Jens‐U. Rahfeld - Concepedia

Concepedia

Author

Jens‐U. Rahfeld

Max Planck Research Unit for Enzymology of Protein Folding

Also Known As

J -U Rahfeld, J. U. Rahfeld, J.U. Rahfeld, Jens-U Rahfeld, Jens-U. Rahfeld, Jens‐U. Rahfeld

14

Publications

1.1K

Citations

10

H-Index

16

Concepts

All Affiliations

Max Planck Research Unit for Enzymology of Protein Folding Max Planck Society Martin Luther University Halle-Wittenberg Max Planck Institute of Biochemistry University of Würzburg

JR

About

Jens‐U. Rahfeld is an author at Max Planck Research Unit for Enzymology of Protein Folding specializing in natural sciences, proteomics, and protein synthesis.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Medicine	3	3	433
2	Natural Sciences	3	3	433
3	Biochemistry	2	2	159
4	Cell Biology	1	1	274
5	Microbiology	1	1	58

Jens‐U. Rahfeld

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10

Publications

1.1K

Citations

10

H-Index

	Year	Citations
A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. Gerlind Stoller, K P Rücknagel, K.H. Nierhaus, The EMBO Journal Transcriptional RegulationTrigger FactorNatural SciencesMedicineProtein Biosynthesis	1995	274
Confirmation of the existence of a third family among peptidyl‐prolyl <i>cis/trans</i> isomerases Amino acid sequence and recombinant production of parvulin Jens‐U. Rahfeld, Karl Peter Rücknagel, Birte Schelbert, FEBS Letters	1994	193
A novel peptidyl‐prolyl <i>cisltrans</i> isomerase from <i>Escherichia coli</i> Jens‐U. Rahfeld, Angelika Schierhorn, Karlheinz Mann, FEBS Letters	1994	152
Characterization of <i>Arabidopsis thaliana At</i>FKBP42 that is membrane‐bound and interacts with Hsp90 Thilo Kamphausen, Jörg Fanghänel, D. Neumann, The Plant Journal	2002	112
Mutations in a Peptidylprolyl-cis/trans-isomerase Gene Lead to a Defect in 3′-End Formation of a Pre-mRNA inSaccharomyces cerevisiae Jean Hani, Birte Schelbert, Anne Bernhardt, Journal of Biological Chemistry 3′-End FormationGeneticsMolecular BiologyMolecular GeneticsPpiase Domain	1999	101
Identification and characterization of a 14 kDa human protein as a novel parvulin‐like peptidyl prolyl <i>cis</i>/<i>trans</i> isomerase Takafumi Uchida, Fumihiro Fujimori, Thomas Tradler, FEBS Letters	1999	91
Comparative mutational analysis of peptidyl prolyl <i>cis/trans</i> isomerases: active sites of <i>Escherichia coli</i> trigger factor and human FKBP12 Thomas Tradler, Gerlind Stoller, Karl Peter Rücknagel, FEBS Letters	1997	64
Isolation and Amino Acid Sequence of a New 22-kDa FKBP-like Peptidyl-prolyl cis/trans-Isomerase of Escherichia coli Jens‐U. Rahfeld, K P Rücknagel, Gerlind Stoller, Journal of Biological Chemistry Mature Fkbp22 EnzymeBiosynthesisBiochemistryNatural SciencesMedicine	1996	58
An 11.8 kDa proteolytic fragment of the <i>E. coli</i> trigger factor represents the domain carrying the peptidyl‐prolyl <i>cis/trans</i> isomerase activity Gerlind Stoller, Thomas Tradler, Karl Peter Rücknagel, FEBS Letters	1996	56
A cyclophilin‐like peptidyl‐prolyl cis/trans isomerase from Legionella pneumophila – characterization, molecular cloning and overexpression Bettina Schmidt, Thomas Tradler, Jens‐U. Rahfeld, Molecular Microbiology	1996	38

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