World's Best Scientists 2026 revealed!
Gregers R. Andersen

Gregers R. Andersen

D-Index & Metrics

Biology and Biochemistry

D-Index
53
Citations
9047
World Ranking
16273
National Ranking
177

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Gene
  • DNA

Gregers R. Andersen mainly focuses on Biochemistry, Elongation factor, Ribosome, Binding site and Protein biosynthesis. His research brings together the fields of Biophysics and Biochemistry. The study incorporates disciplines such as Prokaryotic translation, Transfer RNA, EF-Tu, Antifungal drug and Cell biology in addition to Elongation factor.

His Ribosome research is multidisciplinary, relying on both Protein structure, EEF2 and Diphthamide. As a part of the same scientific study, he usually deals with the Binding site, concentrating on Stereochemistry and frequently concerns with Crystallography, Crystal structure and Complement inhibitor. Gregers R. Andersen usually deals with Protein biosynthesis and limits it to topics linked to Translation and Function, Cytoplasm, Nuclear export signal and Molecular biology.

His most cited work include:

  • Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation (332 citations)
  • Structure of the Exon Junction Core Complex with a Trapped DEAD-Box ATPase Bound to RNA (317 citations)
  • Bacterial Polypeptide Release Factor Rf2 is Structurally Distinct from Eukaryotic Erf1. (177 citations)

What are the main themes of his work throughout his whole career to date?

Gregers R. Andersen mostly deals with Biochemistry, Cell biology, Complement system, Biophysics and Crystallography. His is doing research in Elongation factor, Protein structure, RNA, Receptor and Binding site, both of which are found in Biochemistry. Within one scientific family, Gregers R. Andersen focuses on topics pertaining to Translation under Elongation factor, and may sometimes address concerns connected to Protein biosynthesis and Nucleotide.

In Cell biology, Gregers R. Andersen works on issues like Innate immune system, which are connected to C5-convertase. His work deals with themes such as Structural biology and Complement, which intersect with Complement system. His study in Ribosome is interdisciplinary in nature, drawing from both Transfer RNA and Diphthamide.

He most often published in these fields:

  • Biochemistry (31.52%)
  • Cell biology (26.06%)
  • Complement system (22.42%)

What were the highlights of his more recent work (between 2017-2021)?

  • Complement system (22.42%)
  • Cell biology (26.06%)
  • Alternative complement pathway (10.91%)

In recent papers he was focusing on the following fields of study:

His primary areas of investigation include Complement system, Cell biology, Alternative complement pathway, Properdin and Classical complement pathway. He has researched Complement system in several fields, including Paroxysmal nocturnal hemoglobinuria, Innate immune system, Binding site and Complement. His Cell biology research integrates issues from Receptor, Antibody and Complement receptor.

His Alternative complement pathway research is multidisciplinary, relying on both Inflammation, Cleavage and Flow cytometry. His Properdin research incorporates elements of Biophysics, Docking and Collectin. His study on Protease is covered under Biochemistry.

Between 2017 and 2021, his most popular works were:

  • Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts Fc epsilon RI interaction. (45 citations)
  • Structural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System. (22 citations)
  • A potent complement factor C3-specific nanobody inhibiting multiple functions in the alternative pathway of human and murine complement. (19 citations)

Best Publications

  • Structure of the Exon Junction Core Complex with a Trapped DEAD-Box ATPase Bound to RNA

    Christian B. F. Andersen;Lionel Ballut;Lionel Ballut;Jesper S. Johansen;Hala Chamieh

  • Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation

    Christian M T Spahn;Christian M T Spahn;Christian M T Spahn;Maria G Gomez-Lorenzo;Maria G Gomez-Lorenzo;Robert A Grassucci;Robert A Grassucci;Rene Jørgensen

  • Complement activation, regulation, and molecular basis for complement‐related diseases

    Goran Bajic;Søren E Degn;Steffen Thiel;Gregers R Andersen

  • Elongation factors in protein biosynthesis

    Gregers R Andersen;Poul Nissen;Jens Nyborg

  • Structure of the haptoglobin–haemoglobin complex

    Christian Brix Folsted Andersen;Morten Torvund-Jensen;Marianne Jensby Nielsen;Cristiano Luis Pinto de Oliveira;Cristiano Luis Pinto de Oliveira

  • Structures of modified eEF2.80S ribosome complexes reveal the role of GTP hydrolysis in translocation

    Derek J Taylor;Jakob Nilsson;A Rod Merrill;Gregers Rom Andersen

  • Bacterial Polypeptide Release Factor Rf2 is Structurally Distinct from Eukaryotic Erf1.

    Bente Vestergaard;Lan Bich Van;Gregers R Andersen;Jens Nyborg

  • Structural Basis for Nucleotide Exchange and Competition with tRNA in the Yeast Elongation Factor Complex eEF1A:eEF1Bα

    Gregers Rom Andersen;Lise Pedersen;Louis Valente;Ishita Chatterjee

  • Structure of eEF3 and the Mechanism of Transfer RNA Release From the E-Site

    Christian B. F. Andersen;Thomas Becker;Thomas Becker;Michael Blau;Monika Anand

  • Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase.

    Rene Jørgensen;Pedro A. Ortiz;Anne Carr-Schmid;Poul Nissen

  • Structure of and influence of a tick complement inhibitor on human complement component 5

    Folmer Fredslund;Nick S Laursen;Pietro Roversi;Lasse Jenner

  • Exotoxin A-eEF2 complex structure indicates ADP ribosylation by ribosome mimicry.

    René Jørgensen;A. Rod Merrill;Susan P. Yates;Victor E. Marquez

  • The life and death of translation elongation factor 2

    R. Jørgensen;A.R. Merrill;G.R. Andersen

  • Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex.

    Gregers Rom Andersen;Louis Valente;Lise Pedersen;Terri Goss Kinzy

  • Stealth and mimicry by deadly bacterial toxins.

    Susan P. Yates;René Jørgensen;Gregers R. Andersen;A. Rod Merrill

  • Structural insight on the recognition of surface-bound opsonins by the integrin I domain of complement receptor 3.

    Goran Bajic;Laure Yatime;Robert B. Sim;Thomas Vorup-Jensen

  • Toward a structure-based comprehension of the lectin pathway of complement.

    Troels R. Kjaer;Steffen Thiel;Gregers R. Andersen

  • Structural basis for the function of DEAH helicases.

    Yangzi He;Gregers R Andersen;Klaus H Nielsen

  • Structural insights into the exon junction complex.

    Hervé Le Hir;Gregers Rom Andersen

  • Structural basis for receptor recognition of vitamin-B(12)-intrinsic factor complexes.

    Christian Brix Folsted Andersen;Mette Madsen;Tina Storm;Søren K. Moestrup

Frequent Co-Authors

Steffen Thiel
Steffen Thiel Aarhus University
Lars Sottrup-Jensen
Lars Sottrup-Jensen Aarhus University
Jan Skov Pedersen
Jan Skov Pedersen Aarhus University
Tom Eirik Mollnes
Tom Eirik Mollnes Oslo University Hospital
Roland Beckmann
Roland Beckmann Ludwig-Maximilians-Universität München
Jens C. Jensenius
Jens C. Jensenius Aarhus University
Joachim Frank
Joachim Frank Columbia University
Thorsten Mielke
Thorsten Mielke Max Planck Society
Thomas S. Becker
Thomas S. Becker University of Sydney
Christian M. T. Spahn
Christian M. T. Spahn Charité - University Medicine Berlin

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