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1
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0000091608
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Pathway and mechanism of initiation of protein synthesis
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Edited by Sonenberg N, Hershey JWB, Mathews MB. Cold Spring Harbor: Cold Spring Harbor Laboratory Press. [Cold Spring Harbor monograph series, 39.]
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Hershey JWB, Merrick WC: Pathway and mechanism of initiation of protein synthesis. In Translational Control of Gene Expression, edn 2. Edited by Sonenberg N, Hershey JWB, Mathews MB. Cold Spring Harbor: Cold Spring Harbor Laboratory Press; 2000:33-88. [Cold Spring Harbor monograph series, 39.].
-
(2000)
Translational Control of Gene Expression, Edn 2
, pp. 33-88
-
-
Hershey, J.W.B.1
Merrick, W.C.2
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2
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0035999793
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Structure and function of bacterial initiation factors
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Boelens R., Gualerzi C.O. Structure and function of bacterial initiation factors. Curr. Protein Pept. Sci. 3:2002;107-119.
-
(2002)
Curr. Protein Pept. Sci.
, vol.3
, pp. 107-119
-
-
Boelens, R.1
Gualerzi, C.O.2
-
3
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-
0033522507
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Structure and interactions of the translation initiation factor eIF1
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Fletcher C.M., Pestova T.V., Hellen C.U.T., Wagner G. Structure and interactions of the translation initiation factor eIF1. EMBO J. 18:1999;2631-2639.
-
(1999)
EMBO J.
, vol.18
, pp. 2631-2639
-
-
Fletcher, C.M.1
Pestova, T.V.2
Hellen, C.U.T.3
Wagner, G.4
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5
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0033963789
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The eIF1A solution structure reveals a large RNA-binding surface important for scanning function
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The authors report the NMR structure of eIF1A, revealing the homology to IF1 and demonstrating the functional importance of residues on the RNA-binding face of the factor
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Battiste J.B., Pestova T.V., Hellen C.U.T., Wagner G. The eIF1A solution structure reveals a large RNA-binding surface important for scanning function. Mol. Cell. 5:2000;109-119 The authors report the NMR structure of eIF1A, revealing the homology to IF1 and demonstrating the functional importance of residues on the RNA-binding face of the factor.
-
(2000)
Mol. Cell
, vol.5
, pp. 109-119
-
-
Battiste, J.B.1
Pestova, T.V.2
Hellen, C.U.T.3
Wagner, G.4
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6
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0037439198
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Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo
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in press
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Olsen DS, Mathew A, Zhang F, Krishnamoorthy T, Phan L, Hinnebusch AG: Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo. EMBO J 2003, in press.
-
(2003)
EMBO J
-
-
Olsen, D.S.1
Mathew, A.2
Zhang, F.3
Krishnamoorthy, T.4
Phan, L.5
Hinnebusch, A.G.6
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7
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85031272540
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Mapping the binding interface between human eIF1A and eIF5B - a new interaction between old partners
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in press
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Marintchev A, Kolupaeva VG, Pestova TV, Wagner G: Mapping the binding interface between human eIF1A and eIF5B - a new interaction between old partners. Proc Natl Acad Sci USA 2003, in press.
-
(2003)
Proc Natl Acad Sci USA
-
-
Marintchev, A.1
Kolupaeva, V.G.2
Pestova, T.V.3
Wagner, G.4
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8
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0035910393
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Crystal structure of an initiation factor bound to the 30S ribosomal subunit
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The authors report the X-ray structure of IF1 bound to the 30S ribosomal subunit, revealing that IF1 binds in the A site
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Carter A.P., Clemons W.M. Jr., Brodersen D.E., Morgan-Warren R.J., Hartsch T., Wimberly B.T., Ramakrishnan V. Crystal structure of an initiation factor bound to the 30S ribosomal subunit. Science. 291:2001;498-501 The authors report the X-ray structure of IF1 bound to the 30S ribosomal subunit, revealing that IF1 binds in the A site.
-
(2001)
Science
, vol.291
, pp. 498-501
-
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Carter, A.P.1
Clemons W.M., Jr.2
Brodersen, D.E.3
Morgan-Warren, R.J.4
Hartsch, T.5
Wimberly, B.T.6
Ramakrishnan, V.7
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9
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0034703718
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X-ray structures of the universal translation initiation factor IF2/eIF5B. Conformational changes on GDP and GTP binding
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The authors report the X-ray structure of eIF5B in complex with GDP, GTP and no nucleotide, revealing lever-type domain rearrangements upon nucleotide binding
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Roll-Mecak A., Cao C., Dever T.E., Burley S.K. X-ray structures of the universal translation initiation factor IF2/eIF5B. Conformational changes on GDP and GTP binding. Cell. 103:2000;781-792 The authors report the X-ray structure of eIF5B in complex with GDP, GTP and no nucleotide, revealing lever-type domain rearrangements upon nucleotide binding.
-
(2000)
Cell
, vol.103
, pp. 781-792
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Roll-Mecak, A.1
Cao, C.2
Dever, T.E.3
Burley, S.K.4
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10
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0037184985
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Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity
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Shin B.-S., Maag D., Roll-Mecak A., Arefin M.S., Burley S.K., Lorsch J.R., Dever T.E. Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity. Cell. 111:2002;1015-1025.
-
(2002)
Cell
, vol.111
, pp. 1015-1025
-
-
Shin, B.-S.1
Maag, D.2
Roll-Mecak, A.3
Arefin, M.S.4
Burley, S.K.5
Lorsch, J.R.6
Dever, T.E.7
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11
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0037007203
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The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors
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The authors report the X-ray structure of eIF2γ, revealing the expected similarity to EF-Tu
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Schmitt E., Blanquet S., Mechulam Y. The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors. EMBO J. 21:2002;1821-1832 The authors report the X-ray structure of eIF2γ, revealing the expected similarity to EF-Tu.
-
(2002)
EMBO J.
, vol.21
, pp. 1821-1832
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Schmitt, E.1
Blanquet, S.2
Mechulam, Y.3
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12
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0037035528
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Structure of the β subunit of translation initiation factor 2 from the archaeon Methanococcus jannaschii: A representative of the eIF2β/eIF5 family of proteins
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The authors report the NMR structure of eIF2β, revealing a clustered localization for the mutations in the Zn-ribbon domain that affect AUG codon recognition
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Cho S., Hoffman D.W. Structure of the β subunit of translation initiation factor 2 from the archaeon Methanococcus jannaschii: a representative of the eIF2β/eIF5 family of proteins. Biochemistry. 41:2002;5730-5742 The authors report the NMR structure of eIF2β, revealing a clustered localization for the mutations in the Zn-ribbon domain that affect AUG codon recognition.
-
(2002)
Biochemistry
, vol.41
, pp. 5730-5742
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Cho, S.1
Hoffman, D.W.2
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13
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-
0037109034
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Translation initiation at non-AUG codons mediated by weakened association of eukaryotic initiation factor (eIF) 2 subunits
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Hashimoto N.N., Carnevalli L.S., Castilho B.A. Translation initiation at non-AUG codons mediated by weakened association of eukaryotic initiation factor (eIF) 2 subunits. Biochem. J. 367:2002;359-368.
-
(2002)
Biochem. J.
, vol.367
, pp. 359-368
-
-
Hashimoto, N.N.1
Carnevalli, L.S.2
Castilho, B.A.3
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14
-
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0037053309
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Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2α
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Nonato M.C., Widom J., Clardy J. Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2α J. Biol. Chem. 277:2002;17057-17061.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 17057-17061
-
-
Nonato, M.C.1
Widom, J.2
Clardy, J.3
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15
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0034960171
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Tight binding of the phosphorylated α subunit of initiation factor 2 (eIF2α) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation
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Krishnamoorthy T., Pavitt G.D., Zhang F., Dever T.E., Hinnebusch A.G. Tight binding of the phosphorylated α subunit of initiation factor 2 (eIF2α) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation. Mol. Cell Biol. 21:2001;5018-5030.
-
(2001)
Mol. Cell Biol.
, vol.21
, pp. 5018-5030
-
-
Krishnamoorthy, T.1
Pavitt, G.D.2
Zhang, F.3
Dever, T.E.4
Hinnebusch, A.G.5
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16
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0036670396
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X-ray crystal structure and functional analysis of vaccinia virus K3L reveals molecular determinants for PKR subversion and substrate recognition
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The authors report the X-ray structure of the K3L protein and, by analyzing mutants of the K3L protein, they map the PKR-binding surface. Additional experiments demonstrate that dimerization of PKR is important for recognition of both eIF2α and the K3L protein
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Dar A.C., Sicheri F. X-ray crystal structure and functional analysis of vaccinia virus K3L reveals molecular determinants for PKR subversion and substrate recognition. Mol. Cell. 10:2002;295-305 The authors report the X-ray structure of the K3L protein and, by analyzing mutants of the K3L protein, they map the PKR-binding surface. Additional experiments demonstrate that dimerization of PKR is important for recognition of both eIF2α and the K3L protein.
-
(2002)
Mol. Cell
, vol.10
, pp. 295-305
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Dar, A.C.1
Sicheri, F.2
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17
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0036409394
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Myxoma virus immunomodulatory protein M156R is a structural mimic of eukaryotic translation initiation factor eIF2α
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Ramelot T.A., Cort J.R., Yee A.A., Liu F., Goshe M.B., Edwards A.M., Smith R.D., Arrowsmith C.H., Dever T.E., Kennedy M.A. Myxoma virus immunomodulatory protein M156R is a structural mimic of eukaryotic translation initiation factor eIF2α J. Mol. Biol. 322:2002;943-954.
-
(2002)
J. Mol. Biol.
, vol.322
, pp. 943-954
-
-
Ramelot, T.A.1
Cort, J.R.2
Yee, A.A.3
Liu, F.4
Goshe, M.B.5
Edwards, A.M.6
Smith, R.D.7
Arrowsmith, C.H.8
Dever, T.E.9
Kennedy, M.A.10
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18
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0032834055
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EIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
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Gingras A.-C., Raught B., Sonenberg N. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 68:1999;913-963.
-
(1999)
Annu. Rev. Biochem.
, vol.68
, pp. 913-963
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Gingras, A.-C.1
Raught, B.2
Sonenberg, N.3
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19
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0002411516
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Physical and functional interactions between the mRNA cap structure and the poly(A) tail
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Edited by Sonenberg N, Hershey JWB, Mathews MB. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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Sachs A: Physical and functional interactions between the mRNA cap structure and the poly(A) tail. In Translational Control of Gene Expression, edn 2. Edited by Sonenberg N, Hershey JWB, Mathews MB. Cold Spring Harbor: Cold Spring Harbor Laboratory Press; 2000:447-466.
-
(2000)
Translational Control of Gene Expression, Edn 2
, pp. 447-466
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Sachs, A.1
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20
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0030728936
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Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP
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Marcotrigiano J., Gingras A.C., Sonenberg N., Burley S.K. Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell. 89:1997;951-961.
-
(1997)
Cell
, vol.89
, pp. 951-961
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-
Marcotrigiano, J.1
Gingras, A.C.2
Sonenberg, N.3
Burley, S.K.4
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21
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0030826444
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Structure of translation factor eIF4E bound to m7GDP and interaction with 4E-binding protein
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Matsuo H., Li H., McGuire A.M., Fletcher C.M., Gingras A.C., Sonenberg N., Wagner G. Structure of translation factor eIF4E bound to m7GDP and interaction with 4E-binding protein. Nat. Struct. Biol. 4:1997;717-724.
-
(1997)
Nat. Struct. Biol.
, vol.4
, pp. 717-724
-
-
Matsuo, H.1
Li, H.2
McGuire, A.M.3
Fletcher, C.M.4
Gingras, A.C.5
Sonenberg, N.6
Wagner, G.7
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22
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0037086471
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Crystal structures of 7-methylguanosine 5′-triphosphate (m(7)GTP)- and P(1)-7-methylguanosine-P(3)-adenosine-5′,5′-triphosphate (m(7)GpppA)-bound human full-length eukaryotic initiation factor 4E: Biological importance of the C-terminal flexible region
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This paper shows that the second nucleotide in the cap structure plays an important role in stabilizing the structure of eIF4E
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Tomoo K., Shen X., Okabe K., Nozoe Y., Fukuhara S., Morino S., Ishida T., Taniguchi T., Hasegawa H., Terashima A.et al. Crystal structures of 7-methylguanosine 5′-triphosphate (m(7)GTP)- and P(1)-7-methylguanosine-P(3)-adenosine-5′,5′-triphosphate (m(7)GpppA)-bound human full-length eukaryotic initiation factor 4E: biological importance of the C-terminal flexible region. Biochem. J. 362:2002;539-544 This paper shows that the second nucleotide in the cap structure plays an important role in stabilizing the structure of eIF4E.
-
(2002)
Biochem. J.
, vol.362
, pp. 539-544
-
-
Tomoo, K.1
Shen, X.2
Okabe, K.3
Nozoe, Y.4
Fukuhara, S.5
Morino, S.6
Ishida, T.7
Taniguchi, T.8
Hasegawa, H.9
Terashima, A.10
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23
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0036307897
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Biophysical studies of eIF4E cap-binding protein: Recognition of mRNA 5′ cap structure and synthetic fragments of eIF4G and 4E-BP1 proteins
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Niedzwiecka A., Marcotrigiano J., Stepinski J., Jankowska-Anyszka M., Wyslouch-Cieszynska A., Dadlez M., Gingras A.-C., Mak P., Darzynkiewicz E., Sonenberg N.et al. Biophysical studies of eIF4E cap-binding protein: recognition of mRNA 5′ cap structure and synthetic fragments of eIF4G and 4E-BP1 proteins. J. Mol. Biol. 319:2002;615-635.
-
(2002)
J. Mol. Biol.
, vol.319
, pp. 615-635
-
-
Niedzwiecka, A.1
Marcotrigiano, J.2
Stepinski, J.3
Jankowska-Anyszka, M.4
Wyslouch-Cieszynska, A.5
Dadlez, M.6
Gingras, A.-C.7
Mak, P.8
Darzynkiewicz, E.9
Sonenberg, N.10
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24
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0037273418
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Phosphorylation of eIF4E attenuates its interaction with mRNA cap analogs by electrostatic repulsion; Intein-mediated protein ligation strategy to obtain phosphorylated protein
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in press
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Zuberek J, Wyslouch-Cieszynska A, Niedzwiecka A, Dadlez M, Stepinski J, Augustyniak W, Gingras A-C, Zhang Z, Burley SK, Sonenberg N et al.: Phosphorylation of eIF4E attenuates its interaction with mRNA cap analogs by electrostatic repulsion; Intein-mediated protein ligation strategy to obtain phosphorylated protein. RNA 2003, in press.
-
(2003)
RNA
-
-
Zuberek, J.1
Wyslouch-Cieszynska, A.2
Niedzwiecka, A.3
Dadlez, M.4
Stepinski, J.5
Augustyniak, W.6
Gingras, A.-C.7
Zhang, Z.8
Burley, S.K.9
Sonenberg, N.10
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25
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0036438924
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Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation?
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Scheper G.C., Proud C.G. Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation? Eur. J. Biochem. 269:2002;5350-5359.
-
(2002)
Eur. J. Biochem.
, vol.269
, pp. 5350-5359
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-
Scheper, G.C.1
Proud, C.G.2
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26
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0036178103
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Phosphorylation of eukaryotic translation initiation factor 4E is critical for growth
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Lachance P.E., Miron M., Raught B., Sonenberg N., Lasko P. Phosphorylation of eukaryotic translation initiation factor 4E is critical for growth. Mol. Cell Biol. 22:2002;1656-1663.
-
(2002)
Mol. Cell Biol.
, vol.22
, pp. 1656-1663
-
-
Lachance, P.E.1
Miron, M.2
Raught, B.3
Sonenberg, N.4
Lasko, P.5
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27
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0027969060
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Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: Increased cap affinity of the phosphorylated form
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Minich W.B., Balasta M.L., Goss D.J., Rhoads R.E. Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: increased cap affinity of the phosphorylated form. Proc. Natl. Acad. Sci. U.S.A. 91:1994;7668-7672.
-
(1994)
Proc. Natl. Acad. Sci. U.S.A.
, vol.91
, pp. 7668-7672
-
-
Minich, W.B.1
Balasta, M.L.2
Goss, D.J.3
Rhoads, R.E.4
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29
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0033152072
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Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G
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Marcotrigiano J., Gingras A.C., Sonenberg N., Burley S.K. Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G. Mol. Cell. 3:1999;707-716.
-
(1999)
Mol. Cell
, vol.3
, pp. 707-716
-
-
Marcotrigiano, J.1
Gingras, A.C.2
Sonenberg, N.3
Burley, S.K.4
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30
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0033597729
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The cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1
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Hershey P.E., McWhirter S.M., Gross J.D., Wagner G., Alber T., Sachs A.B. The cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1. J. Biol. Chem. 274:1999;21297-21304.
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 21297-21304
-
-
Hershey, P.E.1
McWhirter, S.M.2
Gross, J.D.3
Wagner, G.4
Alber, T.5
Sachs, A.B.6
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31
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0035105502
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A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery
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The middle domain of eIF4G serves as the eIF4G core that is sufficient for the support of picornavirus internal ribosome entry site (IRES)-mediated translation. The knowledge of the 3D structure provides the basis for performing biochemical and genetic experiments to understand the molecular mechanism and regulation of eIF4G function
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Marcotrigiano J., Lomakin I.B., Sonenberg N., Pestova T.V., Hellen C.U.T., Burley S.K. A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery. Mol. Cell. 7:2001;193-203 The middle domain of eIF4G serves as the eIF4G core that is sufficient for the support of picornavirus internal ribosome entry site (IRES)-mediated translation. The knowledge of the 3D structure provides the basis for performing biochemical and genetic experiments to understand the molecular mechanism and regulation of eIF4G function.
-
(2001)
Mol. Cell
, vol.7
, pp. 193-203
-
-
Marcotrigiano, J.1
Lomakin, I.B.2
Sonenberg, N.3
Pestova, T.V.4
Hellen, C.U.T.5
Burley, S.K.6
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32
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0035968267
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Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages
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Bushell M., Wood W., Carpenter G., Pain V.M., Morley S.J., Clemens M.J. Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages. J. Biol. Chem. 276:2001;23922-23928.
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 23922-23928
-
-
Bushell, M.1
Wood, W.2
Carpenter, G.3
Pain, V.M.4
Morley, S.J.5
Clemens, M.J.6
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33
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0033546405
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The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3′-poly(A) tail of mRNA. Direct association of eRF3/GSPT with polyadenylate-binding protein
-
Hoshino S., Imai M., Kobayashi T., Uchida N., Katada T. The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3′-poly(A) tail of mRNA. Direct association of eRF3/GSPT with polyadenylate-binding protein. J. Biol. Chem. 274:1999;16677-16680.
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 16677-16680
-
-
Hoshino, S.1
Imai, M.2
Kobayashi, T.3
Uchida, N.4
Katada, T.5
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34
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0032473972
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Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation
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Craig A.W., Haghighat A., Yu A.T., Sonenberg N. Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature. 392:1998;520-523.
-
(1998)
Nature
, vol.392
, pp. 520-523
-
-
Craig, A.W.1
Haghighat, A.2
Yu, A.T.3
Sonenberg, N.4
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35
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0035109013
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Translational repression by a novel partner of human poly(A) binding protein, Paip2
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The authors cloned and characterized a novel PABP-binding protein that inhibits translation by removing PABP from the poly-A tail and by preventing PABP interaction with other partners. These results further demonstrate the importance of PABP in translation
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Khaleghpour K., Svitkin Y.V., Craig A.W., DeMaria C.T., Deo R.C., Burley S.K., Sonenberg N. Translational repression by a novel partner of human poly(A) binding protein, Paip2. Mol. Cell. 7:2001;205-216 The authors cloned and characterized a novel PABP-binding protein that inhibits translation by removing PABP from the poly-A tail and by preventing PABP interaction with other partners. These results further demonstrate the importance of PABP in translation.
-
(2001)
Mol. Cell
, vol.7
, pp. 205-216
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-
Khaleghpour, K.1
Svitkin, Y.V.2
Craig, A.W.3
DeMaria, C.T.4
Deo, R.C.5
Burley, S.K.6
Sonenberg, N.7
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36
-
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0032112017
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Circularization of mRNA by eukaryotic translation initiation factors
-
Wells S.E., Hillner P.E., Vale R.D., Sachs A.B. Circularization of mRNA by eukaryotic translation initiation factors. Mol. Cell. 2:1998;135-140.
-
(1998)
Mol. Cell
, vol.2
, pp. 135-140
-
-
Wells, S.E.1
Hillner, P.E.2
Vale, R.D.3
Sachs, A.B.4
-
37
-
-
0026038913
-
The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency
-
Gallie D.R. The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency. Genes Dev. 5:1991;2108-2116.
-
(1991)
Genes Dev.
, vol.5
, pp. 2108-2116
-
-
Gallie, D.R.1
-
38
-
-
0034100762
-
Eukaryotic translation initiation: There are (at least) two sides to every story
-
Sachs A.B., Varani G. Eukaryotic translation initiation: there are (at least) two sides to every story. Nat. Struct. Biol. 7:2000;356-361.
-
(2000)
Nat. Struct. Biol.
, vol.7
, pp. 356-361
-
-
Sachs, A.B.1
Varani, G.2
-
39
-
-
0035787721
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The mRNA closed loop model: the function of PABP and PABP-interacting proteins in mRNA translation
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Cold Spring Harbor: Cold Spring Harbor Laboratory Press
-
Kahvejian A, Roy G, Sonenberg N: The mRNA closed loop model: the function of PABP and PABP-interacting proteins in mRNA translation. In CSHL Symposia on Quantitative Biology. Cold Spring Harbor: Cold Spring Harbor Laboratory Press; 2001, 66:293-300.
-
(2001)
CSHL Symposia on Quantitative Biology
, vol.66
, pp. 293-300
-
-
Kahvejian, A.1
Roy, G.2
Sonenberg, N.3
-
40
-
-
0034959650
-
Dual interactions of the translational repressor Paip2 with poly(A) binding protein
-
The biochemical and thermodynamic analysis of the interactions between PABP and Paip2 provide a basis for understanding translational inhibition by Paip2
-
Khaleghpour K., Kahvejian A., De Crescenzo G., Roy G., Svitkin Y.V., Imataka H., O'Connor-McCourt M., Sonenberg N. Dual interactions of the translational repressor Paip2 with poly(A) binding protein. Mol. Cell Biol. 21:2001;5200-5213 The biochemical and thermodynamic analysis of the interactions between PABP and Paip2 provide a basis for understanding translational inhibition by Paip2.
-
(2001)
Mol. Cell Biol.
, vol.21
, pp. 5200-5213
-
-
Khaleghpour, K.1
Kahvejian, A.2
De Crescenzo, G.3
Roy, G.4
Svitkin, Y.V.5
Imataka, H.6
O'Connor-McCourt, M.7
Sonenberg, N.8
-
41
-
-
0036096544
-
Paip1 interacts with poly(A) binding protein through two independent binding motifs
-
The authors describe detailed biochemical and thermodynamic analyses of the interactions between Paip1 and PABP
-
Roy G., De Crescenzo G., Khaleghpour K., Kahvejian A., O'Connor-McCourt M., Sonenberg N. Paip1 interacts with poly(A) binding protein through two independent binding motifs. Mol. Cell Biol. 22:2002;3769-3782 The authors describe detailed biochemical and thermodynamic analyses of the interactions between Paip1 and PABP.
-
(2002)
Mol. Cell Biol.
, vol.22
, pp. 3769-3782
-
-
Roy, G.1
De Crescenzo, G.2
Khaleghpour, K.3
Kahvejian, A.4
O'Connor-McCourt, M.5
Sonenberg, N.6
-
44
-
-
0037184899
-
A novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in cap/poly(A)-dependent translation
-
The authors identified the amino acid sequence in GSPT/eRF3 that interacts with PABP. They show that inhibition of this interaction reduced the translation of capped, polyadenylated mRNA. This data support the idea that the GSPT/eRF3 interaction with PABP functions to loop out the 3′ UTR and thus facilitate the recycling of the terminating ribosome on the same mRNA
-
Uchida N., Hoshino S.I., Imataka H., Sonenberg N., Katada T. A novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in cap/poly(A)-dependent translation. J. Biol. Chem. 277:2002;50286-50292 The authors identified the amino acid sequence in GSPT/eRF3 that interacts with PABP. They show that inhibition of this interaction reduced the translation of capped, polyadenylated mRNA. This data support the idea that the GSPT/eRF3 interaction with PABP functions to loop out the 3′ UTR and thus facilitate the recycling of the terminating ribosome on the same mRNA.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 50286-50292
-
-
Uchida, N.1
Hoshino, S.I.2
Imataka, H.3
Sonenberg, N.4
Katada, T.5
-
45
-
-
0032535452
-
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. A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. EMBO J. 17:1998;7480-7489.
-
(1998)
EMBO J.
, vol.17
, pp. 7480-7489
-
-
Imataka, H.1
Gradi, A.2
Sonenberg, N.3
-
46
-
-
0036298692
-
Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization
-
The X-ray structure of the C-terminal domain of NSP3 bound to a fragment (30 aa) of eIF4G explains how PABP-eIF4G interaction could lead to mRNA circularization. The authors employed site-directed mutagenesis to show that NSP3 and PABP use similar hydrophobic residues to bind to a common sequence in eIF4G
-
Groft C.M., Burley S.K. Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization. Mol. Cell. 9:2002;1273-1283 The X-ray structure of the C-terminal domain of NSP3 bound to a fragment (30 aa) of eIF4G explains how PABP-eIF4G interaction could lead to mRNA circularization. The authors employed site-directed mutagenesis to show that NSP3 and PABP use similar hydrophobic residues to bind to a common sequence in eIF4G.
-
(2002)
Mol. Cell
, vol.9
, pp. 1273-1283
-
-
Groft, C.M.1
Burley, S.K.2
-
47
-
-
0037059613
-
Recognition of the rotavirus mRNA 3′ consensus by an asymmetric NSP3 homodimer
-
The X-ray structure of the N-terminal domain of NSP3 reveals the molecular basis for the recognition of the tetranucleotide sequence that is present at the 3′ end of all rotavirus mRNAs
-
Deo R.C., Groft C.M., Rajashankar K.R., Burley S.K. Recognition of the rotavirus mRNA 3′ consensus by an asymmetric NSP3 homodimer. Cell. 108:2002;71-81 The X-ray structure of the N-terminal domain of NSP3 reveals the molecular basis for the recognition of the tetranucleotide sequence that is present at the 3′ end of all rotavirus mRNAs.
-
(2002)
Cell
, vol.108
, pp. 71-81
-
-
Deo, R.C.1
Groft, C.M.2
Rajashankar, K.R.3
Burley, S.K.4
-
48
-
-
0032190508
-
Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F
-
Piron M., Vende P., Cohen J., Poncet D. Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F. EMBO J. 17:1998;5811-5821.
-
(1998)
EMBO J.
, vol.17
, pp. 5811-5821
-
-
Piron, M.1
Vende, P.2
Cohen, J.3
Poncet, D.4
-
49
-
-
0031002350
-
The structure of the translational initiation factor IF1 from E. coli contains an oligomer-binding motif
-
Sette M., van Tilborg P., Spurio R., Kaptein R., Paci M., Gualerzi C.O., Boelens R. The structure of the translational initiation factor IF1 from E. coli contains an oligomer-binding motif. EMBO J. 16:1997;1436-1443.
-
(1997)
EMBO J.
, vol.16
, pp. 1436-1443
-
-
Sette, M.1
Van Tilborg, P.2
Spurio, R.3
Kaptein, R.4
Paci, M.5
Gualerzi, C.O.6
Boelens, R.7
-
52
-
-
0028849240
-
Solution structure of the ribosome-binding domain of E. coli translation initiation factor IF3. Homology with the U1A protein of the eukaryotic spliceosome
-
Garcia C., Fortier P.-L., Blanquet S., Lallemand J.-Y., Dardel F. Solution structure of the ribosome-binding domain of E. coli translation initiation factor IF3. Homology with the U1A protein of the eukaryotic spliceosome. J. Mol. Biol. 254:1995;247-259.
-
(1995)
J. Mol. Biol.
, vol.254
, pp. 247-259
-
-
Garcia, C.1
Fortier, P.-L.2
Blanquet, S.3
Lallemand, J.-Y.4
Dardel, F.5
-
53
-
-
0029111710
-
X-ray crystallography shows that translational initiation factor IF3 consists of two compact α/β domains linked by an α-helix
-
Biou V., Shu F., Ramakrishnan V. X-ray crystallography shows that translational initiation factor IF3 consists of two compact α/β domains linked by an α-helix. EMBO J. 14:1995;4056-4064.
-
(1995)
EMBO J.
, vol.14
, pp. 4056-4064
-
-
Biou, V.1
Shu, F.2
Ramakrishnan, V.3
-
54
-
-
0033570135
-
A phylogenetic approach to target selection for structural genomics: Solution structure of YciH
-
Cort J.R., Koonin E.V., Bash P.A., Kennedy M.A. A phylogenetic approach to target selection for structural genomics: solution structure of YciH. Nucleic Acids Res. 27:1999;4018-4027.
-
(1999)
Nucleic Acids Res.
, vol.27
, pp. 4018-4027
-
-
Cort, J.R.1
Koonin, E.V.2
Bash, P.A.3
Kennedy, M.A.4
-
55
-
-
0035188225
-
Structure and dynamics of translation initiation factor aIF-1A from the archaeon Methanococcus jannaschii determined by NMR spectroscopy
-
Li W., Hoffman D.W. Structure and dynamics of translation initiation factor aIF-1A from the archaeon Methanococcus jannaschii determined by NMR spectroscopy. Protein Sci. 10:2001;2426-2438.
-
(2001)
Protein Sci.
, vol.10
, pp. 2426-2438
-
-
Li, W.1
Hoffman, D.W.2
-
56
-
-
0034700086
-
Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
-
Caruthers J.M., Johnson E.R., McKay D.B. Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. Proc. Natl. Acad. Sci. U.S.A. 97:2000;13080-13085.
-
(2000)
Proc. Natl. Acad. Sci. U.S.A.
, vol.97
, pp. 13080-13085
-
-
Caruthers, J.M.1
Johnson, E.R.2
McKay, D.B.3
-
57
-
-
0032167995
-
Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 Å resolution
-
Kim K.K., Hung L.W., Yokota H., Kim R., Kim S.H. Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 Å resolution. Proc. Natl. Acad. Sci. U.S.A. 95:1998;10419-10424.
-
(1998)
Proc. Natl. Acad. Sci. U.S.A.
, vol.95
, pp. 10419-10424
-
-
Kim, K.K.1
Hung, L.W.2
Yokota, H.3
Kim, R.4
Kim, S.H.5
-
59
-
-
0033578927
-
Recognition of polyadenylate RNA by the poly(A)-binding protein
-
Deo R.C., Bonanno J.B., Sonenberg N., Burley S.K. Recognition of polyadenylate RNA by the poly(A)-binding protein. Cell. 98:1999;835-845.
-
(1999)
Cell
, vol.98
, pp. 835-845
-
-
Deo, R.C.1
Bonanno, J.B.2
Sonenberg, N.3
Burley, S.K.4
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