Pierre Goloubinoff - Concepedia

Author

Pierre Goloubinoff

Also Known As

Goloubinoff, Pierre, P Goloubinoff, P. GOLOUBINOFF, P. Goloubinoff, PIERRE GOLOUBINOFF, Pierre Goloubinoff, Pierre Goloubinoff (382998), Wickramaratne, Anushka

151

Publications

13.9K

Citations

H-Index

Concepts

All Affiliations

University of Lausanne Hebrew University of Jerusalem École Polytechnique Fédérale de Lausanne Weizmann Institute of Science Tel Aviv University

About

Pierre Goloubinoff is an author at University of Lausanne specializing in natural sciences, molecular biology, and biochemistry.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Natural Sciences	28	35	3.8K
2	Biochemistry	24	30	3.2K
3	Medicine	23	30	3.5K
4	Engineering	3	3	192
5	Health Sciences	1	1	23

Pierre Goloubinoff

Publications

10.4K

Citations

H-Index

Page 1

	Year	Citations
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP Pierre Goloubinoff, John T. Christeller, Anthony A. Gatenby, Nature Protein ChemistryUnfolded State DependsCellular EnzymologyBiochemistryProtein Assembly	1989	744
GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli Pierre Goloubinoff, Anthony A. Gatenby, George H. Lorimer Nature Protein FoldingVirulence FactorProtein BiosynthesisMolecular BiologyEscherichia Coli	1989	703
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network Pierre Goloubinoff, Axel Mogk, Anat Ben‐Zvi, Proceedings of the National Academy of Sciences	1999	588
Chemical Chaperones Regulate Molecular Chaperones in Vitro and in Cells under Combined Salt and Heat Stresses Sophia Diamant, Noa Eliahu, David Rosenthal, Journal of Biological Chemistry	2001	467
Chaperonin-facilitated refolding of ribulose bisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are potassium dependent Paul V. Viitanen, Thomas Lübben, J. N. Reed, Biochemistry	1990	382
The Small Heat-shock Protein IbpB from Escherichia coli Stabilizes Stress-denatured Proteins for Subsequent Refolding by a Multichaperone Network Lea Veinger, Sophia Diamant, Johannes Büchner, Journal of Biological Chemistry	1998	368
Plasma Membrane Cyclic Nucleotide Gated Calcium Channels Control Land Plant Thermal Sensing and Acquired Thermotolerance Andrija Finka, America Farinia Henriquez Cuendet, Frans J. M. Maathuis, The Plant Cell	2012	365
The Heat Shock Response in Moss Plants Is Regulated by Specific Calcium-Permeable Channels in the Plasma Membrane Younousse Saidi, Andrija Finka, Maude Muriset, The Plant Cell	2009	356
Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the <i>Escherichia coli</i> cytosol Toshifumi Tomoyasu, Axel Mogk, Hanno Langen, Molecular Microbiology	2001	338
<i>Synechocystis</i> HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding Zsolt Török, Pierre Goloubinoff, Ibolya Horváth, Proceedings of the National Academy of Sciences	2001	282

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