Alan R. Fersht

Molecular Biology · 1985–2016

A researcher in the Science corpus: 16 papers; trusts 3 researchers and is trusted by 11 researchers here, as inferred from the citation graph.

Subfields

• Molecular Biology — 89 citations into it; #4,543 of 17,773 by trust here, #5,084 by citations
• Oncology — 75 citations into it; #405 of 1,698 by trust here, #881 by citations
• Materials Chemistry — 15 citations into it; #5,553 of 11,513 by trust here, #6,365 by citations

Whom Alan R. Fersht trusts overall

Their strongest outbound trust, strongest first, inferred from their citations.

1. C. Sherr

Who trusts Alan R. Fersht overall

1. J. Kubelka
2. Vladimir N Uversky
3. I. Korendovych
4. András Szilágyi
5. Frances H. Arnold
6. A. Joerger

Papers from Alan R. Fersht's perspective

Ordered by how strongly the researchers Alan R. Fersht trusts endorse each paper. Same corpus, a different order for every researcher.

1. p53 and human cancer: the first ten thousand mutations. (Advances in Cancer Research)
2. In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2 (Science)
3. Regulation of HDM2 activity by the ribosomal protein L11. (Cancer Cell)
4. Oncogenic mutations of the p53 tumor suppressor: the demons of the guardian of the genome. (Cancer Research)
5. The ARF/p53 pathway. (Current Opinion in Genetics and Development)
6. Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound (Nature Medicine)
7. hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. (Cell)
8. p53 in health and disease (Nature reviews. Molecular cell biology)
9. Human SIR2 deacetylates p53 and antagonizes PML/p53‐induced cellular senescence (EMBO Journal)
10. Small-Molecule Inhibitors of the MDM2-p53 Protein-Protein Interaction to Reactivate p53 Function: A Novel Approach for Cancer Therapy (Annual Review of Pharmacology and Toxicology)

Their papers

• Structure and Function of Intrinsically Disordered Proteins (2009) — 279 citations
• Thermodynamic prediction of protein neutrality. (2004) — 215 citations
• Structural biology of the tumor suppressor p53. (2008) — 681 citations
• PRIMA-1 reactivates mutant p53 by covalent binding to the core domain. (2009) — 595 citations
• Rescuing the function of mutant p53 (2001) — 608 citations
• Is there a unifying mechanism for protein folding? (2003) — 450 citations
• The p53 Pathway: Origins, Inactivation in Cancer, and Emerging Therapeutic Approaches. (2016) — 598 citations
• Awakening guardian angels: drugging the p53 pathway (2009) — 912 citations
• Φ-Analysis at the Experimental Limits: Mechanism of β-Hairpin Formation (2006) — 91 citations
• The crystal structure of human CD1d with and without α-galactosylceramide (2005) — 304 citations
• Binding of Natively Unfolded HIF-1α ODD Domain to p53 (2005) — 99 citations
• Directed evolution of new catalytic activity using the α/β-barrel scaffold (2000) — 178 citations
• A search for single substitutions that eliminate enzymatic function in a bacterial ribonuclease. (1998)
• Principles of protein stability derived from protein engineering experiments (1993)
• Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. (1991)
• Hydrogen bonding and biological specificity analysed by protein engineering (1985)