C. Herring

发表

De novo peptide sequencing in an ion trap mass spectrometer with 18O labeling.

X. Zhang, J. Qin, C. Herring, 1998, Rapid communications in mass spectrometry : RCM.

Domain antibodies: proteins for therapy.

Lucy J. Holt, I. Tomlinson, C. Herring, 2003, Trends in biotechnology.

Expression levels of the DNA repair enzyme HAP1 do not correlate with the radiosensitivities of human or HAP1-transfected rat cell lines

J H Hendry, J. Hendry, C. Herring, 1999, British Journal of Cancer.

Levels of the DNA repair enzyme human apurinic/apyrimidinic endonuclease (APE1, APEX, Ref-1) are associated with the intrinsic radiosensitivity of cervical cancers.

J. Hendry, G. Margison, C. West, 1998, British Journal of Cancer.

Effect of mutating the regulatory phosphoserine and conserved threonine on the activity of the expressed catalytic domain of Acanthamoeba myosin I heavy chain kinase.

J. Qin, J. Gruschus, J. Szczepanowska, 1998, Proceedings of the National Academy of Sciences of the United States of America.

An on-line preconcentrator and the evaluation of electrospray interfaces for the capillary electrophoresis/mass spectrometry of peptides.

J. Qin, C. Herring, 1999, Rapid communications in mass spectrometry : RCM.

Evidence for the existence of cytochrome P450 gene families (CYP1A, 3A, 4A, 11A) and modulation of gene expression (CYP1A) in the mussel Mytilus spp.

A. Wiseman, C. Herring, D. Livingstone, 1995 .

Profiling of acyl-CoA oxidase-deficient and peroxisome proliferator Wy14,643-treated mouse liver protein by surface-enhanced laser desorption/ionization ProteinChip Biology System.

R. Chu, A. Yeldandi, C. Herring, 2002, Gene expression.

Identification of a phosphoenolpyruvate:fructose phosphotransferase system (fructose-1-phosphate forming) in Listeria monocytogenes

M. Saier, C. Hoischen, J. Reizer, 1993, Journal of bacteriology.

Identification by mass spectrometry of the phosphorylated residue responsible for activation of the catalytic domain of myosin I heavy chain kinase, a member of the PAK/STE20 family.

J. Qin, X. Zhang, J. Szczepanowska, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Protein profiling of mouse livers with peroxisome proliferator-activated receptor alpha activation.

Hong Liu, P. Ulintz, R. Chu, 2004, Molecular and cellular biology.

Adenosine metabolism: modification by S-adenosylhomocysteine and 5'-methylthioadenosine.

C. Herring, T. Palella, I. Fox, 1982, Archives of biochemistry and biophysics.

Stimulation of the activity of prolyl hydroxylase in 3T3 fibroblasts by 1,10-phenanthroline.

C. Herring, M. Chvapil, R. Misiorowski, 1977, Biochimica et biophysica acta.

In situ kinase profiling reveals functionally relevant properties of native kinases.

N. Gray, H. Weissig, Jiing-Dwan Lee, 2011, Chemistry & biology.

Autophosphorylation in the Activation Loop Is Required for Full Kinase Activity In Vivo of Human and Yeast Eukaryotic Initiation Factor 2α Kinases PKR and GCN2

A. Hinnebusch, J. Qin, M. Mathews, 1998, Molecular and Cellular Biology.

Anti-serum albumin domain antibodies in the development of highly potent, efficacious and long-acting interferon.

Lucy J. Holt, C. Herring, L. Holt, 2010, Protein engineering, design & selection : PEDS.

Identification of in-vivo Phosphorylation Sites with Mass Spectrometry

J. Qin, Xiaolong Zhang, C. Herring, 2000 .

Identification of phosphorylation sites in proteins separated by polyacrylamide gel electrophoresis.

A. Hinnebusch, P. Romano, J. Qin, 1998, Analytical chemistry.

Protein Profiling of Mouse Livers with Peroxisome Proliferator-Activated Receptor α Activation

Hong Liu, P. Ulintz, R. Chu, 2004, Molecular and Cellular Biology.

AlbudAb™ Technology Platform–Versatile Albumin Binding Domains for the Development of Therapeutics with Tunable Half‐Lives

O. Schon, C. Herring, 2012 .

Anti-serum albumin domain antibodies in the development of highly potent, efficacious and long-acting interferon.

Lucy J. Holt, C. Herring, L. Jespers, 2010, Protein engineering, design & selection : PEDS.