Joseph Schlessinger

Molecular Biology · 1999–2022

A researcher in the Science corpus: 12 papers; trusts 2 researchers and is trusted by 52 researchers here, as inferred from the citation graph.

Subfields

• Molecular Biology — 109 citations into it; #662 of 17,773 by trust here, #1,570 by citations
• Oncology — 49 citations into it; #18 of 1,698 by trust here, #253 by citations
• Cell Biology — 13 citations into it

Whom Joseph Schlessinger trusts overall

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

1. T. Hunter

Who trusts Joseph Schlessinger overall

1. R. Roskoski
2. C. Roy
3. Arnauld Sergé
4. S. Sasagawa
5. Jeffrey L. Wrana
6. Z. Du
7. Boris N. Kholodenko
8. C. Blobel
9. R. Juliano
10. Nicolas Bertaux

Papers from Joseph Schlessinger's perspective

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

1. Improved methods for building protein models in electron density maps and the location of errors in these models.
2. Identification of a novel FGF, FGF-21, preferentially expressed in the liver. (Biochimica et Biophysica Acta)
3. Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. (Cell)
4. Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
5. Mutations Associated with Acquired Resistance to PD-1 Blockade in Melanoma (New England Journal of Medicine)
6. Primary resistance to PD-1 blockade mediated by JAK1/2 mutations (Cancer Discovery)
7. Adaptive resistance to therapeutic PD-1 blockade is associated with upregulation of alternative immune checkpoints (Nature Communications)
8. Regulation of Raf-1 by direct feedback phosphorylation. (Molecules and Cells)
9. Melanoma cell-intrinsic PD-1 receptor functions promote tumor growth (Cell)
10. Nivolumab versus Docetaxel in Advanced Squamous-Cell Non–Small-Cell Lung Cancer (New England Journal of Medicine)

Their papers

• Cell signaling by receptor tyrosine kinases. (2000) — 4,465 citations
• Design of protein-binding proteins from the target structure alone (2022) — 514 citations
• Exome sequencing identifies recurrent somatic RAC1 mutations in melanoma (2012) — 1,151 citations
• Clinical efficacy of a RAF inhibitor needs broad target blockade in BRAF-mutant melanoma (2010) — 1,767 citations
• Cell signaling by receptor-tyrosine kinases (2000) — 4,465 citations
• Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. (2002) — 998 citations
• Discovery of a selective inhibitor of oncogenic B-Raf kinase with potent antimelanoma activity (2008) — 1,352 citations
• Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity. (2000) — 405 citations
• Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization. (2000) — 1,193 citations
• Cellular signaling by fibroblast growth factor receptors. (2005) — 1,938 citations
• Impaired HLA Class I Antigen Processing and Presentation as a Mechanism of Acquired Resistance to Immune Checkpoint Inhibitors in Lung Cancer (2017) — 656 citations
• Structural basis for FGF receptor dimerization and activation. (1999)