A. Sparks

发表

Activation of p53 protein function in response to cellular irradiation.

T. Hupp, J. Blaydes, A. Sparks, 1999, Methods in molecular biology.

Transcription Factor E2F-1 Is Upregulated in Response to DNA Damage in a Manner Analogous to That of p53

C. Blattner, A. Sparks, David Lane, 1999, Molecular and Cellular Biology.

Immunochemical analysis of the interaction of p53 with MDM2;--fine mapping of the MDM2 binding site on p53 using synthetic peptides.

D. Lane, B. Vojtesek, S. Picksley, 1994, Oncogene.

p53 is activated in response to disruption of the pre-mRNA splicing machinery

M. Saville, J. Bourdon, A. Sparks, 2013, Oncogene.

p14 Arf Promotes Small Ubiquitin-like Modifier Conjugation of Werners Helicase*

A. Prescott, D. Lane, M. Saville, 2004, Journal of Biological Chemistry.

Defective nuclear localization of p53 protein in a Chinese hamster cell line is associated with the formation of stable cytoplasmic protein multimers in cells with gene amplification.

D. Lane, G. Fronza, P. Campomenosi, 2000, Carcinogenesis.

Binding to intracellular targets of the metastasis-inducing protein, S100A4 (p9Ka).

P. Rudland, R. Barraclough, A. Sparks, 2001, Biochemical and biophysical research communications.

Ubiquitin receptors play redundant roles in the proteasomal degradation of the p53 repressor MDM2

M. Saville, A. Sparks, C. J. Kelly, 2022, FEBS letters.

Suppression of the Deubiquitinating Enzyme USP5 Causes the Accumulation of Unanchored Polyubiquitin and the Activation of p53*

D. Lane, M. Saville, A. Sparks, 2009, Journal of Biological Chemistry.

The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2

M. Saville, D. Xirodimas, A. Sparks, 2007, The EMBO journal.

Design of a synthetic Mdm2-binding mini protein that activates the p53 response in vivo

David P. Lane, D. Lane, Wei-Li Liu, 1997, Current Biology.

An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo

D. Lane, M. Saville, R. Hay, 2000, Oncogene.

Regulation of p53 by the Ubiquitin-conjugating Enzymes UbcH5B/C in Vivo*

D. Lane, M. Saville, J. Bourdon, 2004, Journal of Biological Chemistry.

The deubiquitinating enzyme USP 2 a regulates the p 53 pathway by targeting Mdm 2

D. Lane, M. Saville, D. Xirodimas, 2013 .

An inhibitor of nuclear export activates the p53 response and induces the localization of HDM2 and p53 to U1A-positive nuclear bodies associated with the PODs.

E. Lane, D. Lane, C. Midgley, 1999, Experimental cell research.

MdmX is a substrate for the deubiquitinating enzyme USP2a

D. Lane, M. Saville, A. Sparks, 2010, Oncogene.

Small peptides activate the latent sequence-specific DNA binding function of p53

D. Lane, T. Hupp, A. Sparks, 1995, Cell.

Cell type-specific responses of human cells to inhibition of replication licensing

D. Lane, S. Shreeram, A. Sparks, 2002, Oncogene.

The degradation of p53 and its major E3 ligase Mdm2 is differentially dependent on the proteasomal ubiquitin receptor S5a

M. Saville, A. Sparks, S. Dayal, 2013, Oncogene.

Naphthyl dioxetane phosphates: synthesis of novel substrates for enzymic chemiluminescent assays

A. Sparks, I. Bronstein, J. Voyta, 1990 .

Epitope analysis of the murine p53 tumour suppressor protein.

D. Lane, B. Vojtesek, T. Hupp, 1996, Oncogene.