target

Uprety, D., & Adjei, A. A. (2020) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2020.102070 · Cited by 271 · see citing works

Identification of Ras farnesyltransferase inhibitors by microbial screening.

Hara, M., Akasaka, K., Akinaga, S., Okabe, M., Nakano, H., Gomez, R., Wood, D., Uh, M., & Tamanoi, F. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.6.2281 · Cited by 257 · see citing works

Inhibition of SHP2-mediated dephosphorylation of Ras suppresses oncogenesis

Bunda, S., Burrell, K., Heir, P., Zeng, L., Alamsahebpour, A., Kano, Y., Raught, B., Zhang, Z.-Y., Zadeh, G., & Ohh, M. (2015) · Nature Communications · doi:10.1038/ncomms9859 · Cited by 249 · see citing works

Combinatorial patterns of somatic gene mutations in cancer

Yeang, C.-H., McCormick, F., & Levine, A. (2008) · The FASEB Journal · doi:10.1096/fj.08-108985 · Cited by 251 · see citing works

Development of small-molecule probes that selectively kill cells induced to express mutant RAS

Weïwer, M., Bittker, J. A., Lewis, T. A., Shimada, K., Yang, W. S., MacPherson, L., Dandapani, S., Palmer, M., Stockwell, B. R., Schreiber, S. L., et al. (2012) · Bioorganic &amp; Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.09.047 · Cited by 237 · see citing works

The origins and genetic interactions of KRAS mutations are allele- and tissue-specific

Cook, J. H., Melloni, G. E. M., Gulhan, D. C., Park, P. J., & Haigis, K. M. (2021) · Nature Communications · doi:10.1038/s41467-021-22125-z · Cited by 208 · see citing works

Fructose-1,6-bisphosphate couples glycolytic flux to activation of Ras

Peeters, K., Van Leemputte, F., Fischer, B., Bonini, B. M., Quezada, H., Tsytlonok, M., Haesen, D., Vanthienen, W., Bernardes, N., Gonzalez-Blas, C. B., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01019-z · Cited by 203 · see citing works

Characterization of Ha-Ras, N-Ras, Ki-Ras4A, and Ki-Ras4B as in Vitro Substrates for Farnesyl Protein Transferase and Geranylgeranyl Protein Transferase Type I

Zhang, F. L., Kirschmeier, P., Carr, D., James, L., Bond, R. W., Wang, L., Patton, R., Windsor, W. T., Syto, R., Zhang, R., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.15.10232 · Cited by 197 · see citing works

Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view

Lu, S., Jang, H., Gu, S., Zhang, J., & Nussinov, R. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00911a · Cited by 188 · see citing works

Role of the aryl hydrocarbon receptor in cell cycle regulation

Puga, A., Xia, Y., & Elferink, C. (2002) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00069-8 · Cited by 192 · see citing works

Peptides from the calcitonin genes: molecular genetics, structure and function

Breimer, L. H., MacIntyre, I., & Zaidi, M. (1988) · Biochemical Journal · doi:10.1042/bj2550377 · Cited by 189 · see citing works

RAS mutations in human cancers: Roles in precision medicine

Murugan, A. K., Grieco, M., & Tsuchida, N. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.06.007 · Cited by 146 · see citing works

Precise characterization of KRAS4b proteoforms in human colorectal cells and tumors reveals mutation/modification cross-talk

Ntai, I., Fornelli, L., DeHart, C. J., Hutton, J. E., Doubleday, P. F., LeDuc, R. D., van Nispen, A. J., Fellers, R. T., Whiteley, G., Boja, E. S., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1716122115 · Cited by 108 · see citing works

The cellular response to induction of the p21 c‐Ha‐ras oncoprotein includes stimulation of jun gene expression.

Sistonen, L., Hölttä, E., Mäkelä, T. P., Keski‐Oja, J., & Alitalo, K. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03442.x · Cited by 109 · see citing works

Tyrosyl phosphorylation of KRAS stalls GTPase cycle via alteration of switch I and II conformation

Kano, Y., Gebregiworgis, T., Marshall, C. B., Radulovich, N., Poon, B. P. K., St-Germain, J., Cook, J. D., Valencia-Sama, I., Grant, B. M. M., Herrera, S. G., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-08115-8 · Cited by 103 · see citing works

A RAS Renaissance: Emerging Targeted Therapies for KRAS-Mutated Non–Small Cell Lung Cancer

Vasan, N., Boyer, J. L., & Herbst, R. S. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-1762 · Cited by 102 · see citing works

The manumycin-group metabolites

Sattler, I., Thiericke, R., & Zeeck, A. (1998) · Natural Product Reports · doi:10.1039/a815221y · Cited by 95 · see citing works

RAS Mutations and Oncogenesis: Not all RAS Mutations are Created Equally

Miller, M. S., & Miller, L. D. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2011.00100 · Cited by 76 · see citing works

Drugging K-RasG12C through covalent inhibitors: Mission possible?

Ni, D., Li, X., He, X., Zhang, H., Zhang, J., & Lu, S. (2019) · Pharmacology &amp; Therapeutics · doi:10.1016/j.pharmthera.2019.06.007 · Cited by 73 · see citing works

Inhibitors of Ras–SOS Interactions

Lu, S., Jang, H., Zhang, J., & Nussinov, R. (2016) · ChemMedChem · doi:10.1002/cmdc.201500481 · Cited by 72 · see citing works

Somatic mutation theory, DNA repair rates, and the molecular epidemiology of p53 mutations

Holmquist, G. P., & Gao, S. (1997) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(96)00045-2 · Cited by 66 · see citing works

Distinct dynamics and interaction patterns in H- and K-Ras oncogenic P-loop mutants: Interaction Patterns in Ras Oncogenic Mutants

Sayyed-Ahmad, A., Prakash, P., & Gorfe, A. A. (2017) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25317 · Cited by 54 · see citing works

Global impact of KRAS mutation patterns in FOLFOX treated metastatic colorectal cancer

Zocche, D. M., Ramirez, C., Fontao, F. M., Costa, L. D., & Redal, M. A. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00116 · Cited by 50 · see citing works

Alterations in Differentiation and Behavior of Monocytic Phagocytes in Transgenic Mice that Express Dominant Suppressors of <i>ras</i> Signaling

Jin, D. I., Jameson, S. B., Reddy, M. A., Schenkman, D., & Ostrowski, M. C. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.2.693 · Cited by 47 · see citing works

New structural and functional insight into the regulation of Ras

Kano, Y., Cook, J. D., Lee, J. E., & Ohh, M. (2016) · Seminars in Cell &amp; Developmental Biology · doi:10.1016/j.semcdb.2016.06.006 · Cited by 38 · see citing works

Communication between the extracellular environment, cytoplasmic signalling cascades and the nuclear cell-cycle machinery

Peeper, D. S., & Bernards, R. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00319-0 · Cited by 36 · see citing works

RBEL1 Is a Novel Gene That Encodes a Nucleocytoplasmic Ras Superfamily GTP-binding Protein and Is Overexpressed in Breast Cancer

Montalbano, J., Jin, W., Sheikh, M. S., & Huang, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704760200 · Cited by 32 · see citing works

Observation of slow dynamic exchange processes in RAS protein crystals by 31P solid state NMR spectroscopy

Stumber, M., Geyer, M., Graf, R., Robert Kalbitzer, H., Scheffzek, K., & Haeberlen, U. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01010-0 · Cited by 22 · see citing works

Clinical features associated with NeoRAS wild-type metastatic colorectal cancer A SCRUM-Japan GOZILA substudy

Osumi, H., Shinozaki, E., Nakamura, Y., Esaki, T., Yasui, H., Taniguchi, H., Satake, H., Sunakawa, Y., Komatsu, Y., Kagawa, Y., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50026-4 · Cited by 17 · see citing works

Genetic mutations, molecular markers and future directions in research

Patel, K. N. (2013) · Oral Oncology · doi:10.1016/j.oraloncology.2013.03.437 · Cited by 6 · see citing works

Drosophila melanogaster 에 미치는 DDVP 의 생리변이적 영향에 관한 연구

최영현, 박연규, 이원호, et al. (1994)

Consequences of homo- and heterospecific rapid remating on the fitness of Drosophila melanogaster females

Jamart, J. A., Casares, P., Carracedo, M. C., et al. (1995) · Journal of Insect Physiology · doi:10.1016/0022-1910(95)00090-h · Cited by 2 · see citing works

A P element of Scaptomyza pallida is active in Drosophila melanogaster.

Simonelig, M., & Anxolabéhère, D. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.14.6102 · Cited by 65 · see citing works

Evolution of the LINE-like I element in the Drosophila melanogaster species subgroup

Sezutsu, H., Nitasaka, E., & Yamazaki, T. (1995) · Molecular and General Genetics MGG · doi:10.1007/bf00290363 · Cited by 11 · see citing works

Regulative interactions between cells of wing discs from different dipteran species

Williams, J. S., Littlefield, C. L., & Nöthiger, R. (1984) · Developmental Biology · doi:10.1016/0012-1606(84)90278-1