Inactivation of Icmt inhibits transformation by oncogenic K-Ras and B-Raf

Mutations of the BRAF gene in human cancer

Davies, H., Bignell, G. R., Cox, C., Stephens, P., Edkins, S., Clegg, S., Teague, J., Woffendin, H., Garnett, M. J., Bottomley, W., et al. (2002) · Nature · doi:10.1038/nature00766 · Cited by 10,674

ras oncogenes in human cancer: a review.

Bos, J. L. (1989) · PubMed · Cited by 5,061

Targeting RAS signalling pathways in cancer therapy

Downward, J. (2003) · Nature reviews. Cancer · doi:10.1038/nrc969 · Cited by 3,354

QUANTITATIVE STUDIES OF THE GROWTH OF MOUSE EMBRYO CELLS IN CULTURE AND THEIR DEVELOPMENT INTO ESTABLISHED LINES

Todaro, G. J., & Green, H. (1963) · The Journal of Cell Biology · doi:10.1083/jcb.17.2.299 · Cited by 2,747

Analysis of lung tumor initiation and progression using conditional expression of oncogenic K-rasPreprint

Jackson, E. L., Willis, N. A., Mercer, K. L., Bronson, R. T., Crowley, D. G., Montoya, R., Jacks, T., & Tuveson, D. A. (2001) · Genes & Development · doi:10.1101/gad.943001 · Cited by 1,927

Inducible Gene Targeting in Mice

Kühn, R., Schwenk, F., Aguet, M., & Rajewsky, K. (1995) · Science · doi:10.1126/science.7660125 · Cited by 1,641

Myc signaling via the ARF tumor suppressor regulates p53-dependent apoptosis and immortalization

Zindy, F., Eischen, C. M., Randle, D. H., Kamijo, T., Cleveland, J. L., Sherr, C. J., & Roussel, M. F. (1998) · Genes & Development · doi:10.1101/gad.12.15.2424 · Cited by 1,245

Radiation-induced cell cycle arrest compromised by p21 deficiency

Brugarolas, J., Chandrasekaran, C., Gordon, J. I., Beach, D., Jacks, T., & Hannon, G. J. (1995) · Nature · doi:10.1038/377552a0 · Cited by 1,242

K- and N-Ras Are Geranylgeranylated in Cells Treated with Farnesyl Protein Transferase Inhibitors

Whyte, D. B., Kirschmeier, P., Hockenberry, T. N., Nunez-Oliva, I., James, L., Catino, J. J., Bishop, W. R., & Pai, J.-K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.22.14459 · Cited by 884

Inhibition of purified p21 farnesyl:protein transferase by Cys-AAX tetrapeptides

Reiss, Y., Goldstein, J. L., Seabra, M. C., Casey, P. J., & Brown, M. S. (1990) · Cell · doi:10.1016/0092-8674(90)90242-7 · Cited by 815

Methotrexate and Ras Methylation: A New Trick for an Old Drug?

Philips, M. R. (2004) · Science s STKE · doi:10.1126/stke.2252004pe13 · Cited by 20

C-terminal proteolysis of prenylated proteins in trypanosomatids and RNA interference of enzymes required for the post-translational processing pathway of farnesylated proteins

Gillespie, J. R., Yokoyama, K., Lu, K., Eastman, R. T., Bollinger, J. G., Voorhis, W. C. V., Gelb, M. H., & C, F. S. B. A. (2007) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2007.02.009 · Cited by 19

Isoprenylcysteine Carboxyl Methyltransferase and Its Substrate Ras Are Critical Players Regulating TLR-Mediated Inflammatory Responses

Yang, W. S., Kim, H. G., Kim, E., Han, S. Y., Aziz, N., Yi, Y., Kim, S.-G., Lee, Y., Yoo, B. C., Han, J., et al. (2020) · Cells · doi:10.3390/cells9051216 · Cited by 18

Endoproteolytic Processing of RhoA by Rce1 Is Required for the Cleavage of RhoA by Yersinia enterocolitica Outer Protein T

Fueller, F., Bergö, M. O., Young, S. G., Aktories, K., & Schmidt, G. (2006) · Infection and Immunity · doi:10.1128/iai.74.3.1712-1717.2006 · Cited by 18

The Emerging Role of p21 in Diabetes and Related Metabolic Disorders

ElMitwalli, O. S., Darwish, R., Al-Jabery, L., Algahiny, A. T., Roy, S., Butler, A. E., & Hasan, A. S. H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252313209 · Cited by 17

Genome-wide association study and predictive ability for growth traits in Nellore cattle

de Carvalho, F. E., Espigolan, R., Berton, M. P., Neto, J. B. S., Silva, R. P., Grigoletto, L., Silva, R. M. O., Ferraz, J. B. S., Eler, J. P., Aguilar, I., et al. (2019) · Livestock Science · doi:10.1016/j.livsci.2019.103861 · Cited by 17

Beyond the Mevalonate Pathway: Control of Post-Prenylation Processing by Mutant p53

Etichetti, C. M. B., Zalazar, E. A., Cocordano, N., & Girardini, J. E. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.595034 · Cited by 17

Recent Progress in Developing Small Molecule Inhibitors Designed to Interfere with Ras Membrane Association

Tamanoi, F., & Lu, J. (2013) · The Enzymes · doi:10.1016/b978-0-12-420146-0.00008-1 · Cited by 18

Hydrophilic Anilinogeranyl Diphosphate Prenyl Analogues Are Ras Function Inhibitors

Roberts, M. J., Troutman, J. M., Chehade, K. A. H., Cha, H. C., Kao, J. P. Y., Huang, X., Zhan, C., Peterson, Y. K., Subramanian, T., Srinivasan, K., et al. (2006) · Biochemistry · doi:10.1021/bi061704+ · Cited by 17

Isoprenylcysteine carboxy methyltransferase (ICMT) is associated with tumor aggressiveness and its expression is controlled by the p53 tumor suppressor

Etichetti, C. B., Benedetto, C. D., Rossi, C., Baglioni, M. V., Bicciato, S., Sal, G. D., Menacho-Márquez, M., & Girardini, J. E. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006037 · Cited by 16

Mutational Analysis of the Integral Membrane Methyltransferase Isoprenylcysteine Carboxyl Methyltransferase (ICMT) Reveals Potential Substrate Binding Sites

Diver, M. M., & Long, S. B. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.585125 · Cited by 15

Rho of Plants patterning: linking mathematical models and molecular diversity

Deinum, E. E., & Jacobs, B. (2023) · Journal of Experimental Botany · doi:10.1093/jxb/erad447 · Cited by 13

Solid-Phase Synthesis of Prenylcysteine Analogs

Donelson, J. L., Hodges, H. B., Henriksen, B. S., Hrycyna, C. A., & Gibbs, R. A. (2009) · The Journal of Organic Chemistry · doi:10.1021/jo8021692 · Cited by 13

Deficiency of Isoprenylcysteine Carboxyl Methyltransferase (ICMT) Leads to Progressive Loss of Photoreceptor Function

Christiansen, J. R., Pendse, N. D., Kolandaivelu, S., Bergö, M. O., Young, S. G., & Ramamurthy, V. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0176-16.2016 · Cited by 13

C-terminus Proteolysis and Palmitoylation Cooperate for Optimal Plasma Membrane Localization of RasA in Aspergillus fumigatus

Abdallah, Q. A., Martín‐Vicente, A., Souza, A. C. O., Ge, W., & Fortwendel, J. R. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00562 · Cited by 12

Isoprenylcysteine carboxylmethyltransferase regulates ovarian cancer cell response to chemotherapy and Ras activation

Liu, Q., Chen, J., Fu, B., Dai, J., Zhao, Y., & Lai, L. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.05.038 · Cited by 12

The Ras Signalling Pathway as a Target in Cancer Therapy

Graham, K., & Olson, M. F. (2007) · Springer eBooks · doi:10.1007/978-3-540-31209-3_8 · Cited by 12

Icmt inhibition exerts anti-angiogenic and anti-hyperpermeability activities impeding malignant pleural effusion

Magkouta, S., Pappas, A., Moschos, C., Vazakidou, M., Psarra, K., & Kalomenidis, I. (2016) · Oncotarget · doi:10.18632/oncotarget.7912 · Cited by 11

Inhibition of isoprenylcysteine carboxylmethyltransferase augments BCR-ABL1 tyrosine kinase inhibition-induced apoptosis in chronic myeloid leukemia

Sun, W. T., Xiang, W., Ng, B. L., Asari, K., Bunte, R. M., Casey, P. J., Wang, M., & Chuah, C. T. H. (2015) · Experimental Hematology · doi:10.1016/j.exphem.2015.12.002 · Cited by 11

Total synthesis of the natural isoprenylcysteine carboxyl methyltransferase inhibitor spermatinamine

García, J. L., Pereira, R., & de Lera, Á. R. (2009) · Tetrahedron Letters · doi:10.1016/j.tetlet.2009.06.087 · Cited by 11

Inhibiting prenylation augments chemotherapy efficacy in renal cell carcinoma through dual inhibition on mitochondrial respiration and glycolysis

Huang, J., Yang, X., Peng, X., & Huang, W. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.09.120 · Cited by 10

Evaluating the Epithelial-Mesenchymal Program in Human Breast Epithelial Cells Cultured in Soft Agar Using a Novel Macromolecule Extraction Protocol

Lau, H. Y., Tang, J., Casey, P. J., & Wang, M. (2021) · Cancers · doi:10.3390/cancers13040807 · Cited by 9

10 Genetic approaches to understanding the physiologic importance of the carboxyl methylation of isoprenylated proteins

Young, S. G., Clarke, S. G., Bergoc, M. O., Phillips, M., & Fong, L. G. (2006) · The Enzymes · doi:10.1016/s1874-6047(06)80012-0 · Cited by 9

RASpecting the oncogene: New pathways to therapeutic advances

Stout, M. C., & Campbell, P. M. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.10.022 · Cited by 7

Activation of Ras by Post-Translational Modifications

Xiang, S., Bai, W., Bepler, G., & Zhang, X. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803505-4.00006-0 · Cited by 8

9 Structure and function of isoprenylcysteine carboxylmethyltransferase (Icmt): A key enzyme in CaaX processing

Anderson, J. L., & Hrycyna, C. A. (2006) · The Enzymes · doi:10.1016/s1874-6047(06)80011-9 · Cited by 7

Small change, big effect: Taking RAS by the tail through suppression of post-prenylation carboxylmethylation

Lau, H. Y., & Wang, M. (2017) · Small GTPases · doi:10.1080/21541248.2017.1415637 · Cited by 7

The role of ral signaling and post translational modifications (PTMs) of Ras in cancer

Zinatizadeh, M. R., Zarandi, P. K., Keshavarz‐Fathi, M., Yousefi, M. H., & Rezaei, N. (2022) · Genome Instability & Disease · doi:10.1007/s42764-022-00059-0 · Cited by 6

Preclinical Evaluation of [ 124 I]-Sotorasib for the Imaging of Kirsten Rat Sarcoma G12C Mutant Tumors

Artschwager, R., Kalidindi, T. M., Johnson, D. S., Brennan, C., Samuels, Z. V., Lito, P., & Pillarsetty, N. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00425 · Cited by 6

Non-substrate based, small molecule inhibitors of the human isoprenylcysteine carboxyl methyltransferase

Butler, K. V., Bohn, K. C., Hrycyna, C. A., & Jin, J. J. (2016) · MedChemComm · doi:10.1039/c6md00130k · Cited by 6

Heterogeneous Prenyl Processing of the Heterotrimeric G protein Gamma Subunits

Hildebrandt, J. D. (2011) · The Enzymes · doi:10.1016/b978-0-12-381339-8.00006-8 · Cited by 6

Uncovering the prevalence, key biogenesis enzymes, and biological significance of archaeal lipoproteins

Hong, Y., Makarova, K. S., Garcia, A. A., Xu, R., Pfeiffer, F., Welander, P. V., & Pohlschröder, M. (2025) · Nature Communications · doi:10.1038/s41467-025-63625-6 · Cited by 5

Isoprenylcysteine carboxyl methyltransferase inhibitors exerts anti-inflammatory activity

Yang, W. S., Kim, H. G., Lee, Y., Yoon, K., Kim, S.-G., Kim, J. H., & Cho, J. Y. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114219 · Cited by 5

Lipid Modification of Ras Superfamily GTPases

Chenette, E., & Der, C. (2011) · The Enzymes · doi:10.1016/b978-0-12-381339-8.00005-6 · Cited by 5

Polyisoprenylated Cysteinyl Amide Inhibitors: A Novel Approach to Controlling Cancers with Hyperactive Growth Signaling

Lamango, N. S., Nkembo, A. T., Ntantie, E., & Tawfeeq, N. (2020) · Current Medicinal Chemistry · doi:10.2174/0929867327666201111140825 · Cited by 5

Distinct functional relevance of dynamic GTPase cysteine methylation in fission yeast

Franco, A., Soto, T., Martı́n-Garcı́a, R., Madrid, M., Vázquez-Marín, B., Vicente‐Soler, J., Coll, P. M., Gacto, M., Pérez, P., & Cansado, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-06053-x · Cited by 4

Targeted genetic and small molecule disruption of N-Ras CaaX cleavage alters its localization and oncogenic potential

Hildebrandt, E. R., Hussain, S. A., Sieburg, M. A., Ravishankar, R., Asad, N., Gore, S., Ito, T., Hougland, J. L., Dore, T. M., & Schmidt, W. K. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107316 · Cited by 4

Alterations in molecular chaperones and eIF2α during lung endothelial cell apoptosis

Lü, Q., Jankowich, M. D., Newton, J., Harrington, E. O., & Rounds, S. (2010) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00416.2009 · Cited by 4

Isoprenylcysteine Carboxy Methylation Is Essential for Development inDictyostelium discoideum

Chen, Y., McQuade, K. J., Guan, X.-J., Thomason, P. A., Wert, M. S., Stock, J. B., & Cox, E. C. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-11-1006 · Cited by 3

Isoprenylcysteine carboxyl methyltransferase (ICMT) promotes invadopodia formation and metastasis in cancer cells

Etichetti, C. B., Zalazar, E. A., Benedetto, C. D., Cocordano, N., Valente, S., Bicciato, S., Menacho-Márquez, M., Larocca, M. C., & Girardini, J. E. (2024) · Biochimie · doi:10.1016/j.biochi.2024.01.015 · Cited by 3

Targeting Ras for Anticancer Drug Discovery

Yeh, J. J., Madigan, J. P., Campbell, P. M., Roberts, P. J., DeGraffenreid, L., & Der, C. J. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00329-6 · Cited by 3

Identification of a novel nanomolar inhibitor of hIcmt via a carboxylate replacement approach

Majmudar, J. D., Morrison-Logue, A., Song, J., Hrycyna, C. A., & Gibbs, R. A. (2012) · MedChemComm · doi:10.1039/c2md20108a · Cited by 3

Identification of a farnesol analog as a Ras function inhibitor using both an in vivo Ras activation sensor and a phenotypic screening approach

Srinivasan, K., Subramanian, T., Spielmann, H. P., & Janetopoulos, C. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1883-4 · Cited by 2

Biochemical and Biological Functions of Isoprenylcysteine Carboxyl Methyltransferase

(2011) · The Enzymes · doi:10.1016/b978-0-12-415922-8.00004-5 · Cited by 2

Solid-phase synthesis of Biotin-S-Farnesyl-l-Cysteine, a surrogate substrate for isoprenylcysteine Carboxylmethyltransferase (ICMT)

Stevenson, G. I., Yong, S. R., Fechner, G. A., Neve, J. E., Lock, A. M., & Avery, V. M. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.08.022 · Cited by 2

Mechanisms of CaaX Protein Processing: Protein Prenylation by FTase and GGTase-I

Blanden, M. J., Ashok, S., & Hougland, J. L. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.14837-1 · Cited by 2

Production of homocysteine in serum-starved apoptotic PC12 cells depends on the activation and modification of Ras

Barbakadze, T., Zhuravliova, E., Sepashvili, M., Zaalishvili, E., Ramsden, J. J., Bátor, J., Szeberényi, J., & Mikeladze, D. (2005) · Neuroscience Letters · doi:10.1016/j.neulet.2005.08.039 · Cited by 2

Effects of isoprenylcysteine carboxyl methyltransferase silencing on the proliferation and apoptosis of tongue squamous cell carcinoma.

Wang, S., Sun, W., Zhou, N., Zhao, K., Li, W., Chi, Z.-P., Wang, Y., Wang, Q., Tong, L., He, Z., et al. (2021) · PubMed Central · doi:10.7518/hxkq.2021.01.010 · Cited by 1

Mutational Activation of KRAS and BRAF in Colorectal Cancer

Pedone, K. H., Sells, J. L., & Der, C. J. (2013) · Springer eBooks · doi:10.1007/978-1-4614-8412-7_5 · Cited by 1

The Ras Converting Enzyme (Rce1p)

Schmidt, W. K., & Dore, T. M. (2011) · The Enzymes · doi:10.1016/b978-0-12-415922-8.00010-0 · Cited by 1

Suppression of isoprenylcysteine carboxylmethyltransferase compromises DNA damage repair

Tang, J., Casey, P. J., & Wang, M. (2021) · Life Science Alliance · doi:10.26508/lsa.202101144 · Cited by 2

In silico Exploration of a Novel ICMT Inhibitor with More Solubility than Cysmethynil against Membrane Localization of KRAS Mutant in Colorectal Cancer

Mouhcine, M., Kadil, Y., Segmani, I., Rahmoune, I., & Filali, H. (2024) · Current Computer - Aided Drug Design · doi:10.2174/0115734099264451231003172217 · Cited by 1

Inactivation of isoprenylcysteine carboxyl methyltransferase reduces proliferation of BRAF and NRAS mutated human melanoma cells

Thorisson, B. (2011) · Chalmers Publication Library (Chalmers University of Technology) · Cited by 1

Targeting the Ras-Ral effector pathway for cancer treatment

Gentry, L. R. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/0e9z-wv10 · Cited by 1

Icmt

Peterson, Y. K., Winter-Vann, A. M., & Casey, P. J. (2005) · AfCS-Nature Molecule Pages · doi:10.1038/mp.a001154.01 · Cited by 1

The mechanisms of the anti-tumour effect of inactivating ICMT in BRAF-induced cancer

Shkoukani, S. (2013) · Chalmers Publication Library (Chalmers University of Technology)

Ras

Cox, A. D., & DeCristo, M. J. (2013) · Cambridge University Press eBooks · doi:10.1017/cbo9781139046947.022

ISOPRENOID ANALOGS AS CHEMICAL GENETIC TOOLS TO PROVIDE INSIGHTS INTO FARNESYL TRANSFERASE TARGET SELECTION AND CELLULAR ACTIVITY

Troutman, J. M. (2006) · UKnowledge (University of Kentucky)

Defining the Role of GGTase-I in the Development of Rheumatoid Arthritis and Atherosclerosis

Khan, O. M. (2012) · Gothenburg University Publications Electronic Archive (Gothenburg University)

Defining RCE1 and ICMT as Therapeutic Targets in K-RAS-induced Cancer

Wahlstrom, A. M. (2009) · Gothenburg University Publications Electronic Archive (Gothenburg University)

The Importance of Isoprenylation and Nf1 Deficiency in K-RAS-induced Cancer

Sjogren, A.-K. M. (2009) · Gothenburg University Publications Electronic Archive (Gothenburg University)

Cysmethynil, a Specific Small-Molecule Inhibitor of Isoprenylcysteine Carboxylmethyl Transferase (Icmt)

Wang, M. (2011) · The Enzymes · doi:10.1016/b978-0-12-415922-8.00011-2

Anti-Ras Strategies for Cancer Treatment

Fiordalisi, J. J., Der, C. J., & Cox, A. D. (2006) · Springer eBooks · doi:10.1007/1-4020-4708-8_15

Viral-Like Proteins

Karyampudi, L., & Knutson, K. L. (2017) · Springer eBooks · doi:10.1007/978-1-4419-0717-2_147

The Influence of Intracellular Location on Function of Ras Proteins

McKay, J., & Buss, J. E. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00213-8

New Insights into the Role of Protein Prenylation and Processing in Plant Development, Phytohormone Signaling, and Secondary Metabolism

Crowell, D. N., & Thangadurai, D. (2015) · Apple Academic Press eBooks · doi:10.1201/b18597-11

Investigação da quinase IKKβ como um alvo terapêutico anti-metastático em câncer de pulmão associado à ativação do oncogene KRAS

Miranda, V. S. (2019) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.46.2019.tde-01082019-085027

Ras and Ras Signaling as a Therapeutic Target in Cancer

Sliker, B. H., & Campbell, P. M. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00006-2

Role for protein prenylation and "CAAX" processing in photoreceptor neurons

Pendse, N. D. (2016) · doi:10.33915/etd.6397

Role of "CAAX" protein processing in the retina

Christiansen, J. R. (2011) · doi:10.33915/etd.4706

Faculty Opinions recommendation of Identification of a novel prenyl and palmitoyl modification at the CaaX motif of Cdc42 that regulates RhoGDI binding.

Wedegaertner, P. (2013) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.717979622.793471407

Ras Oncoproteins

Chenette, E. J., & Der, C. J. (2008) · Wiley eBooks · doi:10.1002/9780470048672.wecb503

Viral-Like Proteins

Karyampudi, L., & Knutson, K. L. (2016) · Springer eBooks · doi:10.1007/978-1-4614-6613-0_147-1

Genome-wide association study and predictive ability for growth traits in Nellore cattle

de Carvalho, F. E. (2019) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.74.2019.tde-25102019-100751

ICMT como potencial biomarcador en el cáncer

Zalazar, E. A., Cocordano, N., Valente, S., Girardini, J. E., & Etichetti, C. B. (2022) · Revista de la Facultad de Ciencias Médicas Universidad Nacional de Rosario · doi:10.35305/fcm.v2i.52

Upstream Proteolysis by Ste24 does not Require a C-Terminal Methyl Ester as Revealed Using 33-Residue a-Factor Precursor Peptide Substrates Synthesized via Epimerization-Free Methods

Bader, T. K., Brown, S. M., Hrycyna, C. A., & Distefano, M. D. (2025) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-024-10677-9

Synthetic essentiality of isoprenylcysteine carboxylmethyltransferase in PTEN deficient triple negative breast cancer

Park, B.-S., Kim, J., Seo, D.-C., Choi, G.-E., Seo, J.-J., Lee, S. E., & Kim, T. (2026) · Experimental Hematology and Oncology · doi:10.1186/s40164-025-00738-0

ICMT deficiency ameliorates weight loss and mortality, but not tumor formation in a mouse model of liver cancer

Czarnota, P., Gromowski, T., Gołda, A., Bryzek, D., Lasota, S., Kozieł, J., Wilamowski, M., & Cisowski, J. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02775-6

Mécanismes moléculaires et cellulaires de formation et de dissolution des « processing bodies » en conditions physiologiques et physiopathologiques

Vidal-Cruchez, O. (2021) · theses.fr (ABES) · doi:10.70675/0c0e4622zadcfz40b9zb89ez6f22a14b8866

ICMT supports BRAF V600E -driven tumor growth by membrane targeting of the CAAX protein INPP5E

Yang, X., Qiao, X., Schmidt, S., Eklund, E. Ä., Ebner-Walter, C., Ivarsson, E. G., Crespo, M. A., Kersemakers, N., Dzanan, J. J., Thorisson, B., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2601795123

BindingDB Entry 50039805: S-Farnesyl-Thiopropionic Acid (FTPA) Triazoles as Potent Inhibitors of Isoprenylcysteine Carboxyl Methyltransferase.

BindingDB (2013) · UC San Diego · doi:10.7270/q26t0npk

BindingDB Entry 50047691: Non-Substrate Based, Small Molecule Inhibitors of the Human Isoprenylcysteine Carboxyl Methyltransferase.

BindingDB (2017) · UC San Diego · doi:10.7270/q2c82c8p

BindingDB Entry 50034481: Amide-modified prenylcysteine based Icmt inhibitors: Structure-activity relationships, kinetic analysis and cellular characterization.

BindingDB (2012) · UC San Diego · doi:10.7270/q2qz2bd2

BindingDB Entry 50042909: Functionalized indoleamines as potent, drug-like inhibitors of isoprenylcysteine carboxyl methyltransferase (Icmt).

BindingDB (2014) · UC San Diego · doi:10.7270/q25140m3

BindingDB Entry 50008021: A Potent Isoprenylcysteine Carboxylmethyltransferase (ICMT) Inhibitor Improves Survival in Ras-Driven Acute Myeloid Leukemia.

BindingDB (2021) · UC San Diego · doi:10.7270/q23x8b01

BindingDB Entry 50032360: Amino derivatives of indole as potent inhibitors of isoprenylcysteine carboxyl methyltransferase.

BindingDB (2011) · UC San Diego · doi:10.7270/q2vt1sb1

BindingDB Entry 50033599: Discovery and SAR of methylated tetrahydropyranyl derivatives as inhibitors of isoprenylcysteine carboxyl methyltransferase (ICMT).

BindingDB (2012) · UC San Diego · doi:10.7270/q2xw4k49

BindingDB Entry 50006469: 8-Hydroxyquinoline-based inhibitors of the Rce1 protease disrupt Ras membrane localization in human cells.

BindingDB (2020) · UC San Diego · doi:10.7270/q2ns0xxq

Genetic and Pharmacologic Analyses of the Role of Icmt in Ras Membrane Association and Function

Svensson, A. W., Casey, P. J., Young, S. G., & Bergö, M. O. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)07013-8 · Cited by 22

Inactivating Icmt ameliorates K-RAS–induced myeloproliferative disease

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