Pierre Goloubinoff
#61,387
Most Influential Person Now
Swiss Israeli Biochemist
Pierre Goloubinoff's AcademicInfluence.com Rankings
Pierre Goloubinoffbiology Degrees
Biology
#12665
World Rank
#16156
Historical Rank
Biochemistry
#2177
World Rank
#2322
Historical Rank
Download Badge
Biology
Pierre Goloubinoff's Degrees
- PhD Biochemistry University of Geneva
- Masters Biochemistry University of Geneva
- Bachelors Biochemistry University of Geneva
Why Is Pierre Goloubinoff Influential?
(Suggest an Edit or Addition)According to Wikipedia, Pierre A. Goloubinoff is a Swiss-Israeli biochemist, author and activist for Yemeni immigration and the preservation of Yemeni heritage. He is also known by the pen names David Hamami or Daoud Hamami.
Pierre Goloubinoff's Published Works
Number of citations in a given year to any of this author's works
Total number of citations to an author for the works they published in a given year. This highlights publication of the most important work(s) by the author
Published Works
- How do plants feel the heat? (2012) (731)
- GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli (1989) (641)
- Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP (1989) (640)
- Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB (1999) (590)
- Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. (1999) (580)
- Chemical Chaperones Regulate Molecular Chaperones in Vitro and in Cells under Combined Salt and Heat Stresses* (2001) (403)
- The Small Heat-shock Protein IbpB from Escherichia coli Stabilizes Stress-denatured Proteins for Subsequent Refolding by a Multichaperone Network* (1998) (349)
- Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol (2001) (329)
- Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent. (1990) (325)
- Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding (2001) (268)
- Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones. (2001) (243)
- Plasma Membrane Cyclic Nucleotide Gated Calcium Channels Control Land Plant Thermal Sensing and Acquired Thermotolerance[C][W] (2012) (238)
- Size-dependent Disaggregation of Stable Protein Aggregates by the DnaK Chaperone Machinery* (2000) (230)
- Evidence for a lipochaperonin: association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions. (1997) (221)
- Heat perception and signalling in plants: a tortuous path to thermotolerance. (2011) (220)
- Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling. (2006) (219)
- The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase. (2010) (211)
- The Heat Shock Response in Moss Plants Is Regulated by Specific Calcium-Permeable Channels in the Plasma Membrane[C][W] (2009) (205)
- Molecular and biochemical mechanisms associated with dormancy and drought tolerance in the desert legume Retama raetam. (2002) (204)
- Heavy metal ions are potent inhibitors of protein folding. (2008) (185)
- Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis (2013) (173)
- The mechanism of Hsp70 chaperones: (entropic) pulling the models together. (2007) (163)
- Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol–overexpressed molecular chaperones (2005) (150)
- Molecular architecture of the rapidly metabolized 32-kilodalton protein of photosystem II. Indications for COOH-terminal processing of a chloroplast membrane polypeptide. (1984) (147)
- Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer. (1994) (146)
- Evolution of maize inferred from sequence diversity of an Adh2 gene segment from archaeological specimens. (1993) (142)
- Hsp110 Is a Bona Fide Chaperone Using ATP to Unfold Stable Misfolded Polypeptides and Reciprocally Collaborate with Hsp70 to Solubilize Protein Aggregates* (2013) (141)
- Heat shock response in photosynthetic organisms: membrane and lipid connections. (2012) (138)
- Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast (2012) (132)
- The growing world of small heat shock proteins: from structure to functions (2017) (129)
- Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells (2010) (128)
- Disaggregating chaperones: an unfolding story. (2009) (107)
- Chloroplast-coded atrazine resistance in Solanum nigrum: psbA loci from susceptible and resistant biotypes are isogenic except for a single codon change. (1984) (106)
- Enhanced heat shock protein 70 expression alters proteasomal degradation of I&kgr;B kinase in experimental acute respiratory distress syndrome* (2007) (104)
- Controlled Expression of Recombinant Proteins in Physcomitrella patens by a Conditional Heat-shock Promoter: a Tool for Plant Research and Biotechnology (2005) (100)
- Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins (2014) (100)
- Active Solubilization and Refolding of Stable Protein Aggregates By Cooperative Unfolding Action of Individual Hsp70 Chaperones* (2004) (100)
- Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes. (2016) (95)
- Chaperones and proteases (2007) (92)
- Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides (2013) (90)
- Membrane lipid composition affects plant heat sensing and modulates Ca2+-dependent heat shock response (2010) (87)
- The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer. (1995) (85)
- Membrane fluidization triggers membrane remodeling which affects the thermotolerance in Escherichia coli. (2005) (84)
- Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones (2015) (82)
- Stable α-Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-domain Co-chaperones* (2010) (79)
- Dicarboxylic amino acids and glycine‐betaine regulate chaperone‐mediated protein‐disaggregation under stress (2003) (77)
- GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP (2013) (74)
- Function, evolution, and structure of J-domain proteins (2018) (74)
- Editorial: The HSP70 Molecular Chaperone Machines (2017) (68)
- Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration. (1998) (68)
- Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins (2018) (65)
- Physical Interaction between Bacterial Heat Shock Protein (Hsp) 90 and Hsp70 Chaperones Mediates Their Cooperative Action to Refold Denatured Proteins* (2014) (64)
- Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs (2015) (62)
- Activation of the heat shock response in plants by chlorophenols: transgenic Physcomitrella patens as a sensitive biosensor for organic pollutants. (2007) (55)
- The enigma of the gene coding for ribosomal protein S12 in the chloroplasts of Nicotiana. (1986) (53)
- The Membrane-Associated Transient Receptor Potential Vanilloid Channel Is the Central Heat Shock Receptor Controlling the Cellular Heat Shock Response in Epithelial Cells (2013) (47)
- Cadmium Causes Misfolding and Aggregation of Cytosolic Proteins in Yeast (2017) (47)
- Purification of mammalian mitochondrial chaperonin 60 through in vitro reconstitution of active oligomers. (1998) (46)
- On the evolution of chaperones and cochaperones and the expansion of proteomes across the Tree of Life (2020) (46)
- Proteinaceous Infectious Behavior in Non-pathogenic Proteins Is Controlled by Molecular Chaperones* (2002) (45)
- Effect of divalent cations on the molecular structure of the GroEL oligomer. (1994) (42)
- Reactivation of protein aggregates by mortalin and Tid1—the human mitochondrial Hsp70 chaperone system (2011) (42)
- Minimal and optimal mechanisms for GroE-mediated protein folding. (1998) (41)
- Misfolding and aggregation of nascent proteins: a novel mode of toxic cadmium action in vivo (2017) (39)
- Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine (2019) (39)
- GroES binding regulates GroEL chaperonin activity under heat shock (1997) (39)
- Increased Efficiency of GroE-assisted Protein Folding by Manganese Ions (*) (1995) (38)
- The CNGCb and CNGCd genes from Physcomitrella patens moss encode for thermosensory calcium channels responding to fluidity changes in the plasma membrane (2013) (37)
- From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL. (2000) (36)
- The knock-out of ARP3a gene affects F-actin cytoskeleton organization altering cellular tip growth, morphology and development in moss Physcomitrella patens. (2008) (36)
- Recent and future grand challenges in protein folding, misfolding, and degradation (2014) (35)
- Probing the different chaperone activities of the bacterial HSP70‐HSP40 system using a thermolabile luciferase substrate (2011) (34)
- In vivo visualization of F-actin structures during the development of the moss Physcomitrella patens. (2007) (34)
- Enhanced expression of 70-kilodalton heat shock protein limits cell division in a sepsis-induced model of acute respiratory distress syndrome* (2008) (32)
- The Novel Hydroxylamine Derivative NG-094 Suppresses Polyglutamine Protein Toxicity in Caenorhabditis elegans* (2011) (32)
- Biophysical characterization of two different stable misfolded monomeric polypeptides that are chaperone-amenable substrates. (2013) (32)
- Seasonal and diurnal variations in gene expression in the desert legume Retama raetam (2002) (28)
- Fluorescence Detection of Symmetric GroEL14(GroES7)2 Heterooligomers Involved in Protein Release during the Chaperonin Cycle* (1996) (27)
- Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling (2016) (25)
- A Mutant at Position 87 of the GroEL Chaperonin Is Affected in Protein Binding and ATP Hydrolysis (*) (1995) (25)
- Molecular Chaperones and Associated Cellular Clearance Mechanisms against Toxic Protein Conformers in Parkinson’s Disease (2011) (24)
- Characterization of the photosystem II 32 kDa protein in Synechococcus PCC7942 (1988) (23)
- Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of chaperonin GroEL14. (1995) (23)
- Mechanisms of protein homeostasis in health, aging and disease. (2016) (22)
- Moderate Fever Cycles as a Potential Mechanism to Protect the Respiratory System in COVID-19 Patients (2020) (21)
- Protein folding: Chaperoning protein evolution. (2012) (21)
- Structural analysis of GroE chaperonin complexes using chemical cross-linking. (1998) (19)
- Quantitative proteomics of rat livers shows that unrestricted feeding is stressful for proteostasis with implications on life span (2016) (19)
- How do plants feel the heat and survive? (2022) (18)
- Molecular characterization of ancient maize: Potentials and pitfalls (1991) (17)
- THE RESPONSE OF PLANTS TO SALINITY: FROM TURGOR ADJUSTMENTS TO GENOME MODIFICATION (1994) (17)
- A gene trap Dissociation insertion line, associated with a RING-H2 finger gene, shows tissue specific and developmental regulated expression of the gene in Arabidopsis. (2002) (16)
- The CaMV 35S promoter has a weak expression activity in dark grown tissues of moss Physcomitrella patens (2009) (15)
- Non-native Proteins as Newly-Identified Targets of Heavy Metals and Metalloids (2011) (15)
- An Hsp90 Inhibitor, Geldanamycin, as a Brassinosteroid Antagonist: Evidence from Salt-Exposed Roots of Vigna radiata (2003) (13)
- Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70–Hsp40 Substrates (2021) (13)
- Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance (2020) (11)
- Synergism between a foldase and an unfoldase: reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaK (2014) (11)
- Molecular Crime and Cellular Punishment (2007) (11)
- The Hsp70 chaperone system: distinct roles in erythrocyte formation and maintenance (2021) (10)
- ZnJ2 Is a Member of a Large Chaperone Family in the Chloroplast of Photosynthetic Organisms that Features a DnaJ-Like Zn-Finger Domain (2018) (9)
- Repair or Degrade: the Thermodynamic Dilemma of Cellular Protein Quality-Control (2021) (8)
- Molecular crime and cellular punishment: active detoxification of misfolded and aggregated proteins in the cell by the chaperone and protease networks. (2007) (8)
- Interdomain communication suppressing high intrinsic ATPase activity of Sse1 is essential for its co‐disaggregase activity with Ssa1 (2020) (7)
- The amino terminal region delimited by Met1 and Met37 is an integral part of the 32 kDa herbicide binding protein (1987) (7)
- How do humans and plants feel the heat? (2022) (6)
- On the evolution of chaperones and co-chaperones and the exponential expansion of proteome complexity (2020) (6)
- Molecular chaperones inject energy from ATP hydrolysis into the non-equilibrium stabilisation of native proteins (2017) (5)
- Entropic Inhibition: How the Activity of a AAA+ Machine Is Modulated by Its Substrate-Binding Domain (2021) (4)
- The HSP70 Molecular Chaperone Machines (2017) (4)
- Farming Amphetamines: Khat (Catha edulis Forsk.) a Traditional Plant with Mild Stimulating Psychoactive and Medicinal Properties (2014) (4)
- The Cellular Functions of Chaperonins (1990) (4)
- Mechanisms of Active Solubilization of Stable Protein Aggregates by Molecular Chaperones (2006) (4)
- A fluorescent multi-domain protein reveals the unfolding mechanism of Hsp70 (2022) (3)
- Role of Chaperonins in Protein Folding (1991) (2)
- A novel fluorescent multi-domain protein construct reveals the individual steps of the unfoldase action of Hsp70 (2022) (2)
- High frequency electromagnetic radiations induce a heat shock-like response in Physcomitrella Patens (2003) (2)
- Bacterial Hsp90 mediates the degradation of aggregation-prone Hsp70-Hsp40 substrates preferentially by HslUV proteolysis (2018) (2)
- Reactivation of protein aggregates by mortalin and Tid1—the human mitochondrial Hsp70 chaperone system (2011) (1)
- Single-molecule spectroscopy reveals dynamic allostery mediated by the substrate-binding domain of a AAA+ machine (2020) (1)
- Molecular dynamics of the 32,000-Dalton photosystem II herbicide-binding protein (1988) (1)
- Recruiting Unfolding Chaperones to Solubilize Misfolded Recombinant Proteins (2014) (1)
- The growing world of small heat shock proteins: from structure to functions (2017) (1)
- Entropic pulling: how Hsp70 chaperones translocate proteins through membrane pores (2006) (0)
- Corrigendum to A gene trap dissociation insertion line, associated with a RING-H2 finger gene, shows tissue specific and developmental regulated expression of the gene in Arabidopsis [Gene 290 (2002): 63-71]. (2017) (0)
- Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs (2015) (0)
- Function, evolution, and structure of J-domain proteins (2018) (0)
- Effect of divalent cations on the molecular structure of the GroEL oligomer. [Erratum to document cited in CA120:317960] (1994) (0)
- Chaperones drive in vitro evolution of uracil glycosylase towards misfolded states (2021) (0)
- The CNGCb and CNGCd genes from Physcomitrella patens moss encode for thermosensory calcium channels responding to fluidity changes in the plasma membrane (2013) (0)
- Author Correction: A fluorescent multi-domain protein reveals the unfolding mechanism of Hsp70 (2023) (0)
- Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins (2014) (0)
- In vitro evolution of uracil glycosylase towards DnaKJ and GroEL binding evolves different misfolded states (2022) (0)
- Capsaicin and capsazepine effects on heat shock protein expression in HEK293e, MLE-12, MCF-7 and HT-29 cells. (2013) (0)
- Towards a unifying mechanism for the Hsp70 chaperones (2007) (0)
- 12. Seed mitochondria harbour stress proteins and display a remarkable cold tolerance allowing energy transduction at negative temperature (2006) (0)
- Quantitative Proteomic of Rat Livers Shows a Major Reprogramming of Mitochondrial Enzymes in Food-Restriction and Increased Stress Hallmarks in Ad Libitum Feeding (2016) (0)
- Important questions and future directions in plant biochemistry. (2022) (0)
- Emerging fields in chaperone proteins: A French workshop. (2018) (0)
- Design of an Arabidopsis thaliana reporter line to detect heat-sensing and signaling mutants (2023) (0)
- Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis (2013) (0)
- Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine (2019) (0)
- Plant Response to Stress: Role of Molecular Chaperones (2004) (0)
- Second Virtual International Symposium on Cellular and Organismal Stress Responses, September 8–9, 2022 (2023) (0)
- The effect of spin exchange interaction on protein structural stability. (2022) (0)
- Tackling the Problem of Thermal versus non Thermal Biological Effects of High Frequency Electromagnetic Radiations (2004) (0)
- Contents Vol. 8, 2011 (2011) (0)
- [The toxic aggregation of proteins: a kind of "molecular delinquency" actively fought in the cell by molecular chaperones and proteases]. (2006) (0)
- Misfolding and aggregation of nascent proteins: a novel mode of toxic cadmium action in vivo (2017) (0)
This paper list is powered by the following services:
Other Resources About Pierre Goloubinoff
What Schools Are Affiliated With Pierre Goloubinoff?
Pierre Goloubinoff is affiliated with the following schools:
