Dieter H. Wolf

14.1k total citations · 2 hit papers
128 papers, 11.2k citations indexed

About

Dieter H. Wolf is a scholar working on Molecular Biology, Cell Biology and Epidemiology. According to data from OpenAlex, Dieter H. Wolf has authored 128 papers receiving a total of 11.2k indexed citations (citations by other indexed papers that have themselves been cited), including 104 papers in Molecular Biology, 78 papers in Cell Biology and 26 papers in Epidemiology. Recurrent topics in Dieter H. Wolf's work include Endoplasmic Reticulum Stress and Disease (68 papers), Ubiquitin and proteasome pathways (50 papers) and Fungal and yeast genetics research (36 papers). Dieter H. Wolf is often cited by papers focused on Endoplasmic Reticulum Stress and Disease (68 papers), Ubiquitin and proteasome pathways (50 papers) and Fungal and yeast genetics research (36 papers). Dieter H. Wolf collaborates with scholars based in Germany, United States and Czechia. Dieter H. Wolf's co-authors include Richard K. Plemper, Thomas Sommer, Javier Bordallo, Wolfgang Heinemeyer, Andreas Finger, Wolfgang Hilt, Alexandra Stolz, Eleonore Fröhlich, Frank Madeo and Martin Ligr and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Dieter H. Wolf

127 papers receiving 11.0k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Oxygen Stress: A Regulator of Apoptosis in Yeast

1999 869 citations Frank Madeo, Eleonore Fröhlich et al. profile →
ER Degradation of a Misfolded Luminal Protein by the Cytosolic Ubiquitin-Proteasome Pathway

1996 604 citations Dieter H. Wolf et al. profile →

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name	h						Papers	Cites
Dieter H. Wolf Germany	54	8.8k	5.4k	2.3k	1.6k	922	128	11.2k
Thomas Sommer Germany	45	6.8k 0.8×	5.1k 0.9×	2.3k 1.0×	823 0.5×	875 0.9×	86	9.4k
Martin Rechsteiner United States	62	12.3k 1.4×	3.9k 0.7×	1.7k 0.8×	3.0k 1.8×	1.7k 1.9×	148	14.5k
Daniel Finley United States	51	13.7k 1.6×	4.9k 0.9×	3.4k 1.5×	3.4k 2.1×	1.1k 1.2×	68	15.4k
Yihong Ye United States	49	6.6k 0.8×	4.8k 0.9×	2.6k 1.1×	977 0.6×	1.0k 1.1×	110	9.9k
Ineke Braakman Netherlands	45	5.2k 0.6×	3.7k 0.7×	1.4k 0.6×	327 0.2×	1.5k 1.6×	100	8.3k
Lars Ellgaard Denmark	37	4.7k 0.5×	4.0k 0.7×	1.2k 0.5×	373 0.2×	1.2k 1.3×	62	7.5k
Stefan Jentsch Germany	64	17.0k 1.9×	4.6k 0.9×	2.4k 1.1×	3.6k 2.2×	1.1k 1.2×	106	19.0k
Raymond L. Erikson United States	62	10.5k 1.2×	4.0k 0.7×	708 0.3×	2.5k 1.5×	1.2k 1.3×	154	13.6k
Gert Kreibich United States	48	5.0k 0.6×	2.5k 0.5×	806 0.4×	581 0.4×	804 0.9×	118	7.7k
Benjamin E. Turk United States	45	6.9k 0.8×	1.3k 0.2×	2.0k 0.9×	1.6k 1.0×	770 0.8×	124	10.3k

Countries citing papers authored by Dieter H. Wolf

Since Specialization

Citations

This map shows the geographic impact of Dieter H. Wolf's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Dieter H. Wolf with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Dieter H. Wolf more than expected).

Fields of papers citing papers by Dieter H. Wolf

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Dieter H. Wolf. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Dieter H. Wolf. The network helps show where Dieter H. Wolf may publish in the future.

Co-authorship network of co-authors of Dieter H. Wolf

This figure shows the co-authorship network connecting the top 25 collaborators of Dieter H. Wolf. A scholar is included among the top collaborators of Dieter H. Wolf based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Dieter H. Wolf. Dieter H. Wolf is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Amm, Ingo, et al.. (2015). Quality Control of a Cytoplasmic Protein Complex. Journal of Biological Chemistry. 290(8). 4677–4687. 20 indexed citations

Amm, Ingo, Thomas Sommer, & Dieter H. Wolf. (2013). Protein quality control and elimination of protein waste: The role of the ubiquitin–proteasome system. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1843(1). 182–196. 353 indexed citations

Stolz, Alexandra, Wolfgang Hilt, Alexander Buchberger, & Dieter H. Wolf. (2011). Cdc48: a power machine in protein degradation. Trends in Biochemical Sciences. 36(10). 515–523. 198 indexed citations

Pfirrmann, Thorsten, et al.. (2011). Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation. FEBS Letters. 585(24). 3856–3861. 38 indexed citations

Stolz, Alexandra & Dieter H. Wolf. (2010). Endoplasmic reticulum associated protein degradation: A chaperone assisted journey to hell. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1803(6). 694–705. 102 indexed citations

Schäfer, Antje, et al.. (2008). Ubiquitin Ligase Hul5 Is Required for Fragment-specific Substrate Degradation in Endoplasmic Reticulum-associated Degradation. Journal of Biological Chemistry. 283(24). 16374–16383. 41 indexed citations

Eisele, Frederik, et al.. (2006). Mutants of the deubiquitinating enzyme Ubp14 decipher pathway diversity of ubiquitin–proteasome linked protein degradation. Biochemical and Biophysical Research Communications. 350(2). 329–333. 15 indexed citations

Schäfer, Antje & Dieter H. Wolf. (2005). Endoplasmic Reticulum-Associated Protein Quality Control and Degradation: Screen for ERAD Mutants After Ethylmethane Sulfonate Mutagenesis. Humana Press eBooks. 301. 283–288. 4 indexed citations

Wolf, Dieter H. & Wolfgang Hilt. (2004). The proteasome: a proteolytic nanomachine of cell regulation and waste disposal. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1695(1-3). 19–31. 203 indexed citations

10.

Ligr, Martin, Eleonore Fröhlich, Frank Madeo, et al.. (2001). The Proteasomal Substrate Stm1 Participates in Apoptosis-like Cell Death in Yeast. Molecular Biology of the Cell. 12(8). 2422–2432. 61 indexed citations

11.

Kiser, Gretchen, Martina Gentzsch, Elisabetta Balzi, et al.. (2001). Expression and Degradation of the Cystic Fibrosis Transmembrane Conductance Regulator in Saccharomyces cerevisiae. Archives of Biochemistry and Biophysics. 390(2). 195–205. 38 indexed citations

12.

Dick, Tobias P., Alexander K. Nussbaum, Martin Deeg, et al.. (1998). Contribution of Proteasomal β-Subunits to the Cleavage of Peptide Substrates Analyzed with Yeast Mutants. Journal of Biological Chemistry. 273(40). 25637–25646. 209 indexed citations

13.

Enenkel, Cordula, et al.. (1998). Mutations in the Yeast Proteasome β-Type Subunit Pre3 Uncover Position-dependent Effects on Proteasomal Peptidase Activity and in Vivo Function. Journal of Biological Chemistry. 273(31). 19443–19452. 20 indexed citations

14.

Hoffmann, Michael, et al.. (1997). Yeast Cycloheximide-resistantcrlMutants Are Proteasome Mutants Defective in Protein Degradation. Molecular Biology of the Cell. 8(12). 2487–2499. 56 indexed citations

15.

Heinemeyer, Wolfgang, et al.. (1996). The Proteasome and Protein Degradation in Yeast. Advances in experimental medicine and biology. 389. 197–202. 7 indexed citations

16.

Enenkel, Cordula, et al.. (1994). PRE3, highly homologous to the human major histocompatibility complex‐linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl‐peptide hydrolyzing activity. FEBS Letters. 341(2-3). 193–196. 70 indexed citations

17.

Fischer, Michael B., et al.. (1994). The 26S proteasome of the yeast Saccharomyces cerevisiae. FEBS Letters. 355(1). 69–75. 31 indexed citations

18.

Wolf, Dieter H., et al.. (1993). Proteasome and cell cycle. FEBS Letters. 336(1). 34–36. 43 indexed citations

19.

Schu, Peter & Dieter H. Wolf. (1991). The proteinase yscA‐inhibitor, I^A₃, gene Studies of cytoplasmic proteinase inhibitor deficiency on yeast physiology. FEBS Letters. 283(1). 78–84. 11 indexed citations

20.

Hirsch, Hans H., et al.. (1988). Aminopeptidase yscII of yeast. European Journal of Biochemistry. 173(3). 589–598. 25 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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