Manajit Hayer-Hartl Singaporean German biochemist
Hayer-Hartl, Manajit 1954-
VIAF ID: 434159234446103371770 (Personal)
Permalink: http://viaf.org/viaf/434159234446103371770
Preferred Forms
4xx's: Alternate Name Forms (4)
5xx's: Related Names (2)
Works
| Title | Sources |
|---|---|
| Active Cage Mechanism of Chaperonin-Assisted Protein Folding Demonstrated at Single-Molecule Level |
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| Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions |
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| Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein |
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| Biogenesis and Metabolic Maintenance of Rubisco |
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| Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation |
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| Chaperone Machineries of Rubisco - The Most Abundant Enzyme |
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| Chaperonin-catalyzed rescue of kinetically trapped states in protein folding |
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| Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes |
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| Complex Chaperone Dependence of Rubisco Biogenesis. |
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| Crystal structure of apo-CbbY from Rhodobacter sphaeroides |
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| Crystal structure of CbbY (AT3G48420) from Arabidobsis thaliana |
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| Crystal structure of human Hsf1 with Satellite III repeat DNA |
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| Crystal Structure of N-acetylneuraminate lyase from Mycoplasma synoviae, crystal form II |
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| Crystal structure of phosphoribulokinase from Synechococcus sp. strain PCC 6301 |
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| Crystal structure of RbcX-IIa from Chlamydomonas reinhardtii in complex with RbcL C-terminal tail |
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| Crystal structure of RbcX point mutant Y17A/Y20L |
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| Crystal structure of the AAA+ protein CbbX, selenomethionine structure |
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| Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK |
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| Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei |
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| DnaK functions as a central hub in the E. coli chaperone network. |
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| Dual Role of a Rubisco Activase in Metabolic Repair and Carboxysome Organization |
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| Erratum: Degradation of potent Rubisco inhibitor by selective sugar phosphatase |
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| Essential role of the chaperonin folding compartment in vivo |
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| Failure of RQC machinery causes protein aggregation and proteotoxic stress. |
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| From chaperonins to Rubisco assembly and metabolic repair |
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| Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed |
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| Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation |
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| Gro-EL Fragment (Apical Domain) Comprising Residues 188-379 |
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| GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding |
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| The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding |
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| How to orient the functional GroEL-SR1 mutant for atomic force microscopy investigations. |
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| In vivo aspects of protein folding and quality control |
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| Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phosphatidylglycerol bilayers, studied by deuterium and phosphorus-31 NMR spectroscopy |
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| Interactions of phospholipids with the mitochondrial cytochrome-c reductase studied by spin-label ESR and NMR spectroscopy |
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| Interplay of Acetyltransferase EP300 and the Proteasome System in Regulating Heat Shock Transcription Factor 1 |
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| A mobile loop order-disorder transition modulates the speed of chaperonin cycling |
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| Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity |
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| Molecular species of cardiolipin in relation to other mitochondrial phospholipids. Is there an acyl specificity of the interaction between cardiolipin and the ADP/ATP carrier? |
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| Monitoring Protein Conformation along the Pathway of Chaperonin-Assisted Folding |
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| The N-terminal domain of Rubisco Accumulation Factor 1 from Arabidopsis thaliana |
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| Negative stain EM Map of the AAA protein CbbX, a red-type Rubisco activase from R. sphaeroides |
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| Nitric Oxide Inhibits the Cochaperone Activity of the RING Finger-like Protein DnaJ |
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| Opposing effects of folding and assembly chaperones on evolvability of Rubisco |
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| Plant RuBisCo assembly in E. coli with five chloroplast chaperones including BSD2. |
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| PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone |
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| Protein folding in the cytoplasm and the heat shock response |
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| The protein import motor of mitochondria: a targeted molecular ratchet driving unfolding and translocation |
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| Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli |
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| Real-time observation of trigger factor function on translating ribosomes. |
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| Recent advances in understanding catalysis of protein folding by molecular chaperones |
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| Role of auxiliary proteins in Rubisco biogenesis and function |
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| Role of small subunit in mediating assembly of red-type form I Rubisco |
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| Rubisco Activases: AAA+ Chaperones Adapted to Enzyme Repair |
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| Scaffolding protein CcmM directs multiprotein phase separation in β-carboxysome biogenesis |
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| Shift reagents for 39K Nmr |
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| A Simple Semiempirical Model for the Effect of Molecular Confinement upon the Rate of Protein Folding |
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| Soluble Oligomers of PolyQ-Expanded Huntingtin Target a Multiplicity of Key Cellular Factors |
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| Structural basis for subunit assembly in UDP-glucose pyrophosphorylase from Saccharomyces cerevisiae |
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| Structural plasticity and noncovalent substrate binding in the GroEL apical domain. A study using electrospay ionization mass spectrometry and fluorescence binding studies |
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| Structure and conformational cycle of a bacteriophage-encoded chaperonin |
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| Structure and mechanism of the Rubisco-assembly chaperone Raf1 |
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| Structure of Chaetomium thermophilum Skn7 coiled-coil domain, crystal form III |
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| Structure of green-type Rubisco activase from tobacco |
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| Structure of human heat-shock transcription factor 1 in complex with DNA |
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| What is the molten globule? |
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