Franz-Ulrich Hartl

Franz-Ulrich Hartl's AcademicInfluence.com Rankings

Franz-Ulrich Hartl

Chemistry

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#640

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Chemistry

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According to Wikipedia, Franz-Ulrich Hartl is a German biochemist and the current Executive Director of the Max Planck Institute of Biochemistry. He is known for his pioneering work in chaperone-mediated protein folding. Early life and education Hartl was born in Essen, West Germany in 1957 to an electrical engineer father and a home economics teacher mother. His family moved to a village in northern part of the Black Forest when he was four. He was intrigued with biology since a young age, thanks to his hobby microscopist grandfather and a family friend who was a biology teacher. Hartl specifically became interested in biochemistry in high school after reading James Watson's account of the discovery of the helical structure of DNA, prompting him to study medicine and specialise in biochemistry at Heidelberg University. It was during this period when he had his first research experience, studying peroxisomes in rat liver. Hartl completed his MD degree in 1985.

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Franz-Ulrich Hartl's Published Works

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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

Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein (2002) (3341)
Molecular chaperones in cellular protein folding (1996) (3174)
Molecular chaperones in protein folding and proteostasis (2011) (2722)
Molecular chaperone functions of heat-shock proteins. (1993) (1581)
Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent (1997) (1305)
Molecular chaperone functions in protein folding and proteostasis. (2013) (1221)
Structure of TPR Domain–Peptide Complexes Critical Elements in the Assembly of the Hsp70–Hsp90 Multichaperone Machine (2000) (1158)
Pathways of chaperone-mediated protein folding in the cytosol (2004) (1142)
Converging concepts of protein folding in vitro and in vivo (2009) (1100)
In vivo aspects of protein folding and quality control (2016) (931)
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding (1992) (921)
Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria (1989) (853)
Molecular chaperones in cellular protein folding. (1995) (827)
Hsp90: a specialized but essential protein-folding tool. (2001) (817)
Molecular Chaperones Hsp90 and Hsp70 Deliver Preproteins to the Mitochondrial Import Receptor Tom70 (2003) (795)
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate (1991) (757)
Mitochondrial protein import. (1987) (757)
Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils. (2000) (679)
Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones (1994) (647)
Amyloid-like Aggregates Sequester Numerous Metastable Proteins with Essential Cellular Functions (2011) (645)
Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli (2005) (630)
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis (1989) (607)
In Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP Hydrolysis (1998) (594)
The proteostasis network and its decline in ageing (2019) (586)
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat‐induced protein damage. (1993) (578)
The binding cascade of SecB to SecA to SecY E mediates preprotein targeting to the E. coli plasma membrane (1990) (547)
Identification of in vivo substrates of the chaperonin GroEL (1999) (525)
Proteostasis impairment in protein-misfolding and -aggregation diseases. (2014) (513)
The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. (1994) (505)
Pathways of cellular proteostasis in aging and disease (2018) (485)
Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. (1997) (483)
Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3 (2009) (474)
Protein abundance profiling of the Escherichia coli cytosol (2008) (470)
Δμ H+ and ATP function at different steps of the catalytic cycle of preprotein translocase (1991) (453)
Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation. (2004) (448)
Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle (1995) (446)
Structure of a Bag/Hsc70 Complex: Convergent Functional Evolution of Hsp70 Nucleotide Exchange Factors (2001) (444)
Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. (2001) (440)
Chaperones increase association of tau protein with microtubules (2003) (440)
Protein sorting to mitochondria: evolutionary conservations of folding and assembly. (1990) (430)
Polypeptide Flux through Bacterial Hsp70 DnaK Cooperates with Trigger Factor in Chaperoning Nascent Chains (1999) (421)
The enzymology of protein translocation across the Escherichia coli plasma membrane. (1991) (410)
Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90. (1996) (409)
Function in protein folding of TRiC, a cytosolic ring complex containing TCP‐1 and structurally related subunits. (1992) (400)
Chaperonin‐mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. (1992) (391)
Recombination of protein domains facilitated by co-translational folding in eukaryotes (1997) (387)
Molecular chaperones in protein folding: the art of avoiding sticky situations. (1994) (385)
Structural Probing of a Protein Phosphatase 2A Network by Chemical Cross-Linking and Mass Spectrometry (2012) (381)
Protein folding in the cytoplasm and the heat shock response. (2010) (375)
CD40, an extracellular receptor for binding and uptake of Hsp70–peptide complexes (2002) (374)
More than folding: localized functions of cytosolic chaperones. (2003) (372)
Protein folding in the central cavity of the GroEL–GroES chaperonin complex (1996) (364)
In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System (1997) (349)
Regulation of the Heat-shock Protein 70 Reaction Cycle by the Mammalian DnaJ Homolog, Hsp40* (1996) (346)
Principles of protein folding in the cellular environment. (1999) (346)
Mitochondrial protein import: Identification of processing peptidase and of PEP, a processing enhancing protein (1988) (334)
PolyQ Proteins Interfere with Nuclear Degradation of Cytosolic Proteins by Sequestering the Sis1p Chaperone (2013) (330)
Widespread Proteome Remodeling and Aggregation in Aging C. elegans (2015) (328)
Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s (2006) (327)
DnaK functions as a central hub in the E. coli chaperone network. (2012) (323)
Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA (2016) (321)
A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1 (1991) (319)
Roles of molecular chaperones in protein misfolding diseases. (2004) (316)
Protein Synthesis upon Acute Nutrient Restriction Relies on Proteasome Function (2005) (312)
Structure of the Molecular Chaperone Prefoldin Unique Interaction of Multiple Coiled Coil Tentacles with Unfolded Proteins (2000) (309)
A zinc finger‐like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. (1996) (307)
Widespread Proteome Remodeling and Aggregation in Aging C. elegans (2017) (304)
A Balance of Protein Synthesis and Proteasome-Dependent Degradation Determines the Maintenance of LTP (2006) (297)
Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase (1986) (296)
Structural Features of the GroEL-GroES Nano-Cage Required for Rapid Folding of Encapsulated Protein (2006) (292)
Prevention of protein denaturation under heat stress by the chaperonin Hsp60. (1992) (290)
Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding (2001) (281)
Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers. (2006) (280)
Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60. (1992) (270)
In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment (2018) (267)
The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding. (2016) (266)
Principles of Chaperone-Assisted Protein Folding: Differences Between in Vitro and in Vivo Mechanisms (1996) (260)
Successive translocation into and out of the mitochondrial matrix: Targeting of proteins to the intermembrane space by a bipartite signal peptide (1987) (258)
The molecular architecture of the eukaryotic chaperonin TRiC/CCT. (2012) (256)
Protein Misfolding Diseases. (2017) (251)
The nucleolus functions as a phase-separated protein quality control compartment (2019) (250)
Role of the Myosin Assembly Protein UNC-45 as a Molecular Chaperone for Myosin (2002) (250)
Structural Basis for the Cooperation of Hsp70 and Hsp110 Chaperones in Protein Folding (2008) (249)
The role of molecular chaperones in protein folding (1995) (249)
Specific Binding of Tetratricopeptide Repeat Proteins to the C-terminal 12-kDa Domain of hsp90* (1998) (248)
The Native 3D Organization of Bacterial Polysomes (2009) (246)
Protein folding in the cell: competing models of chaperonin function (1996) (235)
How do polypeptides cross the mitochondrial membranes? (1990) (233)
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co‐chaperone p23 (2000) (233)
Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms. (1998) (232)
The cellular prion protein mediates neurotoxic signalling of β‐sheet‐rich conformers independent of prion replication (2011) (229)
Function of Trigger Factor and DnaK in Multidomain Protein Folding Increase in Yield at the Expense of Folding Speed (2004) (229)
Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space (1992) (227)
Real-time observation of trigger factor function on translating ribosomes (2006) (221)
In Situ Architecture and Cellular Interactions of PolyQ Inclusions (2017) (221)
Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. (2005) (221)
Roles of molecular chaperones in cytoplasmic protein folding. (2000) (212)
Compartmentation of protein folding in vivo: sequestration of non‐native polypeptide by the chaperonin–GimC system (1999) (208)
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity (2002) (193)
Ligand Discrimination by TPR Domains (2002) (191)
In vivo analysis of the overlapping functions of DnaK and trigger factor (2004) (189)
Molecular chaperones in cellular protein folding. (1994) (186)
Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase (1999) (186)
Detection and selective dissociation of intact ribosomes in a mass spectrometer. (2000) (185)
Induction of cellular immunity by immunization with novel hybrid peptides complexed to heat shock protein 70. (2000) (183)
Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sites (1989) (181)
Chaperone-assisted protein folding. (1997) (177)
Coupled chaperone action in folding and assembly of hexadecameric Rubisco (2010) (175)
Monitoring Protein Conformation along the Pathway of Chaperonin-Assisted Folding (2008) (173)
Firefly luciferase mutants as sensors of proteome stress (2011) (168)
Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress (2013) (164)
Failure of RQC machinery causes protein aggregation and proteotoxic stress (2016) (164)
Soluble Oligomers of PolyQ-Expanded Huntingtin Target a Multiplicity of Key Cellular Factors. (2016) (164)
Polypeptides traverse the mitochondrial envelope in an extended state (1990) (162)
Biogenesis and Metabolic Maintenance of Rubisco. (2017) (159)
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase (2011) (158)
Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. (1996) (156)
The mitochondrial chaperonin hsp60 is required for its own assembly. (1990) (155)
Structure and Function of RbcX, an Assembly Chaperone for Hexadecameric Rubisco (2007) (153)
Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. (1993) (153)
Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha‐lactalbumin. (1994) (153)
Cyclosporin A-binding protein (cyclophilin) of Neurospora crassa. One gene codes for both the cytosolic and mitochondrial forms. (1988) (152)
The role of molecular chaperones in human misfolding diseases (2009) (151)
The three-dimensional organization of polyribosomes in intact human cells. (2010) (145)
Interplay of Acetyltransferase EP300 and the Proteasome System in Regulating Heat Shock Transcription Factor 1 (2014) (144)
Plant RuBisCo assembly in E. coli with five chloroplast chaperones including BSD2 (2017) (144)
Chaperonin-Catalyzed Rescue of Kinetically Trapped States in Protein Folding (2010) (140)
Mechanism of chaperonin action: GroES binding and release can drive GroEL‐mediated protein folding in the absence of ATP hydrolysis. (1996) (138)
Rubisco condensate formation by CcmM in β-carboxysome biogenesis (2019) (134)
In vitro evidence that hsp90 contains two independent chaperone sites (1997) (134)
Proteolytic cleavage of polyglutamine-expanded ataxin-3 is critical for aggregation and sequestration of non-expanded ataxin-3. (2006) (133)
MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin (1999) (132)
Protein folding: Versatility of the cytosolic chaperonin TRiC/CCT (2000) (132)
Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria (1994) (130)
Import of proteins into mitochondria: a multi-step process. (1988) (129)
Role of auxiliary proteins in Rubisco biogenesis and function (2015) (122)
Structure of green-type Rubisco activase from tobacco (2011) (118)
Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system (2003) (118)
The processing peptidase of yeast mitochondria: the two co‐operating components MPP and PEP are structurally related. (1988) (114)
The effect of macromolecular crowding on chaperonin-mediated protein folding. (1997) (114)
GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding (2014) (113)
Cytosolic Protein Vms1 Links Ribosome Quality Control to Mitochondrial and Cellular Homeostasis (2017) (110)
De novo folding of GFP fusion proteins: high efficiency in eukaryotes but not in bacteria. (2005) (109)
TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes (2003) (108)
Quantitative Proteomics Reveals That Hsp90 Inhibition Preferentially Targets Kinases and the DNA Damage Response* (2011) (103)
The mitochondrial chaperonin hsp60 is required for its own assembly (1990) (101)
Identification of Anti-prion Compounds as Efficient Inhibitors of Polyglutamine Protein Aggregation in a Zebrafish Model* (2007) (99)
Calpain Inhibition Is Sufficient to Suppress Aggregation of Polyglutamine-expanded Ataxin-3* (2007) (98)
Mass spectrometry of ribosomes and ribosomal subunits. (1998) (95)
Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES (1993) (93)
Spatiotemporal Proteomic Profiling of Huntington’s Disease Inclusions Reveals Widespread Loss of Protein Function (2017) (91)
Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry. (2000) (91)
Mitochondrial precursor proteins are imported through a hydrophilic membrane environment. (1987) (89)
Structure of human heat-shock transcription factor 1 in complex with DNA (2016) (89)
Prediction of Novel Bag-1 Homologs Based on Structure/Function Analysis Identifies Snl1p as an Hsp70 Co-chaperone in Saccharomyces cerevisiae * (2002) (88)
Identification of Nascent Chain Interaction Sites on Trigger Factor* (2007) (88)
Functional Modules of the Proteostasis Network. (2019) (86)
Cellular Homeostasis and Aging. (2016) (86)
Structure of hibernating ribosomes studied by cryoelectron tomography in vitro and in situ (2010) (85)
SnapShot: Molecular Chaperones, Part I (2007) (85)
Characterization of a Receptor for Heat Shock Protein 70 on Macrophages and Monocytes (2000) (84)
Opposing effects of folding and assembly chaperones on evolvability of Rubisco. (2015) (82)
ER Stress-Induced eIF2-alpha Phosphorylation Underlies Sensitivity of Striatal Neurons to Pathogenic Huntingtin (2014) (79)
Integral membrane polypeptides of rat liver peroxisomes: topology and response to different metabolic states. (1987) (79)
Essential role of the chaperonin folding compartment in vivo (2008) (78)
Proteome-wide observation of the phenomenon of life on the edge of solubility (2019) (73)
Sorting pathways of mitochondrial inner membrane proteins. (1990) (71)
Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco (2011) (70)
Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein. (1992) (70)
Advancing Cell Biology Through Proteomics in Space and Time (PROSPECTS)* (2012) (70)
High-resolution structure and biophysical characterization of the nucleocapsid phosphoprotein dimerization domain from the Covid-19 severe acute respiratory syndrome coronavirus 2 (2020) (68)
Proteotoxic stress and ageing triggers the loss of redox homeostasis across cellular compartments (2015) (68)
Hsp90 (2001) (66)
Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein (2020) (65)
Rubisco condensate formation by CcmM in beta-carboxysome biogenesis (2018) (64)
Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle (2013) (64)
Coexistence of Group I and Group II Chaperonins in the Archaeon Methanosarcina mazei* (2003) (63)
ATP‐dependent protein refolding activity in reticulocyte lysate (1993) (63)
Structure and mechanism of the Rubisco-assembly chaperone Raf1 (2015) (62)
Recent advances in understanding catalysis of protein folding by molecular chaperones (2020) (60)
Significant hydrogen exchange protection in GroEL‐bound DHFR is maintained during iterative rounds of substrate cycling (1996) (60)
The heat shock protein 90-targeting drug cisplatin selectively inhibits steroid receptor activation. (2003) (60)
Essential Role of the Unusual DNA-binding Motif of BAG-1 for Inhibition of the Glucocorticoid Receptor* 210 (2003) (58)
Energy requirements for unfolding and membrane translocation of precursor proteins during import into mitochondria. (1990) (57)
Folding of large multidomain proteins by partial encapsulation in the chaperonin TRiC/CCT (2012) (57)
Protein Folding In The Cell: The Role Of Molecular Chaperones (1996) (57)
Pathway of Actin Folding Directed by the Eukaryotic Chaperonin TRiC (2018) (56)
Functional interaction of heat shock protein GroEL with an RNase E-like activity in Escherichia coli. (1993) (56)
Action of the Hsp70 chaperone system observed with single proteins (2015) (54)
Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding (1995) (54)
Crystal structure of an archaeal actin homolog. (2006) (54)
The thermosome of Thermoplasma acidophilum and its relationship to the eukaryotic chaperonin TRiC (1995) (53)
Physicochemical determinants of chaperone requirements. (2010) (53)
Mitochondrial stress signaling: a pathway unfolds. (2008) (53)
Molecular and structural architecture of polyQ aggregates in yeast (2018) (53)
An unstable transmembrane segment in the cystic fibrosis transmembrane conductance regulator (1999) (52)
Chaperonin-mediated de novo generation of prion protein aggregates. (2001) (52)
Identification of GroEL as a constituent of an mRNA‐protection complex in Escherichia coli (1995) (51)
Responses to Peroxynitrite in Yeast: Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) as a Sensitive Intracellular Target for Nitration and Enhancement of Chaperone Expression and Ubiquitination (2000) (50)
Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome (2014) (50)
A protein quality control pathway regulated by linear ubiquitination (2019) (50)
The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding (1998) (50)
The formation, function and regulation of amyloids: insights from structural biology (2016) (50)
Rubisco Activases: AAA+ Chaperones Adapted to Enzyme Repair (2017) (49)
Erratum: Degradation of potent Rubisco inhibitor by selective sugar phosphatase (2015) (49)
Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei (2009) (48)
Contribution of molecular chaperones to protein folding in the cytoplasm of prokaryotic and eukaryotic cells. (2001) (47)
Structure and function of Vms1 and Arb1 in RQC and mitochondrial proteome homeostasis (2019) (47)
Mechanism of Enzyme Repair by the AAA+ Chaperone Rubisco Activase. (2017) (47)
A Stress Sensor for the Bacterial Periplasm (2003) (46)
In situ architecture of neuronal α-Synuclein inclusions (2020) (46)
10 Molecular Chaperone Functions of hsp70 and hsp60 in Protein Folding (1994) (46)
Inhibition of GR‐mediated transcription by p23 requires interaction with Hsp90 (2004) (44)
Improved isolation and purification of rat liver peroxisomes by combined rate zonal and equilibrium density centrifugation. (1985) (43)
Versatility of Trigger Factor Interactions with Ribosome-Nascent Chain Complexes (2010) (43)
Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein. (2010) (43)
Systematic Identification of Antiprion Drugs by High-Throughput Screening Based on Scanning for Intensely Fluorescent Targets (2005) (43)
Chaperonin Cofactors, Cpn10 and Cpn20, of Green Algae and Plants Function as Hetero-oligomeric Ring Complexes*♦ (2012) (42)
In Situ Structure of Neuronal C 9 orf 72 Poly-GA Aggregates Reveals Proteasome Recruitment Graphical (2018) (42)
A sensitive filter retention assay for the detection of PrPSc and the screening of anti‐prion compounds (2001) (41)
Chaperone-assisted protein folding: the path to discovery from a personal perspective (2011) (41)
What is the molten globule? (1995) (41)
Fes1p acts as a nucleotide exchange factor for the ribosome-associated molecular chaperone Ssb1p (2006) (40)
Rat liver peroxisomes. I. New peroxisome population induced by thyroid hormones in the liver of male rats. (1982) (40)
Exploring the capacity of trigger factor to function as a shield for ribosome bound polypeptide chains (2006) (40)
Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level. (2014) (39)
The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding (1999) (39)
Protein folding. Secrets of a double-doughnut. (1994) (38)
The dynamic tunnel (2004) (38)
Rat liver peroxisomes, II. Stimulation of peroxisomal fatty-acid beta-oxidation by thyroid hormones. (1983) (38)
Post-translational protein import and folding. (1994) (37)
GroEL Ring Separation and Exchange in the Chaperonin Reaction (2018) (36)
SnapShot: Molecular Chaperones, Part II (2007) (36)
Hats Off to the Tricorn Protease (1996) (35)
Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry. (1994) (35)
Chaperonin-Assisted Protein Folding: Relative Population of Asymmetric and Symmetric GroEL:GroES Complexes. (2015) (35)
Cell‐to‐cell transmission of C9orf72 poly‐(Gly‐Ala) triggers key features of ALS/FTD (2020) (35)
Amplifiers co-translationally enhance CFTR biosynthesis via PCBP1-mediated regulation of CFTR mRNA. (2020) (34)
Protein-catalysed protein folding. (1990) (33)
Active Cage Mechanism of Chaperonin-Assisted Protein Folding Demonstrated at Single-Molecule Level (2014) (33)
Role of Small Subunit in Mediating Assembly of Red-type Form I Rubisco (2014) (32)
Heat shock proteins in protein folding and membrane translocation. (1991) (32)
The thermosome of Thermoplasma acidophilum and its relationship to the eukaryotic chaperonin TRiC. (1995) (31)
Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and yeast. (1994) (31)
The Hsp70 Chaperone System Stabilizes a Thermo-sensitive Subproteome in E. coli. (2019) (30)
Functional Characterization of an Archaeal GroEL/GroES Chaperonin System (2004) (28)
Chaperone Machineries of Rubisco - The Most Abundant Enzyme. (2020) (28)
Directionality of Polypeptide Transfer in the Mitochondrial Pathway of Chaperone-Mediated Protein Folding (1998) (28)
Improved recombinant expression and purification of functional plant Rubisco (2019) (26)
Efficient production of native actin upon translation in a bacterial lysate supplemented with the eukaryotic chaperonin TRiC (2005) (25)
Sugarcoating ER Stress (2014) (24)
Molecular chaperones of the Hsp 110 family act as nucleotide exchange factors of Hsp 70 s (2013) (24)
Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi‐domain proteins in Escherichia coli (2010) (24)
Hsp90 structure: when two ends meet (2006) (22)
Heat shock proteins in protein folding and membrane translocation. (1991) (22)
The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends (2020) (22)
High capacity of the endoplasmic reticulum to prevent secretion and aggregation of amyloidogenic proteins (2018) (22)
On the Role of Symmetrical and Asymmetrical Chaperonin Complexes in Assisted Protein Folding (1999) (20)
TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes (2008) (20)
Role for ribosome-associated quality control in sampling proteins for MHC class I-mediated antigen presentation (2020) (19)
Chaperones and transcriptional regulation by nuclear receptors (2002) (19)
Protein folding in the cell: molecular chaperones pave the way. (1993) (19)
Molecular chaperones in protein folding in the cell (2000) (18)
L25 functions as a conserved ribosomal docking site shared by nascent chain‐associated complex and signal‐recognition particle (2007) (18)
Sis1 potentiates the stress response to protein aggregation and elevated temperature (2020) (18)
The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model (2021) (18)
Dual Functions of a Rubisco Activase in Metabolic Repair and Recruitment to Carboxysomes (2020) (18)
Principles of chaperone-mediated protein folding. (1995) (17)
Translocation intermediates on the import pathway of proteins into mitochondria. (1987) (16)
A comment on: ‘The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60): Evidence for the presence of a single tryptophan’, by N.C. Price, S.M. Kelly, S. Wood and A. auf der Mauer (1991) FEBS Lett. 292, 9–12 (1993) (15)
Synergistic Inhibition of the Glucocorticoid Receptor by Radicicol and Benzoquinone Ansamycins (2001) (14)
Biogenesis of Rat Liver Peroxisomal Membrane Polypeptides (1987) (14)
Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii (2015) (14)
Role of the ribosomal quality control machinery in nucleocytoplasmic translocation of polyQ-expanded huntingtin exon-1. (2017) (14)
An inventory of interactors of the human HSP60/HSP10 chaperonin in the mitochondrial matrix space (2020) (14)
Distinct binding sites for the ATPase and substrate-binding domain of human Hsp70 on the cell surface of antigen presenting cells. (2008) (14)
Affinity purification of molecular chaperones of the yeast Hansenula polymorpha using immobilized denatured alcohol oxidase (1993) (13)
Scaffolding protein CcmM directs multiprotein phase separation in β-carboxysome biogenesis (2021) (13)
L25 functions as a conserved ribosomal docking site shared by nascent chain‐associated complex and signal‐recognition particle (2006) (12)
Erratum: Widespread Proteome Remodeling and Aggregation in Aging C. elegans (Cell (2015) 161(4) (919–932) (S0092867415003207)(10.1016/j.cell.2015.03.032) (2017) (12)
A signal recognition particle in Escherichia coli? (1993) (11)
Topology of the morphological domains of the chaperonin GroEL visualized by immuno-electron microscopy. (1994) (11)
Efficient Catalysis of Protein Folding by GroEL/ES of the Obligate Chaperonin Substrate MetF. (2020) (11)
N-terminal polyglutamine-containing fragments inhibit androgen receptor transactivation function (2008) (11)
Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2. (2019) (11)
Gel‐like inclusions of C‐terminal fragments of TDP‐43 sequester stalled proteasomes in neurons (2022) (11)
The pathway of chaperone-assisted protein folding (1992) (10)
Import of proteins into the various submitochondrial compartments (1989) (10)
Multiple pathways of toxicity induced by C9orf72 dipeptide repeat aggregates and G4C2 RNA in a cellular model (2020) (10)
The chaperone Clusterin in neurodegeneration−friend or foe? (2022) (10)
Ligand discrimination by TPR domains : Relevance and selectivity of EEVD-recognition in Hsp 70-Hop-Hsp 90 complexes RUNNING TITLE : PEPTIDE RECOGNITION MOTIFS OF HOP TPR DOMAINS (2002) (9)
Structure and conformational cycle of a bacteriophage-encoded chaperonin (2020) (9)
Import of Cytochromes b2 and c1 into Mitochondria is Dependent on Both Membrane Potential and Nucleoside Triphosphates (1987) (9)
Aberrant protein interactions in amyloid disease (2011) (9)
Lord of the Rings: GroES Structure (1996) (8)
The AAA+ chaperone VCP disaggregates Tau fibrils and generates aggregate seeds in a cellular system (2022) (8)
Protein Folding In Vivo (2002) (8)
The processing peptidase of yeast mitochondria (1988) (8)
Fluc‐EGFP reporter mice reveal differential alterations of neuronal proteostasis in aging and disease (2021) (7)
Protein targeting to mitochondria (1996) (7)
Protein Folding and Chaperones (2006) (7)
Unfolding the chaperone story (2017) (6)
Secrets of a double-doughnut (1994) (5)
Hitzeschockprotein Hsp 60 als Katalysator für die Kettenfaltung mitochondrialer Proteine (1989) (5)
Dual Role of a Rubisco Activase in Metabolic Repair and Carboxysome Organization (2020) (5)
Protein folding. Secrets of a double-doughnut. (1994) (5)
Mechanisms and pathways of chaperone-mediated protein folding. (1995) (4)
Role of HSP60 in Folding/Assembly of Mitochondrial Proteins (1991) (4)
Gel-like inclusions of C-terminal fragments of TDP-43 sequester and inhibit proteasomes in neurons (2021) (4)
Stress proteins and mitochondrial protein import (1990) (4)
Bacterial RF3 senses chaperone function in co-translational folding. (2021) (3)
Formation and quantification of protein complexes between peroxisomal alcohol oxidase and GroEL (1992) (3)
The first chaperonin (2013) (3)
Quality Control: Maintaining molecular order and preventing cellular chaos. (2022) (3)
Chapter 3. Role of Molecular Chaperones in Protein Folding (2010) (3)
Single, Rapid Coastal Settlement of Asia Revealed by Analysis of Complete Mitochondrial Genomes (2005) (3)
Structure and Function of GimC/Prefoldin (2008) (3)
The Role of Molecular Chaperones Hsp70 And Hsp60 in Protein Folding (1996) (2)
Susan Lee Lindquist (1949-2016)-pioneer in the study of cellular protein folding and disease. (2016) (2)
Molekulare Mechanismen des Alterns (2007) (2)
Bacterial RF3 Senses Chaperone Function in Co-Translational Folding (2020) (2)
Chaperone-assisted protein folding in the cytosol (2005) (2)
Molecular chaperones: guardians of the proteome (2015) (2)
Towards a complete structure of Hsp90. (2005) (2)
Structural Characterization of Mutant Huntingtin Inclusion Bodies by Cryo-Electron Tomography (2016) (2)
Formation of toxic oligomers of polyQ-expanded Huntingtin by prion-mediated cross-seeding. (2022) (2)
Membrane translocation and refolding mitochondrial proteins (1990) (1)
Ueber einige neue organische Doppelsalze mit Wismutchlorid (1)
Efficient Production of Native Actin upon Translation in a Bacterial Lysate Supplemented Exclusively with the Eukaryotic Chaperonin TRiC (2005) (1)
Crystal Structure of N-acetylneuraminate lyase from Mycoplasma synoviae, crystal form II (2014) (1)
To Our Authors, Readers and Subscribers (2001) (1)
Molecular chaperone action in polyglutamine aggregation disease (2004) (1)
Ribosomes under stress: Structural variability of the 100S particles studied by cryoelectron tomography (2007) (1)
A new way of D/Ealing with protein misfolding. (2021) (1)
Resolving chaperone-assisted protein folding on the ribosome at the peptide level (2022) (1)
Degradation of potent Rubisco inhibitor by selective sugar phosphatase (2015) (1)
Crystal structure of the HspBP1 core domain complexed with the fragment of Hsp70 ATPase domain (2005) (0)
Import of Cytochrome c1 and Cytochrome b2 into Mitochondria (1987) (0)
Crystal structure of RbcX-IIa from Chlamydomonas reinhardtii (2015) (0)
Crystal structure of human Hsf1 with HSE DNA (2015) (0)
Crystal structure of CbbY (mutant D10N) from Rhodobacter sphaeroides in complex with Xylulose-(1,5)bisphosphate, crystal form II (2014) (0)
Molecular architecture of the eukaryotic chaperonin TRiC/CCT derived by a combination of chemical crosslinking and mass-spectrometry, XL-MS (2012) (0)
Crystal structure of RbcX, crystal form II (2007) (0)
Crystal structure of the BSD2 homolog of Arabidopsis thaliana (2017) (0)
The chaperonin GroEL is involved in RNA binding and stabilization (1995) (0)
Ground state 26S proteasome (GS2) (2018) (0)
Edinburgh Research Explorer Structure of hibernating ribosomes studied by cryoelectron tomography in vitro and in situ (2018) (0)
Cryo-electron Tomography of in vitro Translation Systems (2005) (0)
Crystal structure of RbcX point mutant Q29A (2007) (0)
Publisher Correction: Structure and function of Vms1 and Arb1 in RQC and mitochondrial proteome homeostasis (2019) (0)
Paper of the Year 2002: Award to Cordelia Schiene-Fischer. (2003) (0)
Session 7. Protein Transport and Assembly (2012) (0)
Crystal structure of the AAA+ protein CbbX, native structure (2011) (0)
Vms 1 antagonizes CAT tailing by Rqc 2 , thereby avoiding aggregate formation d Vms 1 is a key component of a ribosome quality-control pathway termed (2017) (0)
Crystal structure of the chaperonin gp146 from the bacteriophage EL 2 (Pseudomonas aeruginosa) in presence of ATP-BeFx, crystal form II (2020) (0)
Molecular Cell Structural Organization of Human Polyribosomes RESULTS Clusters of Ribosomes in Tomograms of Human Glia Cells (2012) (0)
Structure and function of Vms1 and Arb1 in RQC and mitochondrial proteome homeostasis (2019) (0)
Cyclosporin A-binding Protein ( Cyclophilin ) of Neurospora crassu * ONE GENE (2001) (0)
Chaperone molecules concentrate together with the ubiquitin-proteasome system inside particulate cytoplasmic structures : possible role in metabolism of misfolded proteins (2015) (0)
Single molecule analysis of protein aggregation and prions by SIFT (2005) (0)
Crystal structure of Ta0583, an archaeal actin homolog, complex with ADP (2006) (0)
Crystal structure of Chaetomium thermophilum Skn7 with SSRE DNA (2015) (0)
CryoEM structure of the interaction between Rubisco Activase small-subunit-like (SSUL) domain with Rubisco from Nostoc sp. (strain PCC7120) (2020) (0)
Negative stain EM Map of the AAA protein CbbX, a red-type Rubisco activase from R. sphaeroides (2011) (0)
Rubisco condensate formation by CcmM in β-carboxysome biogenesis (2019) (0)
Structure of the chaperonin gp146 from the bacteriophage EL (Pseudomonas aeruginosa) in complex with ADP (2020) (0)
Membrane Protein Biosynthesis and Transport. Felix Bronner (1986) (0)
Franz Herzog Cross-Linking and Mass Spectrometry Structural Probing of a Protein Phosphatase 2 A Network by Chemical (2012) (0)
Structure of Hgh1, crystal form II (2019) (0)
The interaction network of the GroEL chaperonin (2012) (0)
Crystal Structure of the small subunit-like domain 1 of CcmM from Synechococcus elongatus (strain PCC 7942), thiol-oxidized form (2018) (0)
Crystal structure of RbcX in complex with substrate (2007) (0)
Crystal structure of RbcX-IIa from Chlamydomonas reinhardtii in complex with RbcL C-terminal tail (2015) (0)
Crystal structure of redox-inhibited phosphoribulokinase from Synechococcus sp. (strain PCC 6301) (2019) (0)
Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein (2020) (0)
Crystal structure of redox-inhibited phosphoribulokinase from Synechococcus sp. (strain PCC 6301), osmate derivative (2019) (0)
25th Biennial Meeting of the International Society for Neurochemistry jointly with the 13th Meeting of the Asian-Pacific Society for Neurochemistry in conjunction with the 35th Meeting of the Australasian Neuroscience Society 23-27 August 2015, Cairns, Australia. (2015) (0)
Resolution of distinct steps in mitochondrial protein import (1988) (0)
PRESENT POSITION AND ADDRESS: Associate Professor, with Tenure. Departments of Neuroscience & Cell Biology and Biochemistry & Molecular Biology (2015) (0)
Crystal structure of the TPR1 domain of HOP in complex with a HSC70 peptide (2000) (0)
CryoEM structure of Rubisco Activase with its substrate Rubisco from Nostoc sp. (strain PCC7120) (2020) (0)
Light-Driven Dihydrogen Production in [2Fe2S]-Metalloporphyrin Supramolecular Assemblies (2008) (0)
A06 Tuning the stress response pathway to respond to polyq aggregation (2021) (0)
In vivo substrates of the GroEL/ GroES chaperonin system (2005) (0)
Function of Molecular Chaperones in Protein Folding (1994) (0)
Novel proteostasis reporter mouse reveals different effects of cytoplasmic and nuclear aggregates on protein quality control in neurons (2020) (0)
CHAPERONE‐ASSISTED PROTEIN FOLDING IN THE CYTOSOL (2007) (0)
An organometallic polymer of osmium(0). Its electrosynthesis and electrocatalytic properties towards CO2 reduction (2001) (0)
Role of Prokaryotic Chaperonins in Protein Folding (1996) (0)
MODEL OF HEXAMERIC AAA DOMAIN ARRANGEMENT OF GREEN-TYPE RUBISCO ACTIVASE FROM TOBACCO. (2011) (0)
Crystal structure of the chaperonin gp146 from the bacteriophage EL 2 (Pseudomonas aeruginosa) in presence of ATP-BeFx, crystal form I (2020) (0)
Mitochondria and friends – a special issue in honor of Walter Neupert (1939–2019) (2020) (0)
The proteostasis network and its decline in ageing (2019) (0)
An inventory of interactors of the human HSP60/HSP10 chaperonin in the mitochondrial matrix space (2020) (0)
The mitochondrial stress protein HSP60 as a catalyst of protein folding (1990) (0)
Elektronikschutzgehäuse zur aufnahme einer elektronik (2014) (0)
Verfahren zur Ermittlung einer Temperatur von Flüssigmetall, Signalverarbeitungseinrichtung und metallurgische Vorrichtung (2010) (0)
Metallindustrieanlage und Verfahren zur Verfolgung eines Gefäßes, insbesondere eines metallurgischen Gefäßes (2014) (0)
Proteinfaltung in der Zelle: Die Rolle molekularer Chaperone (2007) (0)
Structure of Hgh1, crystal form I, Selenomethionine derivative (2019) (0)
Walter Neupert (1939–2019) (2019) (0)
Wolfgang Baumeister – Felix Hoppe-Seyler Lecturer 2004 (2004) (0)
Die verschuldung der freizeitwirtschaft ein versagen des marktes für beteiligungskapital (1995) (0)
Fabrikation von Knochenöl (0)
Crystal structure of the carbonic anhydrase-like domain of CcmM in complex with the C-terminal 17 residues of CcaA from Synechococcus elongatus (strain PCC 7942) (2021) (0)
Einfluss einer antiinflammatorischen Therapie auf die Colitis ulcerosa. Eine retrospektive Analyse. (2011) (0)
Crystal Structure of the small subunit-like domain 1 of CcmM from Synechococcus elongatus (strain PCC 7942) (2018) (0)
70 Three-dimensional arrangements of ribosomes inside fast growing E. coli cells (2015) (0)
Structure of the repeat unit in the network formed by CcmM and Rubisco from Synechococcus elongatus (2018) (0)
Quantitative Proteomics Reveals That Hsp90 Inhibition Preferentially Targets Kinases and the DNA Damage Response*□S (2012) (0)
Paper of the Year 2002: Award to Cordelia Schiene-Fischer. (2003) (0)
Steroid receptor inhibition by targeting heat shock protein 90 (2002) (0)
Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3 This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits distribution,andreproductioninanymedium,providedtheoriginalauthorandsourcearecredited. (2009) (0)
HUMAN HSP40 (HDJ-1), NMR (1996) (0)
Weichenantrieb with internal lock (1976) (0)
The N-terminal domain of Rubisco Accumulation Factor 1 from Arabidopsis thaliana (2015) (0)
MOLECULAR CHAPERONES & STRESS RESPONSES (2010) (0)
Crystal structure of the HspBP1 core domain (2005) (0)
Mechanisms of Stop Codon Readthrough Mitigation Reveal Principles of GCN1 Mediated Translational Quality Control (2022) (0)
Soluble polyQ protein impairs transcription factor function in a yeast model system (2005) (0)
Crystal structure of the full-length Hsp110 molecular chaperone in the nucleotide-free state (2008) (0)
Crystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVD (2000) (0)
Crystal structure of the GroEL mutant A109C in complex with GroES and ADP BeF2 (2018) (0)
Crystal structure of the AAA+ protein CbbX, selenomethionine structure (2011) (0)
Crystal structure of apo-CbbY from Rhodobacter sphaeroides (2014) (0)
Structure of the chaperonin gp146 from the bacteriophage EL (Pseudomonas aeruginosa) in complex with ATPgammaS (2020) (0)
Roger D. Kornberg Felix Hoppe-Seyler Lecturer 2001 (2001) (0)
Crystal structure of the BSD2 homolog of Arabidopsis thaliana bound to the octameric assembly of RbcL from Thermosynechococcus elongatus (2017) (0)
Crystal structure of human Hsf1 with Satellite III repeat DNA (2015) (0)
Crystal structure of RbcX point mutant Y17A/Y20L (2007) (0)
Substrate processing state 26S proteasome (SPS1) (2018) (0)
Structure of Rubisco from Rhodobacter sphaeroides in complex with CABP (2017) (0)
Chaperone mechanisms in cellular protein folding (2007) (0)
Pathways of chaperone-assisted protein folding in the cytosol (2000) (0)
Protein Folding | Chaperonins (2021) (0)
Structure of Chaetomium thermophilum Skn7 coiled-coil domain, crystal form III (2015) (0)
Paper of the Year 2001: Award to Peter Hacke. (2002) (0)
Structure of the chaperonin gp146 from the bacteriophage EL (Pseudomonas aeruginosa) in the apo state (2020) (0)
Crystal structure of CbbY (AT3G48420) from Arabidobsis thaliana (2014) (0)
Proteome-wide analysis of protein stability in E. coli using pulse proteolysis (2019) (0)
Crystal structure of the carbonic anhydrase-like domain of CcmM from Synechococcus elongatus (strain PCC 7942) (2021) (0)
Crystal structure of RbcX from Anabaena CA (2007) (0)
Alexander J. Varshavsky Felix Hoppe-Seyler Lecturer 2000 (2000) (0)
Protein Translocation Across Biological Membranes (1990) (0)
Paper of the Year 2004: Award to Yin Wang and Iris Lorenzi (2005) (0)
Cryo-EM structure of the RbcL-RbcX complex (2010) (0)
Crystal structure of selenomethionine-labeled RbcX (2007) (0)
mdepende t mech isms (1998) (0)
Ground state 26S proteasome (GS1) (2018) (0)
Structure of Hgh1, crystal form I (2019) (0)
Quo vadis with the Q tracts (2001) (0)
Crystal structure of CbbY from Rhodobacter sphaeroides in complex with phosphate (2014) (0)
Science Journals — AAAS (2017) (0)
Single molecule studies of the influence of GroEL in protein folding (2007) (0)
Substrate processing state 26S proteasome (SPS2) (2018) (0)
Crystal structure of the GroEL mutant A109C (2018) (0)
Prokaryotic secretion: a signal recognition particle in Escherichia coli? (1993) (0)
Crystal structure of Ta0583, an archaeal actin homolog, native data (2006) (0)
The C-terminal domain of Rubisco Accumulation Factor 1 from Arabidopsis thaliana, crystal form II (2015) (0)

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