G. Kramer

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Specificity of the protein kinase activity associated with the hemin-controlled repressor of rabbit reticulocyte.

G. Kramer, J. M. Cimadevilla, B. Hardesty, 1976, Proceedings of the National Academy of Sciences of the United States of America.

The 90-kilodalton peptide of the heme-regulated eIF-2 alpha kinase has sequence similarity with the 90-kilodalton heat shock protein.

G. Kramer, B. Hardesty, D. W. Rose, 1987, Biochemistry.

Possible involvement of the 90-kDa heat shock protein in the regulation of protein synthesis.

W. Welch, G. Kramer, B. Hardesty, 1989, The Journal of biological chemistry.

Structure, Function, and Genetics of Ribosomes

G. Kramer, B. Hardesty, 1986, Springer Series in Molecular Biology.

An effect of polyethylene glycol 8000 on protein mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and a method for eliminating this effect.

O. W. Odom, G. Kramer, B. Hardesty, 1997, Analytical biochemistry.

Distances between 3' ends of ribosomal ribonucleic acids reassembled into Escherichia coli ribosomes.

O. W. Odom, D. Robbins, G. Kramer, 1980, Biochemistry.

Localization of 3' ends of 5S and 23S rRNAs in reconstituted subunits of Escherichia coli ribosomes.

O. W. Odom, G. Kramer, B. Hardesty, 1981, Proceedings of the National Academy of Sciences of the United States of America.

Globin mRNA translation on Artemia salina ribosomes with components from Friend leukemia cells.

G. Kramer, B. Hardesty, D. Konecki, 1975, European journal of biochemistry.

Elongation and folding of nascent ricin chains as peptidyl-tRNA on ribosomes: the effect of amino acid deletions on these processes.

O. W. Odom, G. Kramer, B. Hardesty, 1995, Journal of molecular biology.

Identification and characterization of archaeal and fungal tRNA methyltransferases.

D. Graham, G. Kramer, 2007, Methods in enzymology.

The 90-kDa component of reticulocyte heme-regulated eIF-2 alpha (initiation factor 2 alpha-subunit) kinase is derived from the beta subunit of spectrin.

G. Kramer, B. Hardesty, W. Kudlicki, 1985, Proceedings of the National Academy of Sciences of the United States of America.

The phosphorylation state of the reticulocyte 90-kDa heat shock protein affects its ability to increase phosphorylation of peptide initiation factor 2 alpha subunit by the heme-sensitive kinase.

G. Kramer, B. Hardesty, R. Szyszka, 1989, Biochemistry.

Regulation of Reticulocyte eIF-2α Kinases by Phosphorylation

G. Kramer, B. Hardesty, W. Kudlicki, 1993 .

Preparation and application of chaperone-deficient Escherichia coli cell-free translation systems.

T. Zhang, G. Kramer, B. Hardesty, 1998, Methods in enzymology.

Eukaryotic protein synthesis initiation factor 2. A target for inactivation by proanthocyanidin.

W. Picking, G. Kramer, B. Hardesty, 1991, European journal of biochemistry.

Partial reaction of peptide initiation inhibited by phosphorylation of either initiation factor eIF-2 or 40S ribosomal proteins.

G. Kramer, B. Hardesty, P. Pinphanichakarn, 1977, Proceedings of the National Academy of Sciences of the United States of America.

Reactivation of thermally inactivated pre‐β‐lactamase by DnaK, DnaJ, and GrpE

G. Kramer, B. Hardesty, D. Mccarthy, 1998, Protein science : a publication of the Protein Society.

An additional serine residue at the C terminus of rhodanese destabilizes the enzyme.

P. Horowitz, G. Kramer, B. Hardesty, 2001, Archives of biochemistry and biophysics.

Separate pyrimidine-nucleotide pools for messenger-RNA and ribosomal-RNA synthesis in HeLa S3 cells.

G. Kramer, H. Hilz, U. Wiegers, 1976, European journal of biochemistry.

Evidence for a second phosphorylation site on eIF‐2α from rabbit reticulocytes

B. Kemp, G. Kramer, B. Hardesty, 1987 .

Cotranslational folding of nascent proteins on Escherichia coli ribosomes.

O. W. Odom, T. Zhang, G. Kramer, 1995, Biochemistry and cell biology = Biochimie et biologie cellulaire.

The Importance of the N-terminal Segment for DnaJ-mediated Folding of Rhodanese While Bound to Ribosomes as Peptidyl-tRNA (*)

O. W. Odom, P. Horowitz, G. Kramer, 1995, The Journal of Biological Chemistry.

GroEL and GroES increase the specific enzymatic activity of newly-synthesized rhodanese if present during in vitro transcription/translation.

P. Horowitz, G. Kramer, B. Hardesty, 1993, Biochemistry.

Phosphorylation of glycogen synthase and of the beta subunit of eukaryotic initiation factor two by a common protein kinase.

A. Depaoli-Roach, P. Roach, G. Kramer, 1981, The Journal of biological chemistry.

Purification and partial characterization of the catalytic subunit of cAMP-dependent protein kinases from reticulocytes.

G. Kramer, B. Hardesty, N. Grankowski, 1979, Archives of biochemistry and biophysics.

ATP requirement for binding of 125I-labeled globin mRNA to Artemia salina ribosomes.

G. Kramer, J. M. Cimadevilla, B. Hardesty, 1976, Archives of biochemistry and biophysics.

Domain Separation Precedes Global Unfolding of Rhodanese*

P. Horowitz, G. Kramer, B. Hardesty, 1999, The Journal of Biological Chemistry.

Different conformations of nascent peptides on ribosomes.

O. W. Odom, G. Kramer, B. Hardesty, 1998, Journal of molecular biology.

The 90,000 dalton heat shock protein, a lot of smoke but no function as yet.

G. Kramer, B. Hardesty, 1989, Biochemistry and cell biology = Biochimie et biologie cellulaire.

Control of eukaryotic protein synthesis by phosphorylation.

G. Kramer, B. Hardesty, P. Pinphanichakarn, 1979, Haematology and blood transfusion.

Chaperone-dependent folding and activation of ribosome-bound nascent rhodanese. Analysis by fluorescence.

O. W. Odom, G. Kramer, B. Hardesty, 1994, Journal of molecular biology.

Two phosphorylation sites on eIF‐2α

G. Kramer, 1990 .

Binding of iodine-labeled mRNA to 40 S ribosomal subunits.

G. Kramer, B. Hardesty, A. Henderson, 1979, Methods in enzymology.

A type 1 phosphoprotein phosphatase active with phosphorylated Mr = 68,000 initiation factor 2 kinase.

G. Kramer, B. Hardesty, W. Kudlicki, 1989, The Journal of biological chemistry.

Co-translational folding.

G. Kramer, B. Hardesty, B Hardesty, 1999, Current opinion in structural biology.

Partial characterization of a 230,000-dalton reticulocyte protein and peptides derived from it that affect the activity of a protein phosphatase.

G. Kramer, B. Hardesty, S. C. Chen, 1984, Journal of Biological Chemistry.

mRNA turnover studies applying labeled uridine require an evaluation of specific radioactivities of UTP and RNA-U.

G. Kramer, H. Hilz, U. Wiegers, 1973, Biochemical and biophysical research communications.

Determination of mRNA half-life in HeLa cultures by a poly(A)-independent direct analysis of specific radioactivity of mRNA.

G. Kramer, W. Rehpenning, H. Hilz, 1975, European journal of biochemistry.

Three phosphorylation sites in elongation factor 2

L. Ovchinnikov, G. Kramer, B. Hardesty, 1990, FEBS letters.

Quantification and characterization of regulin, a Mr-230,000 highly elongated protein of rabbit reticulocytes.

G. Kramer, B. Hardesty, G. Zardeneta, 1988, European journal of biochemistry.

Association of the Heme-Controlled eIF-2α Kinase with Spectrin-Derived Peptides

G. Kramer, B. Hardesty, W. Kudlicki, 1987 .

Involvement of the membrane skeleton in the regulation of the cAMP-independent protein kinase and a protein phosphatase that control protein synthesis.

G. Kramer, B. Hardesty, W. Kudlicki, 1987, Haematology and blood transfusion.

Inhibition of protein synthesis by the β‐subunit of spectrin

G. Kramer, B. Hardesty, W. Kudlicki, 1986 .

Regulin, a cytoskeleton-associated protein affecting phosphorylation-dephosphorylation.

G. Kramer, B. Hardesty, W. Kudlicki, 1985, Haematology and blood transfusion.

The NH2-terminal sequence of the alpha and gamma subunits of eukaryotic initiation factor 2 and the phosphorylation site for the heme-regulated eIF-2 alpha kinase.

G. Kramer, B. Hardesty, R. Wettenhall, 1986, The Journal of biological chemistry.

In vitro protein engineering using synthetic tRNA(Ala) with different anticodons.

O. W. Odom, G. Kramer, B. Hardesty, 1993, Biochemistry.

Determination of specific radioactivity of UTP in HeLa cells by an enzymatic method and its alteration under various growth conditions.

G. Kramer, H. Hilz, K. Klapproth, 1972, Biochimica et biophysica acta.

Polyamines are necessary for maximum in vitro synthesis of globin peptides and play a role in chain initiation.

G. Kramer, B. Hardesty, D. Konecki, 1975, Archives of biochemistry and biophysics.

Dissociation of protein kinase activity and the induction of the antiviral state in a cell line responsive to the antiviral effects of interferon.

R. Saneto, G. Kramer, B. Hardesty, 1981, Biochemical and biophysical research communications.

Partial purification and characterization of a translational inhibitor from Friend leukemia cells.

G. Kramer, B. Hardesty, P. Pinphanichakarn, 1977, The Journal of biological chemistry.

Inhibition of peptide chain initiation by a nonhemin-regulated translational repressor from Friend leukemia cells.

G. Kramer, J. M. Cimadevilla, B. Hardesty, 1975, Archives of biochemistry and biophysics.

Yeast Mitochondrial Initiator tRNA Is Methylated at Guanosine 37 by the Trm5-encoded tRNA (Guanine-N1-)-methyltransferase*

D. Graham, G. Kramer, D. Appling, 2007, Journal of Biological Chemistry.

Folding of a nascent peptide on the ribosome.

G. Kramer, B. Hardesty, 2001, Progress in nucleic acid research and molecular biology.

Single synonymous codon substitution eliminates pausing during chloramphenicol acetyl transferase synthesis on Escherichia coli ribosomes in vitro

P. Horowitz, G. Kramer, B. Hardesty, 2002, FEBS letters.

Fluorophores at the N Terminus of Nascent Chloramphenicol Acetyltransferase Peptides Affect Translation and Movement through the Ribosome*

G. Kramer, B. Hardesty, C. Willms, 2000, The Journal of Biological Chemistry.

2 – Regulation of Eukaryotic Protein Synthesis

G. Kramer, B. Hardesty, 1980 .

High efficiency cell-free synthesis of proteins: refinement of the coupled transcription/translation system.

G. Kramer, B. Hardesty, W. Kudlicki, 1992, Analytical biochemistry.

Ribosomes and ribosomal RNA as chaperones for folding of proteins.

G. Kramer, B. Hardesty, W. Kudlicki, 1997, Folding & design.

Characterization of the C2 subdomain of yeast mitochondrial initiation factor 2.

G. Kramer, D. Appling, C. Garofalo, 2005, Archives of biochemistry and biophysics.

Mammalian Mitochondrial Initiation Factor 2 Supports Yeast Mitochondrial Translation without Formylated Initiator tRNA*

G. Kramer, B. Hardesty, D. Appling, 2003, Journal of Biological Chemistry.

Purification and characterization of yeast mitochondrial initiation factor 2.

G. Kramer, B. Hardesty, D. Appling, 2003, Archives of biochemistry and biophysics.

The effect of a hydrophobic N-terminal probe on translational pausing of chloramphenicol acetyl transferase and rhodanese.

G. Kramer, B. Hardesty, T. Tsalkova, 1999, Journal of molecular biology.

GTP hydrolysis during methionyl-tRNAf binding to 40 S ribosomal subunits and the site of edeine inhibition.

G. Kramer, B. Hardesty, P. Pinphanichakarn, 1978, The Journal of biological chemistry.

Yeast AEP3p Is an Accessory Factor in Initiation of Mitochondrial Translation*

G. Kramer, D. Appling, A. S. Tibbetts, 2009, The Journal of Biological Chemistry.

Truncations at the NH2 Terminus of Rhodanese Destabilize the Enzyme and Decrease Its Heterologous Expression*

J. Chirgwin, P. Horowitz, G. Kramer, 1998, The Journal of Biological Chemistry.

Identification of spectrin-related peptides associated with the reticulocyte heme-controlled alpha subunit of eukaryotic translational initiation factor 2 kinase and of Mr 95,000 peptide that appears to be the catalytic subunit.

R. Read, G. Kramer, B. Hardesty, 1987, The Journal of biological chemistry.

A simple method for the purification of reticulocyte globin messenger ribonucleic acid

G. Kramer, J. M. Cimadevilla, B. Hardesty, 1975, Molecular Biology Reports.

Renaturation of Rhodanese by Translational Elongation Factor (EF) Tu

G. Kramer, B. Hardesty, W. Kudlicki, 1997, The Journal of Biological Chemistry.

Selective determination of mRNA specific radioactivity in HeLa cells without the use of inhibitors.

G. Kramer, H. Hilz, U. Wiegers, 1973, Biochemical and biophysical research communications.

Simultaneous determination of mRNA, 18S and 28S RNA specific radioactivities in HeLa cells.

G. Kramer, H. Hilz, U. Wiegers, 1973, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.

The Conformation and Path of Nascent Proteins in Ribosomes

O. W. Odom, M. Eisenstein, A. Yonath, 1995 .

Inhibition of the release factor-dependent termination reaction on ribosomes by DnaJ and the N-terminal peptide of rhodanese

O. W. Odom, G. Kramer, B. Hardesty, 1995, Journal of bacteriology.

Extension and Folding of Nascent Peptides on Ribosomes

O. W. Odom, G. Kramer, B. Hardesty, 1993 .

Expression of different coding sequences in cell‐free bacterial and eukaryotic systems indicates translational pausing on Escherichia coli ribosomes

G. Kramer, B. Hardesty, V. Ramachandiran, 2000, FEBS letters.

Folding of Nascent Peptides on Ribosomes

G. Kramer, B. Hardesty, T. Tsalkova, 2000 .

N-terminal and C-terminal modifications affect folding, release from the ribosomes and stability of in vitro synthesized proteins.

G. Kramer, B. Hardesty, W. Kudlicki, 1999, The international journal of biochemistry & cell biology.

Binding of an N-terminal Rhodanese Peptide to DnaJ and to Ribosomes*

O. W. Odom, G. Kramer, B. Hardesty, 1996, The Journal of Biological Chemistry.

The molecular chaperone DnaK is not recruited to translating ribosomes that lack trigger factor.

P. Horowitz, G. Kramer, B. Hardesty, 2002, Archives of biochemistry and biophysics.

Cotranslational folding--omnia mea mecum porto?

G. Kramer, B. Hardesty, V. Ramachandiran, 2001, The international journal of biochemistry & cell biology.

Activation and release of enzymatically inactive, full-length rhodanese that is bound to ribosomes as peptidyl-tRNA.

O. W. Odom, G. Kramer, B. Hardesty, 1994, The Journal of biological chemistry.

Development of a chaperone-deficient system by fractionation of a prokaryotic coupled transcription/translation system.

G. Kramer, B. Hardesty, W. Kudlicki, 1994, Analytical biochemistry.

Partial purification and characterization of a 90,000-dalton peptide involved in activation of the eIF-2 alpha protein kinase of the hemin-controlled translational repressor.

G. Kramer, B. Hardesty, M. Wallis, 1980, Biochemistry.

Folding of an enzyme into an active conformation while bound as peptidyl-tRNA to the ribosome.

J. Chirgwin, G. Kramer, B. Hardesty, 1995, Biochemistry.

Fluorescence studies on the interaction of inhibitor 2 and okadaic acid with the catalytic subunit of type 1 phosphoprotein phosphatases.

A. Depaoli-Roach, W. Merlevede, I. Park, 1991, Biochemistry.

Inhibition of peptide initiation by a low molecular weight RNA from rabbit reticulocytes.

C. Dionne, G. Kramer, B. Hardesty, 1982, The Journal of biological chemistry.

Partial reaction of peptide initiation inhibited by the reticulocyte hemin-controlled repressor.

G. Kramer, B. Hardesty, P. Pinphanichakarn, 1976, Biochemical and biophysical research communications.

Translation level control in normal and leukemic cells.

G. Kramer, B. Hardesty, D. Konecki, 1976, Hamatologie und Bluttransfusion.

[51] Polyamines in eukaryotic peptide initiation

O. W. Odom, G. Kramer, B. Hardesty, 1979 .

Phosphorylation reactions that influence the activity of elF-2.

G. Kramer, B. Hardesty, 1981, Current topics in cellular regulation.

[THE INDUCTION OF MUTANTS OF TOBACCO MOSAIC VIRUS BY INCORPORATION OF FLUOROURACIL INTO VIRAL NUCLEIC ACIDS].

G. Kramer, H. Schuster, H. Wittmann, 1964, Zeitschrift fur Naturforschung. Teil B, Chemie, Biochemie, Biophysik, Biologie und verwandte Gebiete.

Position of transfer ribonucleic acid on Escherichia coli ribosomes. Distance from the 3' end of 16S ribonucleic acid to three points on phenylalanine-accepting transfer ribonucleic acid in the donor site of 70S ribosomes.

O. W. Odom, J. Ofengand, D. Robbins, 1981, Biochemistry.

Isolation and partial characterization of an Mr 60,000 subunit of a type 2A phosphatase from rabbit reticulocytes.

G. Kramer, B. Hardesty, S. C. Chen, 1989, The Journal of biological chemistry.

A possible biochemical basis for the use of hyperthermia in the treatment of cancer and virus infection.

G. Kramer, B. Hardesty, A. Henderson, 1981, Haematology and blood transfusion.

Two phosphorylation sites on eIF-2 alpha.

G. Kramer, 1990, FEBS letters.

Yeast AEP3p Is an Accessory Factor in Initiation of Mitochondrial Translation*

G. Kramer, D. Appling, A. S. Tibbetts, 2009, The Journal of Biological Chemistry.

Initiation of protein synthesis with fluorophore-Met-tRNA(f) and the involvement of IF-2.

G. Kramer, B. Hardesty, B. McIntosh, 2000, Biochimie.

The isolation and partial characterization of two substrate-specific protein activators of the reticulocyte phosphoprotein phosphatase.

G. Kramer, B. Hardesty, N. Grankowski, 1980, The Journal of biological chemistry.

Partial purification and characterization of reticulocyte phosphatase with activity for phosphorylated peptide initiation factor 2.

G. Kramer, B. Hardesty, N. Grankowski, 1980, The Journal of biological chemistry.

No effect of cAMP on protein synthesis in reticulocyte lysates.

G. Kramer, B. Hardesty, N. Grankowski, 1979, The Journal of biological chemistry.