Christopher J. Oldfield

Molecular Biology · 2001–2016

A researcher in the Science corpus: 17 papers; trusts 41 researchers and is trusted by 45 researchers here, as inferred from the citation graph.

Subfields

• Molecular Biology — 422 citations into it; #502 of 17,773 by trust here, #716 by citations
• Materials Chemistry — 162 citations into it; #792 of 11,513 by trust here, #1,810 by citations
• Cell Biology — 60 citations into it; #1,549 of 2,073 by trust here, #945 by citations
• Spectroscopy — 55 citations into it
• Computational Biology & Bioinformatics — 37 citations into it
• Physiology — 10 citations into it

Whom Christopher J. Oldfield trusts overall

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

1. Vladimir N Uversky
2. A. Keith Dunker
3. Pedro Romero
4. Zoran Obradovic
5. C. Brown
6. Lilia M. Iakoucheva
7. Predrag Radivojac
8. Peter Tompa
9. Peter E. Wright
10. H. J. Dyson

Who trusts Christopher J. Oldfield overall

1. Vladimir N Uversky
2. A. Keith Dunker
3. Bálint Mészáros
4. Sheng Wang
5. Zhenling Peng
6. Fanchi Meng
7. Lukasz Kurgan
8. Jack Hanson
9. Nawar Malhis
10. Predrag Radivojac

Papers from Christopher J. Oldfield's perspective

Ordered by how strongly the researchers Christopher J. Oldfield trusts endorse each paper. Same corpus, a different order for every researcher.

1. Intrinsically disordered protein.
2. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.
3. Coupling of folding and binding for unstructured proteins.
4. Intrinsic disorder and protein function. (Biochemistry)
5. GlobPlot: exploring protein sequences for globularity and disorder
6. Intrinsically unstructured proteins. (TIBS -Trends in Biochemical Sciences. Regular ed)
7. Statistics of Local Complexity in Amino Acid Sequences and Sequence Databases
8. The importance of intrinsic disorder for protein phosphorylation. (Nucleic Acids Research)
9. Twilight zone of protein sequence alignments.
10. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life.

Their papers

• Intrinsic disorder and functional proteomics. (2007) — 690 citations
• Intrinsically disordered protein. (2001) — 1,652 citations
• Analysis of molecular recognition features (MoRFs). (2006) — 725 citations
• Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling (2005) — 826 citations
• Intrinsic disorder in transcription factors. (2006) — 727 citations
• Intrinsic Disorder Is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes (2006) — 576 citations
• Intrinsically disordered proteins in human diseases: introducing the D2 concept. (2008) — 1,356 citations
• Comparing and combining predictors of mostly disordered proteins. (2005) — 513 citations
• Intrinsically disordered proteins and intrinsically disordered protein regions. (2014) — 953 citations
• Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners (2008) — 594 citations
• Characterization of molecular recognition features, MoRFs, and their binding partners. (2007) — 473 citations
• Coupled folding and binding with α-helix-forming molecular recognition elements (2005) — 574 citations
• MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins (2012) — 340 citations
• Classification of Intrinsically Disordered Regions and Proteins (2014) — 1,960 citations
• DisProt 7.0: a major update of the database of disordered proteins (2016) — 138 citations
• Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions. (2007) — 532 citations
• DisProt 7.0: a major update of the database of disordered proteins (2016) — 203 citations