I. Berg

Ecology · Applied and Environmental Microbiology · 2007–2011

A researcher in the Science corpus: 3 papers; trusts 11 researchers and is trusted by 2 researchers here, as inferred from the citation graph.

Subfields

Whom I. Berg trusts overall

Their strongest outbound trust, strongest first, inferred from their citations.

  1. Michael Hügler
  2. S. Ragsdale
  3. William F. Martin
  4. Jörg Overmann
  5. J. E. Keeley
  6. M. Badger
  7. C. Schleper
  8. G. Price
  9. G. Farquhar
  10. R. Thauer

Who trusts I. Berg overall

  1. J. Raven
  2. G. Fuchs
  3. Li‐Mei Zhang
  4. Michael Hügler
  5. M. Tourna
  6. Hangwei Hu
  7. William F. Martin

Papers from I. Berg's perspective

Ordered by how strongly the researchers I. Berg trusts endorse each paper. Same corpus, a different order for every researcher.

  1. Genomic studies of uncultivated archaea (Nature Reviews Microbiology)
  2. Methanogenic archaea: ecologically relevant differences in energy conservation (Nature Reviews Microbiology)
  3. Pathways of Carbon Assimilation and Ammonia Oxidation Suggested by Environmental Genomic Analyses of Marine Crenarchaeota (PLoS Biology)
  4. A 3-Hydroxypropionate/4-Hydroxybutyrate Autotrophic Carbon Dioxide Assimilation Pathway in Archaea (Science)
  5. Reverse Methanogenesis: Testing the Hypothesis with Environmental Genomics (Science)
  6. Autotrophic carbon fixation in archaea (Nature Reviews Microbiology)
  7. Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea (Proceedings of the National Academy of Sciences of the United States of America)
  8. Acetogenesis and the Wood-Ljungdahl Pathway of CO2 Fixation (Biochimica et Biophysica Acta)
  9. A Nitrospira metagenome illuminates the physiology and evolution of globally important nitrite-oxidizing bacteria (Proceedings of the National Academy of Sciences of the United States of America)
  10. Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized. (Proceedings of the National Academy of Sciences of the United States of America)

Their papers