F. Hartl
Molecular Biology · 2000–2019
A researcher in the Science corpus: 11 papers; trusts 19 researchers and is trusted by 13 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 230 citations into it; #3,227 of 17,773 by trust here, #2,904 by citations
- Cell Biology — 87 citations into it; #264 of 2,073 by trust here, #203 by citations
- Physiology — 50 citations into it
- Aging — 44 citations into it
- Cellular and Molecular Neuroscience — 42 citations into it
- Immunology — 19 citations into it; #628 of 2,160 by trust here, #1,217 by citations
- Spectroscopy — 10 citations into it
Whom F. Hartl trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
- Richard I. Morimoto
- Judith Frydman
- Fabrizio Chiti
- Anat Ben-Zvi
- William E. Balch
- James F Morley
- Mikko Taipale
- Christopher M. Dobson
- Fabio Demontis
- A. Dillin
Who trusts F. Hartl overall
- Christopher M. Dobson
- A. Goldberg
- G. Collins
- Richard I. Morimoto
- Gretchen E. Hofmann
- M. Hipp
- M. Hayer-Hartl
- U. Hartl
- P. Muchowski
- E. Nollen
Papers from F. Hartl's perspective
Ordered by how strongly the researchers F. Hartl trusts endorse each paper. Same corpus, a different order for every researcher.
- Protein misfolding, functional amyloid, and human disease. (Annual Review of Biochemistry)
- Opposing Activities Protect Against Age-Onset Proteotoxicity (Science)
- Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis (Science)
- Biological and chemical approaches to diseases of proteostasis deficiency. (Annual Review of Biochemistry)
- Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. (Genes & Development)
- Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death (Nature)
- Protein folding and misfolding
- Identifying the amylome, proteins capable of forming amyloid-like fibrils (Proceedings of the National Academy of Sciences of the United States of America)
- Principles that govern the folding of protein chains.
- Misfolded proteins partition between two distinct quality control compartments (Nature)
Their papers
- Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. (2000) — 1,225 citations
- Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein (2002) — 3,467 citations
- Molecular chaperone functions in protein folding and proteostasis. (2013) — 1,454 citations
- Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils. (2000) — 709 citations
- Pathways of chaperone-mediated protein folding in the cytosol (2004) — 1,165 citations
- In vivo aspects of protein folding and quality control (2016) — 1,271 citations
- Molecular chaperones in protein folding and proteostasis (2011) — 3,354 citations
- Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. (2011) — 688 citations
- Proteostasis impairment in protein-misfolding and -aggregation diseases. (2014) — 629 citations
- The proteostasis network and its decline in ageing (2019) — 1,284 citations
- Pathways of cellular proteostasis in aging and disease (2018) — 690 citations