F. Ulrich Hartl - Concepedia

Author

F. Ulrich Hartl

Max Planck Institute of Biochemistry ORCID

Also Known As

F -U Hartl, F HARTL, F U Hartl, F Ulrich Hartl, F. U. Hartl, F. Ulrich Hartl, F.-U. Hartl, F.-Ulrich Hartl, F.U. Hartl, F.Ulrich Hartl

481

Publications

68.3K

Citations

133

H-Index

150

Concepts

All Affiliations

Max Planck Institute of Biochemistry Ludwig-Maximilians-Universität München Memorial Sloan Kettering Cancer Center Max Planck Society Howard Hughes Medical Institute

About

F. Ulrich Hartl is an author at Max Planck Institute of Biochemistry specializing in molecular biology, natural sciences, and medicine.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Medicine	78	115	25K
2	Natural Sciences	78	121	26.1K
3	Engineering	7	7	593
4	Health Sciences	1	1	47
5	Social Sciences	1	1	96

F. Ulrich Hartl

217

Publications

41.8K

Citations

104

H-Index

Page 1

	Year	Citations
Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent C. Erec Stebbins, Alicia A. Russo, Christine Schneider, Cell	1997	1.4K
Structure of TPR Domain–Peptide Complexes Clemens Scheufler, Achim Brinker, Gleb Bourenkov, Cell Peptide LibraryTpr Domain–peptide ComplexesStructural BiologyBiochemistry	2000	1.2K
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding Thomas Langer, Chi Zen Lu, Harrison Echols, Nature Protein FunctionProtein AssemblyBiochemistryProtein FoldingNatural Sciences	1992	966
Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria Ming Cheng, F. Ulrich Hartl, Jörg Martin, Nature Mitochondrial BiogenesisMitochondrial FunctionBiochemistryProtein FoldingYeast Mitochondria	1989	952
Molecular Chaperones Hsp90 and Hsp70 Deliver Preproteins to the Mitochondrial Import Receptor Tom70 Jason C. Young, Nicholas J. Hoogenraad, F. Ulrich Hartl Cell	2003	896
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate Jörg Martin, Thomas Langer, Raina Boteva, Nature Protein ChemistryChaperonin-mediated Protein FoldingProtein AssemblyProtein FoldingNatural Sciences	1991	858
Amyloid-like Aggregates Sequester Numerous Metastable Proteins with Essential Cellular Functions Heidi Olzscha, Sonya M. Schermann, Andreas C. Woerner, Cell Protein FunctionProtein AssemblyBiochemistryProtein FoldingNatural Sciences	2011	701
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis Joachim Ostermann, Arthur L. Horwich, Walter Neupert, Nature Protein AssemblyBiochemistryProtein FoldingMitochondrial FunctionNatural Sciences	1989	677
Hsp70 and Hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils Paul J. Muchowski, Gregor Schaffar, Annie Sittler, Proceedings of the National Academy of Sciences Protein AssemblyMolecular BiologyProtein Phase SeparationProtein AggregatesProtein Refolding	2000	669
Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli Michael J. Kerner, Dean J. Naylor, Yasushi Ishihama, Cell	2005	664

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