V. M. Pain

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Initiation of protein synthesis in eukaryotic cells.

V. M. Pain, 1996, European journal of biochemistry.

Differential requirements for caspase‐8 activity in the mechanism of phosphorylation of eIF2α, cleavage of eIF4GI and signaling events associated with the inhibition of protein synthesis in apoptotic Jurkat T cells

M. Clemens, M. Bushell, V. M. Pain, 2000, FEBS letters.

The Association of Initiation Factor 4F with Poly(A)-binding Protein Is Enhanced in Serum-stimulated Xenopus Kidney Cells*

C. Fraser, V. M. Pain, S. Morley, 1999, The Journal of Biological Chemistry.

MECHANISM AND REGULATION OF PROTEIN BIOSYNTHESIS IN EUKARYOTIC CELLS

M. Clemens, V. M. Pain, 1980 .

Purification and phosphorylation of initiation factor eIF‐2 from rabbit skeletal muscle

C. Proud, V. M. Pain, 1982, FEBS letters.

Compartmentalisation and localisation of the translation initiation factor (eIF) 4F complex in normally growing fibroblasts.

V. M. Pain, S. Morley, M. Willett, 2006, Experimental cell research.

Expression of fragments of translation initiation factor eIF4GI reveals a nuclear localisation signal within the N-terminal apoptotic cleavage fragment N-FAG

V. M. Pain, S. Morley, T. Hinton, 2004, Journal of Cell Science.

Effect of streptozotocin diabetes and insulin treatment on the rate of protein synthesis in tissues of the rat in vivo.

P. Garlick, V. M. Pain, 1974, The Journal of biological chemistry.

Protein metabolism in skeletal muscle, diaphragm, and heart of diabetic rats.

P. Garlick, V. M. Pain, E. Albertse, 1983, The American journal of physiology.

Translational control during amino acid starvation.

V. M. Pain, 1994, Biochimie.

Analysis of translational activity of extracts derived from oocytes and eggs of Xenopus laevis.

R. Cox, V. M. Pain, S. Morley, 1998, Methods in molecular biology.

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*

M. Clemens, M. Bushell, V. M. Pain, 2001, The Journal of Biological Chemistry.

Effect of diabetes on the ultrastructure of the hepatocyte and on the distribution and activity of ribosomes in the free and membrane-bound populations.

M. Clemens, J. Bergeron, V. M. Pain, 1974, Biochimica et biophysica acta.

Effects of starvation, diabetes and acute insulin treatment on the regulation of polypeptide-chain initiation in rat skeletal muscle.

C. Proud, V. M. Pain, C. Harmon, 1984, The Biochemical journal.

Conditions that alter rates of tissue protein synthesis in vivo.

M. McNurlan, P. Garlick, V. M. Pain, 1980, Biochemical Society transactions.

Protein synthesis in liver and skeletal muscle of mice bearing an ascites tumor.

P. Garlick, V. M. Pain, D. P. Randall, 1984, Cancer research.

The role of soluble protein factors in the translational control of protein synthesis in eukaryotic cells

M. Clemens, V. M. Pain, Virginia M. Pain, 1973, FEBS letters.

Translation initiation factor 4E.

L. McKendrick, V. M. Pain, S. Morley, 1999, The international journal of biochemistry & cell biology.

The effects of amino acid starvation on regulation of polypeptide chain initiation in Ehrlich ascites tumor cells.

M. Clemens, J. Lewis, E. Henshaw, 1980, The Journal of biological chemistry.

Initiation of protein synthesis in Ehrlich ascites tumour cells. Evidence for physiological variation in the association of methionyl-tRNAf with native 40-S ribosomal subunits in vivo.

E. Henshaw, V. M. Pain, 1975, European journal of biochemistry.

Protein synthesis in a postmitochondrial supernatant system from rat liver. An effect of diabetes at the level of peptide chain initiation.

V. M. Pain, 1973, FEBS letters.

Initiation of protein synthesis in mammalian cells.

V. M. Pain, 1986, The Biochemical journal.

The Histone 3′-Terminal Stem-Loop-Binding Protein Enhances Translation through a Functional and Physical Interaction with Eukaryotic Initiation Factor 4G (eIF4G) and eIF3

W. Marzluff, V. M. Pain, D. Gallie, 2002, Molecular and Cellular Biology.

Proteolytic cleavage of initiation factor eIF-4 gamma in the reticulocyte lysate inhibits translation of capped mRNAs but enhances that of uncapped mRNAs.

V. M. Pain, T. Ohlmann, S. Morley, 1995, Nucleic acids research.

Proteasome inhibitors and immunosuppressive drugs promote the cleavage of eIF4GI and eIF4GII by caspase‐8‐independent mechanisms in Jurkat T cell lines

V. M. Pain, S. Morley, 2001, FEBS letters.

The proteolytic cleavage of eukaryotic initiation factor (eIF) 4G is prevented by eIF4E binding protein (PHAS‐I; 4E‐BP1) in the reticulocyte lysate

V. M. Pain, T. Ohlmann, S. Morley, 1997, The EMBO journal.

Effect of diabetes on the rates of synthesis and degradation of ribosomes in rat muscle and liver in vivo.

A. Ashford, V. M. Pain, 1986, The Journal of biological chemistry.

Influence of streptozotocin diabetes on the ability of muscle cell sap to support protein synthesis by ribosomes in cell-free systems.

V. M. Pain, 1973, Biochimica et biophysica acta.

Phosphorylation of eukaryotic initiation factor 4E (eIF4E) at Ser209 is not required for protein synthesis in vitro and in vivo.

L. McKendrick, R. Jagus, V. M. Pain, 2001, European journal of biochemistry.

Hormonal requirements for acute stimulation of rat liver polysome formation by amino acid feeding.

M. Clemens, V. M. Pain, 1974, Biochimica et biophysica acta.

Effect of starvation and diabetes on the activity of the eukaryotic initiation factor eIF-2 in rat skeletal muscle.

F. Kelly, J. Hershey, V. M. Pain, 1990, Biochimie.

Cellular stress in xenopus kidney cells enhances the phosphorylation of eukaryotic translation initiation factor (eIF)4E and the association of eIF4F with poly(A)-binding protein.

C. Fraser, V. M. Pain, S. Morley, 1999, The Biochemical journal.

Stimulation by insulin of protein synthesis in cultured chick embryo fibroblasts.

V. M. Pain, I. Jeffrey, 1993, Biochimie.

Cellular stress in xenopus kidney cells enhances the phosphorylation of eukaryotic translation initiation factor (eIF)4E and the association of eIF4F with poly(A)-binding protein.

C. Fraser, V. M. Pain, S. Morley, 1999, The Biochemical journal.

Phosphorylation inhibits guanine nucleotide exchange on eukaryotic initiation factor 2

M. Clemens, E. Henshaw, V. M. Pain, 1982, Nature.

A fractionated reticulocyte lysate system for studies on protein synthesis initiation factors.

V. M. Pain, T. Ohlmann, S. Morley, 1998, Methods in molecular biology.

Regulation of binding of initiator tRNA to eukaryotic initiation factor eIF‐2

C. Proud, M. Clemens, V. M. Pain, 1982, FEBS letters.

Translational Control of Gene Expression , edited by Nahum Sonenberg, John W.B. Hershey, and Michael B. Mathews. 2000. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press. Cloth, 1,020 pp. $113.

N. Standart, V. M. Pain, 2001 .

Preparation and characterization of cell-free protein synthesis systems from oocytes and eggs of Xenopus laevis.

V. M. Pain, T. Patrick, C. E. Lewer, 1989, Development.

The effect of dietary protein deficiency on albumin synthesis and on the concentration of active albumin messenger ribonucleic acid in rat liver.

M. Clemens, P. Garlick, V. M. Pain, 1978, The Biochemical journal.

Protein turnover in tissues of diabetic rats.

M. McNurlan, P. Garlick, V. M. Pain, 1981, Acta biologica et medica Germanica.

The metabolic state of muscle in the isolated perfused rat hemicorpus in relation to rates of protein synthesis.

V. Preedy, P. Garlick, V. M. Pain, 1984, The Biochemical journal.

eIF4G: translation's mystery factor begins to yield its secrets.

V. M. Pain, S. Morley, P. S. Curtis, 1997, RNA.

Stimulation of initiation factor eIF-2 by a rat liver protein with GDPase activity.

M. Clemens, V. M. Pain, V. Tilleray, 1980, Biochemical and biophysical research communications.

Translation initiation factor modifications and the regulation of protein synthesis in apoptotic cells

M J Clemens, M. Clemens, M. Bushell, 2000, Cell Death and Differentiation.

The role of 5'-leader length, secondary structure and PABP concentration on cap and poly(A) tail function during translation in Xenopus oocytes.

M. Niepel, V. M. Pain, D. Gallie, 2000, Nucleic acids research.

Characterization fo a macromolecular inhibitor of polypeptide chain initiation from ehrlich ascites tumor cells

I. London, M. Clemens, E. Henshaw, 1976 .

Hormone-induced meiotic maturation in Xenopus oocytes occurs independently of p70s6k activation and is associated with enhanced initiation factor (eIF)-4F phosphorylation and complex formation.

V. M. Pain, S. Morley, 1995, Journal of cell science.

Increased phosphorylation of eukaryotic initiation factor 4 alpha during early activation of T lymphocytes correlates with increased initiation factor 4F complex formation.

V. M. Pain, S. Morley, J. Kay, 1993, European journal of biochemistry.

A Reevaluation of the Cap-binding Protein, eIF4E, as a Rate-limiting Factor for Initiation of Translation in Reticulocyte Lysate (*)

V. M. Pain, T. Ohlmann, S. Morley, 1996, The Journal of Biological Chemistry.

Functional Analysis of Individual Binding Activities of the Scaffold Protein eIF4G*

V. M. Pain, S. Morley, T. Hinton, 2007, Journal of Biological Chemistry.

Investigation of the role of uncharged tRNA in the regulation of polypeptide chain initiation by amino acid starvation in cultured mammalian cells; a reappraisal.

M. Clemens, S. Austin, J. Lewis, 2005, European journal of biochemistry.

Assembly and breakdown of mammalian protein synthesis initiation complexes: regulation by guanine nucleotides and by phosphorylation of initiation factor eIF-2.

M. Clemens, V. M. Pain, 1983, Biochemistry.

Inhibition of Protein Synthesis by the Heme-Controlled Eif-2α kinase Leads to the Appearance of mRNA-Containing 48S Complexes that Contain eIF-4E but Lack Methionyl-tRNAf

R. Rhoads, V. M. Pain, S. Morley, 1995 .

Inhibition of protein synthesis by the heme-controlled eIF-2 alpha kinase leads to the appearance of mRNA-containing 48S complexes that contain eIF-4E but lack methionyl-tRNA(f).

R. Rhoads, V. M. Pain, S. Morley, 1995, European journal of biochemistry.

Radioactive puromycin formation as an assay for the proportion of active ribosomes in mammalian cells: correlation with polysome profiles under different physiological conditions.

V. M. Pain, B. Unsworth, 1983, Life sciences.

Translational regulation during activation of porcine peripheral blood lymphocytes: association and phosphorylation of the alpha and gamma subunits of the initiation factor complex eIF-4F.

V. M. Pain, S. Morley, 1995, The Biochemical journal.

Insulin stimulation of growth in diabetic rats. Synthesis and degradation of ribosomes and total tissue protein in skeletal muscle and heart.

A. Ashford, V. M. Pain, 1986, The Journal of biological chemistry.

Protein synthesis in vivo during pregnancy and lactation in the mouse

V. M. Pain, R. Vernon, P. Millican, 1985 .

The C‐terminal domain of eukaryotic protein synthesis initiation factor (eIF) 4G is sufficient to support cap‐independent translation in the absence of eIF4E.

V. M. Pain, T. Ohlmann, S. Morley, 1996, The EMBO journal.

Overproduction of a conserved domain of fission yeast and mammalian translation initiation factor eIF4G causes aberrant cell morphology and results in disruption of the localization of F‐actin and the organization of microtubules

V. M. Pain, S. Morley, J. Thorpe, 2003, Genes to cells : devoted to molecular & cellular mechanisms.

The effect of an Ehrlich ascites tumour on the rate of protein synthesis in muscle and liver of the host [proceedings].

P. Garlick, V. M. Pain, 1980, Biochemical Society transactions.

Association of initiation factor eIF-2 with a rapidly sedimenting fraction from Ehrlich ascites-tumour cells.

M. Clemens, V. M. Pain, 1981, The Biochemical journal.

Characterization of a macromolecular inhibitor of polypeptide chain initiation from Ehrlich ascites tumor cells.

I. London, M. Clemens, E. Henshaw, 1976, Biochemical and biophysical research communications.

Regulation of binding of initiator tRNA to eukaryotic initiation factor eIF‐2

C. Proud, M. Clemens, V. M. Pain, 1982, FEBS letters.

Stimulation of rat liver initiation factor eIF-2 by a factor with guanosine diphosphase activity [proceedings].

M. Clemens, V. M. Pain, V. Tilleray, 1980, Biochemical Society transactions.