The Poly(A)-Binding Protein and an mRNA Stability Protein Jointly Regulate an Endoribonuclease Activity

Hematology: Basic Principles and Practice

(1991) · Annals of Internal Medicine · doi:10.7326/0003-4819-115-3-238_2 · Cited by 1,862 · see citing works

mRNA stability in mammalian cells

Ross, J. (1995) · Microbiological Reviews · doi:10.1128/mr.59.3.423-450.1995 · Cited by 1,324 · see citing works

Circularization of mRNA by Eukaryotic Translation Initiation Factors

Wells, S. E., Hillner, P. E., Vale, R. D., & Sachs, A. B. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80122-7 · Cited by 968 · see citing works

Messenger RNA degradation in eukaryotes

Sachs, A. B. (1993) · Cell · doi:10.1016/0092-8674(93)80043-e · Cited by 846 · see citing works

Hematology: Basic Principles and Practice

Simon, T. (2001) · Transfusion · doi:10.1046/j.1537-2995.2001.41091177.x · Cited by 745 · see citing works

Association of the yeast poly(A) tail binding protein with translation initiation factor eIF‐4G.

Tarun, S. Z., & Sachs, A. B. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01108.x · Cited by 690 · see citing works

Removal of poly(A) and consequent degradation of c-fos mRNA facilitated by 3′ AU-rich sequences

Wilson, T., & Treisman, R. (1988) · Nature · doi:10.1038/336396a0 · Cited by 685 · see citing works

Degradation of mRNA in eukaryotes

Beelman, C. A., & Parker, R. (1995) · Cell · doi:10.1016/0092-8674(95)90326-7 · Cited by 652 · see citing works

A newly identified N‐terminal amino acid sequence of human eIF4G binds poly(A)‐binding protein and functions in poly(A)‐dependent translation

Imataka, H., Gradi, A., & Sonenberg, N. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7480 · Cited by 572 · see citing works

Two distinct destabilizing elements in the c-fos message trigger deadenylation as a first step in rapid mRNA decay.Preprint

Shyu, A. B., Belasco, J. G., & Greenberg, M. E. (1991) · Genes & Development · doi:10.1101/gad.5.2.221 · Cited by 546 · see citing works

Recognition of Polyadenylate RNA by the Poly(A)-Binding Protein

Deo, R. C., Bonanno, J. B., Sonenberg, N., & Burley, S. K. (1999) · Cell · doi:10.1016/s0092-8674(00)81517-2 · Cited by 513 · see citing works

Thalassemia Syndromes

Raj, S. R., Chen, S. R. W., Sheldon, R. S., et al. (2009) · Springer eBooks · doi:10.1007/978-3-540-29676-8_1731 · Cited by 475 · see citing works

The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA stability in vitro.

Bernstein, P., Peltz, S. W., & Ross, J. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.2.659 · Cited by 373 · see citing works

Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation

Craig, A. W., Haghighat, A., Yu, A. T. K., & Sonenberg, N. (1998) · Nature · doi:10.1038/33198 · Cited by 367 · see citing works

Rotavirus RNA‐binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F

Piron, M., Vende, P., Cohen, J., et al. (1998) · The EMBO Journal · doi:10.1093/emboj/17.19.5811 · Cited by 334 · see citing works

Evidence that the pathway of transferrin receptor mRNA degradation involves an endonucleolytic cleavage within the 3′ UTR and does not involve poly(A) tail shortening.

Binder, R., Horowitz, J. A., Basilion, J. P., Koeller, D. M., Klausner, R. D., & Harford, J. B. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06466.x · Cited by 289 · see citing works

Multiple functions for the poly(A)-binding protein in mRNA decapping and deadenylation in yeast.Preprint

Caponigro, G., & Parker, R. (1995) · Genes & Development · doi:10.1101/gad.9.19.2421 · Cited by 279 · see citing works

Hematology: Basic Principles and Practice

Barrett, O. (1991) · JAMA · doi:10.1001/jama.1991.03470160128049 · Cited by 275 · see citing works

The Eukaryotic Polypeptide Chain Releasing Factor (eRF3/GSPT) Carrying the Translation Termination Signal to the 3′-Poly(A) Tail of mRNA

Hoshino, S.-I., Imai, M., Kobayashi, T., Uchida, N., & Katada, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.24.16677 · Cited by 267 · see citing works

An mRNA Stability Complex Functions with Poly(A)-Binding Protein To Stabilize mRNA In Vitro

Wang, Z., Day, N., Trifillis, P., & Kiledjian, M. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.7.4552 · Cited by 262 · see citing works

Thalassemia: The consequences of unbalanced hemoglobin synthesis

Nathan, D. G., & Gunn, R. B. (1966) · The American Journal of Medicine · doi:10.1016/0002-9343(66)90039-8 · Cited by 260 · see citing works

Identification of two KH domain proteins in the alpha‐globin mRNP stability complex.

Kiledjian, M., Wang, X., & Liebhaber, S. A. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00110.x · Cited by 242 · see citing works

The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes

Körner, C. G., Wormington, M., Muckenthaler, M. U., Schneider, S., Dehlin, E., & Wahle, E. (1998) · The EMBO Journal · doi:10.1093/emboj/17.18.5427 · Cited by 242 · see citing works

Mechanisms of mRNA degradation in eukaryotes

Decker, C. J., & Parker, R. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90073-6 · Cited by 235 · see citing works

The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities.

Burd, C. G., Matunis, E. L., & Dreyfuss, G. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.7.3419 · Cited by 222 · see citing works

XenopusPoly(A) Binding Protein: Functional Domains in RNA Binding and Protein – Protein Interaction

Kühn, U., & Pieler, T. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0065 · Cited by 222 · see citing works

Messenger RNA deadenylylation precedes decapping in mammalian cells

Couttet, P., Fromont‐Racine, M., Steel, D., PICTET, R. L., & Grange, T. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.11.5628 · Cited by 209 · see citing works

Characterisation of Two Major Cellular Poly(rC)-Binding Human Proteins, Each Containing Three K-homologous (KH) Domains

Leffers, H. C. B., Dejgaard, K., & Celis, J. E. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0447h.x · Cited by 205 · see citing works

The Mechanisms of mRNA Degradation in Eukaryotes

Zhang, G., & Muyuan, Z. (1999) · Europe PMC (PubMed Central) · Cited by 203 · see citing works

Detection and Characterization of a 3′ Untranslated Region Ribonucleoprotein Complex Associated with Human α-Globin mRNA Stability

Wang, X., Kiledjian, M., Weiss, I. M., & Liebhaber, S. A. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.3.1769 · Cited by 192 · see citing works

Pbp1p, a Factor Interacting withSaccharomyces cerevisiaePoly(A)-Binding Protein, Regulates Polyadenylation

Mangus, D. A., Amrani, N., & Jacobson, A. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7383 · Cited by 190 · see citing works

Human mRNA polyadenylate binding protein: evolutionary conservation of a nucleic acid binding motif

Grange, T., de, C. M., Oddos, J., et al. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.12.4771 · Cited by 188 · see citing works

Characterisation of Two Major Cellular Poly(rC)-Binding Human Proteins, Each Containing Three K-homologous (KH) Domains

Leffers, H. C. B., Dejgaard, K., & Celis, J. E. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20581.x · Cited by 181 · see citing works

Erythroid Cell-Specific mRNA Stability Elements in the α2-Globin 39 Nontranslated Region

Weiss, I. M., & Liebhaber, S. A. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.5.2457 · Cited by 171 · see citing works

RNA Recognition Motif 2 of Yeast Pab1p Is Required for Its Functional Interaction with Eukaryotic Translation Initiation Factor 4G

Kessler, S. H., & Sachs, A. B. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.1.51 · Cited by 167 · see citing works

Identification of AUF1 (Heterogeneous Nuclear Ribonucleoprotein D) as a Component of the α-Globin mRNA Stability Complex

Kiledjian, M., DeMaria, C. T., Brewer, G., & Novick, K. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.8.4870 · Cited by 145 · see citing works

The Xenopus laevis poly(A) binding protein is composed of multiple functionally independent RNA binding domains.

Nietfeld, W., Mentzel, H., & Pieler, T. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07582.x · Cited by 133 · see citing works

mRNA metabolism and post-transcriptional gene regulation

Harford, J. B., & Morris, D. R. (1997) · Wiley-Liss eBooks · Cited by 130 · see citing works

Assembly of the α-Globin mRNA Stability Complex Reflects Binary Interaction between the Pyrimidine-Rich 3′ Untranslated Region Determinant and Poly(C) Binding Protein αCP

Chkheidze, A. N., Lyakhov, D. L., Makeyev, A. V., et al. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.7.4572 · Cited by 128 · see citing works

Purification and properties of a protein that binds to the C-terminal coding region of human c-myc mRNA.

Prokipcak, R. D., Herrick, D., & Ross, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37102-8 · Cited by 125 · see citing works

The Poly(A) Tail Inhibits the Assembly of a 3′-to-5′ Exonuclease in an In Vitro RNA Stability System

Ford, L. P., Bagga, P. S., & Wilusz, J. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.1.398 · Cited by 108 · see citing works

A Set of Highly Conserved RNA-binding Proteins, αCP-1 and αCP-2, Implicated in mRNA Stabilization, Are Coexpressed from an Intronless Gene and Its Intron-containing Paralog

Makeyev, A. V., Chkheidze, A. N., & Liebhaber, S. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.35.24849 · Cited by 103 · see citing works

Sequence-specific endonucleolytic cleavage and protection of mRNA in Xenopus and Drosophila.Preprint

Brown, B. D., Zipkin, I. D., & Harland, R. M. (1993) · Genes & Development · doi:10.1101/gad.7.8.1620 · Cited by 99 · see citing works

Human beta‐globin mRNAs that harbor a nonsense codon are degraded in murine erythroid tissues to intermediates lacking regions of exon I or exons I and II that have a cap‐like structure at the 5′ termini.

Lim, S. K., & Maquat, L. E. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05405.x · Cited by 89 · see citing works

Processing of 9E3 mRNA and regulation of its stability in normal and Rous sarcoma virus-transformed cells.

Stoeckle, M. Y., & Hanafusa, H. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.11.4738 · Cited by 85 · see citing works

A guanosine quadruplex and two stable hairpins flank a major cleavage site in insulin-like growth factor II mRNA

Christiansen, J., Kofod, M., & Nielsen, F. C. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.25.5709 · Cited by 85 · see citing works

Identification of an erythroid‐enriched endoribonuclease activity involved in specific mRNA cleavage

Wang, Z., & Kiledjian, M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.2.295 · Cited by 83 · see citing works

Destabilization of Human α-Globin mRNA by Translation Anti-termination Is Controlled during Erythroid Differentiation and Is Paralleled by Phased Shortening of the Poly(A) Tail

Morales, J., Russell, J., & Liebhaber, S. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.10.6607 · Cited by 72 · see citing works

Purification and Characterization of a Polysome-associated Endoribonuclease That Degrades c-myc mRNA in Vitro

Lee, C. H., Leeds, P., & Ross, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.39.25261 · Cited by 70 · see citing works

Estrogen-induced ribonuclease activity in Xenopus liver

Pastori, R. L., Moskaitis, J. E., & Schoenberg, D. R. (1991) · Biochemistry · doi:10.1021/bi00107a018 · Cited by 65 · see citing works

Removal of a 3′ non-coding sequence is an initial step in degradation of groα mRNA and is regulated by interleukin-1

Stoeckle, M. Y. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.5.1123 · Cited by 64 · see citing works

Novel metabolism of several beta zero‐thalassemic beta‐globin mRNAs in the erythroid tissues of transgenic mice.

Lim, S. K., Mullins, J. J., Chen, C. M., et al. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08401.x · Cited by 55 · see citing works

A polysomal ribonuclease involved in the destabilization of albumin mRNA is a novel member of the peroxidase gene family

Chernokalskaya, E., DUBELL, A. N., Cunningham, K. S., Hanson, M. N., Dompenciel, R. E., & Schoenberg, D. R. (1998) · RNA · doi:10.1017/s1355838298980451 · Cited by 51 · see citing works

Configuration of β-globin messenger RNA in rabbit reticulocytes

Albrecht, G. R., Krówczyńska, A., & Brawerman, G. (1984) · Journal of Molecular Biology · doi:10.1016/0022-2836(84)90317-6 · Cited by 43 · see citing works

mRNA turnover in yeast promoted by the MATalpha1 instability element

Caponigro, G. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.21.4304 · Cited by 34 · see citing works

Purification and RNA Binding Properties of the Polycytidylate-Binding Proteins αCP1 and αCP2

Kiledjian, M., Day, N., & Trifillis, P. (1999) · Methods · doi:10.1006/meth.1998.0710 · Cited by 23 · see citing works

Assignment of Human KH-Box-Containing Genes byin SituHybridization:HNRNPKMaps to 9q21.32–q21.33,PCBP1to 2p12–p13, andPCBP2to 12q13.12–q13.13, Distal toFRA12A

Tommerup, N., & Leffers, H. C. B. (1996) · Genomics · doi:10.1006/geno.1996.0121 · Cited by 22 · see citing works

The cis-acting elements involved in endonucleolytic cleavage of the 3' UTR of human IGF-II mRNAs bind a 50 kDa protein

Scheper, W. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.6.1000 · Cited by 17 · see citing works

Estrogen-induced destabilization and associated degradation intermediates of apolipoprotein II mRNA.

Binder, R., Gordon, D. A., Hwang, S., et al. (1990) · PubMed · Cited by 3 · see citing works

Role of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly

Nakayama, J.-I., Rice, J. C., Strahl, B. D., Allis, C. D., & Grewal, S. I. S. (2001) · Science · doi:10.1126/science.1060118 · Cited by 1,739 · see citing works

Advances in COVID-19 mRNA vaccine development

Fang, E., Liu, X., Li, M., Zhang, Z., Song, L., Zhu, B., Wu, X., Liu, J., Zhao, D., & Li, Y. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00950-y · Cited by 601 · see citing works

Emergence of synthetic mRNA: In vitro synthesis of mRNA and its applications in regenerative medicine

Kwon, H., Kim, M., Seo, Y., Moon, Y. S., Lee, H. J., Lee, K., & Lee, H. (2018) · Biomaterials · doi:10.1016/j.biomaterials.2017.11.034 · Cited by 208 · see citing works

The 64-kilodalton subunit of the CstF polyadenylation factor binds to pre-mRNAs downstream of the cleavage site and influences cleavage site location.

MacDonald, C. C., Wilusz, J., & Shenk, T. E. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.10.6647 · Cited by 234 · see citing works

The 64-Kilodalton Subunit of the CstF Polyadenylation Factor Binds to Pre-mRNAs Downstream of the Cleavage Site and Influences Cleavage Site Location

MacDonald, C. C., Wilusz, J., & Shenk, T. E. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.10.6647-6654.1994 · Cited by 97 · see citing works

A multisubunit factor, CstF, is required for polyadenylation of mammalian pre-mRNAs.Preprint

Takagaki, Y., Manley, J. L., MacDonald, C. C., Wilusz, J., & Shenk, T. E. (1990) · Genes & Development · doi:10.1101/gad.4.12a.2112 · Cited by 232 · see citing works

Sequences downstream of AAUAAA signals affect pre-mRNA cleavage and polyadenylation in vitro both directly and indirectly.

Ryner, L. C., Takagaki, Y., & Manley, J. L. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.4.1759 · Cited by 24 · see citing works

Reconstitution of 3′ end processing of mammalian pre-mRNA reveals a central role of RBBP6Preprint

Schmidt, M., Kluge, F., Sandmeir, F., Kühn, U., Schäfer, P., Tüting, C., Ihling, C. H., Conti, E., & Wahle, E. (2022) · Genes & Development · doi:10.1101/gad.349217.121 · Cited by 52 · see citing works