G E Mortimore

426 citations
11 papers · 383 · h-index 8

Impact in

Papers in

    • Pancreatic function and diabetes 7
    • Autophagy in Disease and Therapy 3
    • Liver Disease Diagnosis and Treatment 2

G E Mortimore

11 papers receiving 356 citations

Peers

G E Mortimore
Comparison fields: 5 of 65
  • Clinical Biochemistry 58
  • Cell Biology 116
  • Biochemistry 50
  • Physiology 116
  • Physiology 17
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Citations per year

Countries citing papers authored by G E Mortimore

Since Specialization
Citations

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

Fields of papers citing papers by G E Mortimore

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by G E Mortimore. 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 G E Mortimore. The network helps show where G E Mortimore may publish in the future.

Co-authors

The 8 scholars most cited alongside G E Mortimore, linked wherever they have co-authored with each other. Click a name or a connecting line to browse the papers they share.

Border = papers with G E Mortimore Line = papers co-authored together G E Mortimore links everyone, so they are left out of the graph.

All Works

11 of 11 papers shown
#Work
1 196890
2 198778
3
Lysosomal pathways in hepatic protein degradation: regulatory role of amino acids.
198450
4 199448
5 196743
6 196737
7
Behavior of the lysosomal system during organ perfusion. An inquiry into the mechanism of hepatic proteolysis.
197617
8
Modulation of kidney cell protein degradation by insulin.
19909
9
Amino acid control of hepatic protein degradation: novel requirement for alanine.
19854
10
Studies on the fate of insulin-I131 in the perfused rat liver.
19594
11
Internalization of cytoplasmic protein by lysosomes as the mechanism of resident protein turnover in liver.
19813

About G E Mortimore

G E Mortimore is a scholar working on Surgery, Epidemiology, Physiology, Clinical Biochemistry and Molecular Biology, having authored 11 papers that have together received 383 indexed citations. Recurring topics across this work include Pancreatic function and diabetes (7 papers), Metabolism, Diabetes, and Cancer (3 papers), Autophagy in Disease and Therapy (3 papers), Liver Disease Diagnosis and Treatment (2 papers), Diet and metabolism studies (1 paper), Lysosomal Storage Disorders Research (1 paper), Biomedical Research and Pathophysiology (1 paper) and Machine Learning in Bioinformatics (1 paper). The work is most often cited by research in Clinical Biochemistry (58 citations), Cell Biology (116 citations), Biochemistry (50 citations), Physiology (116 citations) and Physiology (17 citations). G E Mortimore has collaborated with scholars based in United States, France and Italy. Frequent co-authors include A.R. Pösö, Motoni Kadowaki, Oriano Marin, Giovanni Miotto, Rina Venerando, Noris Siliprandi, Frank Tietze and Ralph Rabkin. Their work appears in journals such as American Journal of Physiology-Legacy Content, Journal of Biological Chemistry and PubMed.

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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