Joseph Krebs

3.8k total citations · 1 hit paper
37 papers, 3.2k citations indexed

About

Joseph Krebs is a scholar working on Molecular Biology, Nutrition and Dietetics and Physical and Theoretical Chemistry. According to data from OpenAlex, Joseph Krebs has authored 37 papers receiving a total of 3.2k indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 8 papers in Nutrition and Dietetics and 5 papers in Physical and Theoretical Chemistry. Recurrent topics in Joseph Krebs's work include Cell death mechanisms and regulation (8 papers), Enzyme function and inhibition (7 papers) and Clinical Nutrition and Gastroenterology (6 papers). Joseph Krebs is often cited by papers focused on Cell death mechanisms and regulation (8 papers), Enzyme function and inhibition (7 papers) and Clinical Nutrition and Gastroenterology (6 papers). Joseph Krebs collaborates with scholars based in United States, Switzerland and Spain. Joseph Krebs's co-authors include Carol A. Fierke, Kevin J. Tomaselli, K J Tomaselli, Robert C. Armstrong, Teresa Fernandes‐Alnemri, L C Fritz, Emad S. Alnemri, Donald S. Karanewsky, Srinivasa M. Srinivasula and Joseph A. Trapani and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Nucleic Acids Research.

In The Last Decade

Joseph Krebs

36 papers receiving 3.1k 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.

In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains.

1996 660 citations Teresa Fernandes‐Alnemri, Robert C. Armstrong et al. Proceedings of the National Academy of Sciences profile →

Peers

Joseph Krebs

IMMUN

ONCOL

EPIDE

Chaohong Sun United States

Robert Eskes Switzerland

Thomas A. Rano United States

Gorka Basáñez Spain

Dita Rasper Canada

Louise Fairall United Kingdom

Ido Goldstein United States

James M. Trevillyan United States

Seong Eon Ryu South Korea

Karen L. Leach United States

Chaohong Sun United States

Joseph Krebs

2.8k ×1.1

399 ×0.6

IMMUN

524 ×1.4

ONCOL

373 ×1.2

EPIDE

262 ×1.0

Citations per year, relative to Joseph Krebs Joseph Krebs (= 1×) peers Chaohong Sun

Countries citing papers authored by Joseph Krebs

Since Specialization

Citations

This map shows the geographic impact of Joseph Krebs'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 Joseph Krebs with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Joseph Krebs more than expected).

Fields of papers citing papers by Joseph Krebs

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Joseph Krebs. 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 Joseph Krebs. The network helps show where Joseph Krebs may publish in the future.

Co-authorship network of co-authors of Joseph Krebs

This figure shows the co-authorship network connecting the top 25 collaborators of Joseph Krebs. A scholar is included among the top collaborators of Joseph Krebs 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 Joseph Krebs. Joseph Krebs 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

Deleyto-Seldas, Nerea, Fernando Garcı́a, Eduardo Caleiras, et al.. (2024). Hepatic nutrient and hormone signaling to mTORC1 instructs the postnatal metabolic zonation of the liver. Nature Communications. 15(1). 1878–1878. 4 indexed citations

Krebs, Joseph, et al.. (2023). Carrageenan-Based Crowding and Confinement Combination Approach to Increase Collagen Deposition for In Vitro Tissue Development. Gels. 9(9). 705–705. 5 indexed citations

Chen, Alan, et al.. (2022). Beyond lipids: Novel mechanisms for parenteral nutrition–associated liver disease. Nutrition in Clinical Practice. 37(2). 265–273. 5 indexed citations

Austin, A, et al.. (2022). Lower systemic inflammation is associated with gut firmicutes dominance and reduced liver injury in a novel ambulatory model of parenteral nutrition. Annals of Medicine. 54(1). 1701–1713. 26 indexed citations

Song, Eric, et al.. (2021). Parenteral Nutrition and Cardiotoxicity. Cardiovascular Toxicology. 21(4). 265–271. 5 indexed citations

Madsen, Erik, A Austin, Eric Song, et al.. (2021). Novel NMP split liver model recapitulates human IRI and demonstrates ferroptosis modulators as a new therapeutic strategy. Pediatric Transplantation. 26(2). e14164–e14164. 3 indexed citations

Towbin, Jeffrey A., et al.. (2019). Concurrent Use of Calcium Chloride and Arginine Vasopressin Infusions in Pediatric Patients with Acute Cardiocirculatory Failure. Pediatric Cardiology. 40(5). 1046–1056. 4 indexed citations

Puthenveetil, Sujiet, Landon R. Whitby, Jin Ren, et al.. (2006). Controlling activation of the RNA-dependent protein kinase by siRNAs using site-specific chemical modification. Nucleic Acids Research. 34(17). 4900–4911. 63 indexed citations

Blanchard, Helen, Lalitha Kodandapani, Peer R. E. Mittl, et al.. (1999). The three-dimensional structure of caspase-8: an initiator enzyme in apoptosis. Structure. 7(9). 1125–1133. 121 indexed citations

10.

Karanewsky, Donald S., et al.. (1998). Conformationally constrained inhibitors of caspase-1 (interleukin-1β converting enzyme) and of the human ced-3 homologue caspase-3 (CPP32, apopain). Bioorganic & Medicinal Chemistry Letters. 8(19). 2757–2762. 36 indexed citations

11.

Srinivasan, Anu, Feng Li, Angela Wong, et al.. (1998). Bcl-xL Functions Downstream of Caspase-8 to Inhibit Fas- and Tumor Necrosis Factor Receptor 1-induced Apoptosis of MCF7 Breast Carcinoma Cells. Journal of Biological Chemistry. 273(8). 4523–4529. 154 indexed citations

12.

Mittl, Peer R. E., Stefania Di Marco, Joseph Krebs, et al.. (1997). Structure of Recombinant Human CPP32 in Complex with the Tetrapeptide Acetyl-Asp-Val-Ala-Asp Fluoromethyl Ketone. Journal of Biological Chemistry. 272(10). 6539–6547. 214 indexed citations

13.

Armstrong, Robert C., Teresa Aja, Jialing Xiang, et al.. (1996). Fas-induced Activation of the Cell Death-related Protease CPP32 Is Inhibited by Bcl-2 and by ICE Family Protease Inhibitors. Journal of Biological Chemistry. 271(28). 16850–16855. 293 indexed citations

14.

Fernandes‐Alnemri, Teresa, Robert C. Armstrong, Joseph Krebs, et al.. (1996). In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains.. Proceedings of the National Academy of Sciences. 93(15). 7464–7469. 660 indexed citations breakdown →

15.

Bertin, John, Susan M. Mendrysa, Douglas LaCount, et al.. (1996). Apoptotic suppression by baculovirus P35 involves cleavage by and inhibition of a virus-induced CED-3/ICE-like protease. Journal of Virology. 70(9). 6251–6259. 149 indexed citations

16.

Krebs, Joseph, et al.. (1995). Detection of a Catalytic Antibody Species Acylated at the Active Site by Electrospray Mass Spectrometry. Biochemistry. 34(3). 720–723. 31 indexed citations

17.

Nair, Satish K., Joseph Krebs, David W. Christianson, & Carol A. Fierke. (1995). Structural basis of inhibitor affinity to variants of human carbonic anhydrase II. Biochemistry. 34(12). 3981–3989. 50 indexed citations

18.

Stewart, John, Joseph Krebs, Gary Siuzdak, et al.. (1994). Dissection of an antibody-catalyzed reaction.. Proceedings of the National Academy of Sciences. 91(16). 7404–7409. 28 indexed citations

19.

Kiefer, Laura L., et al.. (1993). Engineering a cysteine ligand into the zinc binding site of human carbonic anhydrase II. Biochemistry. 32(38). 9896–9900. 48 indexed citations

20.

Fierke, Carol A., Tiffany L. Calderone, & Joseph Krebs. (1991). Functional consequences of engineering the hydrophobic pocket of carbonic anhydrase II. Biochemistry. 30(46). 11054–11063. 109 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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