Johannes Buchner
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German biochemist
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Johannes Buchnerbiology Degrees
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Biochemistry
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Biology
Johannes Buchner's Degrees
- PhD Biochemistry Ludwig Maximilian University of Munich
- Masters Chemistry Ludwig Maximilian University of Munich
- Bachelors Chemistry Ludwig Maximilian University of Munich
Why Is Johannes Buchner Influential?
(Suggest an Edit or Addition)According to Wikipedia, Johannes Buchner is a German biochemist and professor at the Technische Universität München, Munich, Germany. Career Buchner obtained his PhD at the University of Regensburg, Germany, working with Rainer Rudolph and Rainer Jaenicke. He performed his postdoctoral research in the lab of Ira Pastan at the National Cancer Institute of the National Institutes of Health in Bethesda, USA, before becoming assistant professor at the University of Regensburg and subsequently full professor and Chair of Biotechnology at the TUM.
Johannes Buchner'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
- The heat shock response: life on the verge of death. (2010) (1519)
- Small heat shock proteins are molecular chaperones. (1993) (1369)
- The HSP90 chaperone machinery (2017) (903)
- Some like it hot: the structure and function of small heat-shock proteins (2005) (780)
- Binding of non‐native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation (1997) (757)
- Regulation of Hsp27 Oligomerization, Chaperone Function, and Protective Activity against Oxidative Stress/Tumor Necrosis Factor α by Phosphorylation* (1999) (746)
- Hsp90 & Co. - a holding for folding. (1999) (654)
- Hsp70 and Hsp90--a relay team for protein folding. (2004) (599)
- Hsp90: Chaperoning signal transduction (2001) (585)
- Hsp90 chaperones protein folding in vitro (1992) (479)
- Hsp26: a temperature‐regulated chaperone (1999) (453)
- The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones. (2012) (452)
- Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1 (2011) (438)
- Protein Aggregation in vitro and in vivo: A Quantitative Model of the Kinetic Competition between Folding and Aggregation (1991) (425)
- Supervising the fold: functional principles of molecular chaperones (1996) (423)
- GroE facilitates refolding of citrate synthase by suppressing aggregation. (1991) (417)
- Structure, Function and Regulation of the Hsp90 Machinery (2013) (384)
- Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones. (1994) (376)
- Renaturation, Purification and Characterization of Recombinant Fab-Fragments Produced in Escherichia coli (1991) (373)
- The Hsp90 Chaperone Machinery* (2008) (367)
- Transient Interaction of Hsp90 with Early Unfolding Intermediates of Citrate Synthase (1995) (366)
- Chaperone Function of Hsp90-Associated Proteins (1996) (365)
- The Small Heat-shock Protein IbpB from Escherichia coli Stabilizes Stress-denatured Proteins for Subsequent Refolding by a Multichaperone Network* (1998) (349)
- A method for increasing the yield of properly folded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodies. (1992) (344)
- Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90 (2009) (323)
- Molecular chaperones--cellular machines for protein folding. (2002) (319)
- p53 contains large unstructured regions in its native state. (2002) (269)
- Protein folding handbook (2005) (264)
- The chaperone Hsp90: changing partners for demanding clients. (2013) (262)
- Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence. (1998) (250)
- The N-terminal domain of p53 is natively unfolded. (2003) (239)
- Asymmetric activation of the hsp90 dimer by its cochaperone aha1. (2010) (230)
- How chaperones fold proteins. (1998) (228)
- The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis (2009) (224)
- Independent evolution of the core domain and its flanking sequences in small heat shock proteins (2010) (224)
- The architecture of functional modules in the Hsp90 co‐chaperone Sti1/Hop (2012) (209)
- Analysis of chaperone function using citrate synthase as nonnative substrate protein. (1998) (203)
- An unfolded CH1 domain controls the assembly and secretion of IgG antibodies. (2009) (203)
- Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae (2004) (196)
- ThT 101: a primer on the use of thioflavin T to investigate amyloid formation (2017) (196)
- Coordinated ATP Hydrolysis by the Hsp90 Dimer* (2001) (193)
- Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40. (2001) (185)
- Disassembling Protein Aggregates in the Yeast Cytosol (2005) (184)
- Sti1 Is a Non-competitive Inhibitor of the Hsp90 ATPase (2003) (182)
- The Hsp90 Cochaperone, FKBP51, Increases Tau Stability and Polymerizes Microtubules (2010) (181)
- Symmetric complexes of GroE chaperonins as part of the functional cycle. (1994) (175)
- The Dynamics of Hsp25 Quaternary Structure (1999) (171)
- The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90 (2006) (170)
- Analysis of the Interaction of Small Heat Shock Proteins with Unfolding Proteins* (2003) (168)
- How antibodies fold. (2010) (164)
- The Hsp90 complex--a super-chaperone machine as a novel drug target. (1998) (164)
- Hsp90 is regulated by a switch point in the C‐terminal domain (2009) (162)
- Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions (2011) (160)
- Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. (2010) (158)
- Noncatalytic Role of the FKBP52 Peptidyl-Prolyl Isomerase Domain in the Regulation of Steroid Hormone Signaling (2007) (156)
- Regulated structural transitions unleash the chaperone activity of αB-crystallin (2013) (156)
- The biology of heat shock proteins and molecular chaperones: edited by R.I. Morimoto, A. Tisslères and C. Georgopoulos, Cold Spring Harbor Laboratory Press, 1994. $97.00 (vii + 610 pages) ISBN 0 87969 427 0 (1994) (156)
- Substrate transfer from the chaperone Hsp70 to Hsp90. (2006) (154)
- Hsp90 Regulates the Activity of Wild Type p53 under Physiological and Elevated Temperatures* (2004) (153)
- The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. (2004) (153)
- Mixed Hsp90–cochaperone complexes are important for the progression of the reaction cycle (2011) (152)
- On the role of groES in the chaperonin-assisted folding reaction. Three case studies. (1994) (151)
- Alternatively folded states of an immunoglobulin. (1991) (150)
- The Charged Linker Region Is an Important Regulator of Hsp90 Function* (2009) (138)
- Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach (2011) (138)
- Stress‐ and mitogen‐induced phosphorylation of the small heat shock protein Hsp25 by MAPKAP kinase 2 is not essential for chaperone properties and cellular thermoresistance. (1994) (137)
- Small heat shock proteins: Simplicity meets complexity (2018) (134)
- Modulation of the Hsp90 chaperone cycle by a stringent client protein. (2014) (133)
- Human Heat Shock Protein 70 Enhances Tumor Antigen Presentation through Complex Formation and Intracellular Antigen Delivery without Innate Immune Signaling* (2007) (133)
- Sti1 Is a Novel Activator of the Ssa Proteins* (2003) (133)
- The growing world of small heat shock proteins: from structure to functions (2017) (129)
- The Prion Curing Agent Guanidinium Chloride Specifically Inhibits ATP Hydrolysis by Hsp104* (2004) (129)
- Conserved Conformational Changes in the ATPase Cycle of Human Hsp90* (2008) (127)
- The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client (2015) (125)
- Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation. (2012) (122)
- Analysis of the Regulation of the Molecular Chaperone Hsp26 by Temperature-induced Dissociation (2004) (121)
- BiP Binding Sequences in Antibodies (*) (1995) (120)
- The eye lens chaperone α-crystallin forms defined globular assemblies (2009) (118)
- Mouse Hsp25, a small heat shock protein (2000) (117)
- BiP and PDI Cooperate in the Oxidative Folding of Antibodiesin Vitro * (2000) (117)
- Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle (2010) (113)
- Cpr6 and Cpr7, Two Closely Related Hsp90-associated Immunophilins from Saccharomyces cerevisiae, Differ in Their Functional Properties* (2000) (113)
- The ATPase Cycle of the Endoplasmic Chaperone Grp94* (2007) (112)
- C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle. (2000) (112)
- Evolution of Escherichia coli for Growth at High Temperatures* (2010) (111)
- Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53 (2011) (111)
- The Hsp90 machinery facilitates the transport of diphtheria toxin into human cells (2017) (111)
- The Yeast Hsp110 Sse1 Functionally Interacts with the Hsp70 Chaperones Ssa and Ssb* (2005) (110)
- IspH protein of Escherichia coli: studies on iron-sulfur cluster implementation and catalysis. (2004) (109)
- Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop (2014) (108)
- Alternative bacterial two-component small heat shock protein systems (2012) (106)
- Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle (2013) (106)
- The Chaperone Activity and Substrate Spectrum of Human Small Heat Shock Proteins* (2016) (105)
- The ATPase Cycle of the Mitochondrial Hsp90 Analog Trap1* (2008) (105)
- Structure, Function, and Regulation of the Hsp90 Machinery. (2019) (104)
- Molecular Chaperones — Cellular Machines for Protein Folding (2002) (103)
- p53--a natural cancer killer: structural insights and therapeutic concepts. (2006) (102)
- A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization. (2004) (102)
- Activation of the chaperone Hsp26 is controlled by the rearrangement of its thermosensor domain. (2008) (99)
- ATP-binding Properties of Human Hsp90* (1997) (99)
- Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of alpha-glucosidase from yeast. (1991) (95)
- The Plasticity of the Hsp90 Co-chaperone System. (2017) (95)
- The charged region of Hsp90 modulates the function of the N-terminal domain. (1999) (93)
- Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. (2006) (92)
- An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function. (1999) (92)
- Functional Characterization of the Higher Plant Chloroplast Chaperonins (*) (1995) (91)
- Assessment of the ATP Binding Properties of Hsp90 (*) (1996) (90)
- Membrane Translocation of Binary Actin-ADP-Ribosylating Toxins from Clostridium difficile and Clostridium perfringens Is Facilitated by Cyclophilin A and Hsp90 (2011) (89)
- The activation mechanism of Hsp26 does not require dissociation of the oligomer. (2005) (88)
- Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules (2015) (85)
- Renaturation of a Single–Chain Immunotoxin Facilitated by Chaperones and Protein Disulfide Isomerase (1992) (83)
- Review: a structural view of the GroE chaperone cycle. (2001) (83)
- Catalysis of protein folding by symmetric chaperone complexes. (1997) (82)
- Structure and function of α-crystallins: Traversing from in vitro to in vivo. (2016) (82)
- Influence of protein disulfide isomerase (PDI) on antibody folding in vitro. (1994) (82)
- Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain (2009) (82)
- Independent domain folding of Pseudomonas exotoxin and single-chain immunotoxins: influence of interdomain connections. (1992) (82)
- Folding and association of the antibody domain CH3: prolyl isomerization preceeds dimerization. (1999) (81)
- The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function (2014) (81)
- Structure of the murine unglycosylated IgG1 Fc fragment. (2009) (80)
- Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p. (2001) (80)
- Conformational processing of oncogenic v-Src kinase by the molecular chaperone Hsp90 (2015) (79)
- Chaperone function of sHsps. (2002) (78)
- Structural Organization of Procaryotic and Eucaryotic Hsp90. INFLUENCE OF DIVALENT CATIONS ON STRUCTURE AND FUNCTION (*) (1995) (78)
- NMR Chemical Shift Perturbation Study of the N‐Terminal Domain of Hsp90 upon Binding of ADP, AMP‐PNP, Geldanamycin, and Radicicol (2003) (77)
- Multi-Angle Effector Function Analysis of Human Monoclonal IgG Glycovariants (2015) (77)
- Folding mechanism of the CH2 antibody domain. (2004) (75)
- Interaction of GroE with an all-beta-protein. (1992) (75)
- Importance of cycle timing for the function of the molecular chaperone Hsp90 (2016) (72)
- High-resolution structures of the IgM Fc domains reveal principles of its hexamer formation (2013) (72)
- Prolyl isomerases catalyze antibody folding in vitro (1993) (72)
- Association of antibody chains at different stages of folding: prolyl isomerization occurs after formation of quaternary structure. (1995) (71)
- Mouse Hsp25, a small shock protein. The role of its C-terminal extension in oligomerization and chaperone action. (2000) (68)
- Intrinsic Inhibition of the Hsp90 ATPase Activity* (2006) (67)
- N-terminal Residues Regulate the Catalytic Efficiency of the Hsp90 ATPase Cycle* (2002) (64)
- Refolding of inclusion body proteins. (2004) (64)
- Localization of the Chaperone Domain of FKBP52* (2001) (62)
- Role of CypA and Hsp90 in membrane translocation mediated by anthrax protective antigen (2011) (62)
- The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins (2014) (60)
- Cns1 Is an Activator of the Ssa1 ATPase Activity* (2004) (60)
- Structural dynamics of archaeal small heat shock proteins. (2008) (59)
- FK506-binding protein 52 phosphorylation: a potential mechanism for regulating steroid hormone receptor activity. (2007) (58)
- Dynamics of the GroEL-protein complex: effects of nucleotides and folding mutants. (1996) (58)
- Dissection of the Contribution of Individual Domains to the ATPase Mechanism of Hsp90* (2003) (58)
- BiP-binding Sequences in HIV gp160 (1999) (58)
- hsp90: Twist and Fold (2006) (57)
- The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25. (1998) (56)
- Folding and association of β-galactosidase (1998) (54)
- Hsc70, immunoglobulin heavy chain binding protein, and Hsp90 differ in their ability to stimulate transport of precursor proteins into mammalian microsomes. (1993) (54)
- Posttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitors. (2013) (54)
- Cytosolic Hsp70 and Hsp40 chaperones enable the biogenesis of mitochondrial β-barrel proteins (2018) (53)
- The cytosolic cochaperone Sti1 is relevant for mitochondrial biogenesis and morphology (2016) (53)
- Modulation of the ATPase cycle of BiP by peptides and proteins. (2003) (52)
- Cooperative binding of p53 to DNA: regulation by protein-protein interactions through a double salt bridge. (2005) (51)
- Folding and oxidation of the antibody domain C(H)3. (2002) (51)
- The small heat shock protein Hsp27 affects assembly dynamics and structure of keratin intermediate filament networks. (2013) (51)
- Small heat shock proteins: multifaceted proteins with important implications for life (2019) (50)
- Folding and assembly of the large molecular machine Hsp90 studied in single-molecule experiments (2016) (50)
- Coordinated Conformational Processing of the Tumor Suppressor Protein p53 by the Hsp70 and Hsp90 Chaperone Machineries. (2019) (49)
- Oncogenic mutations reduce the stability of SRC kinase. (2004) (48)
- Formation of She2p tetramers is required for mRNA binding, mRNP assembly, and localization. (2009) (48)
- The Chaperone Activity of the Developmental Small Heat Shock Protein Sip1 Is Regulated by pH-Dependent Conformational Changes. (2015) (47)
- The Heat Shock Response in Yeast Maintains Protein Homeostasis by Chaperoning and Replenishing Proteins. (2019) (47)
- Stabilization of proteins and peptides in diagnostic immunological assays by the molecular chaperone Hsp25. (1998) (46)
- Allosteric Regulation Points Control the Conformational Dynamics of the Molecular Chaperone Hsp90. (2016) (46)
- The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity (2008) (45)
- Purification and characterization of small heat shock proteins. (1998) (44)
- The alternatively folded state of the antibody C(H)3 domain. (2001) (44)
- Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding. (1995) (44)
- Analysis of Chaperone Properties of Small Hsp (2000) (43)
- Binding sites for Hsp70 molecular chaperones in natural proteins. (1995) (43)
- Influence of the internal disulfide bridge on the folding pathway of the CL antibody domain. (2007) (42)
- BiPPred: Combined sequence‐ and structure‐based prediction of peptide binding to the Hsp70 chaperone BiP (2016) (42)
- Refolding and structural characterization of the human p53 tumor suppressor protein. (2002) (41)
- Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes (2007) (41)
- Conformational selection in substrate recognition by Hsp70 chaperones. (2013) (41)
- The State of the Art of Chemical Biology (2009) (40)
- Functional principles and regulation of molecular chaperones. (2019) (40)
- Protein aggregation as a cause for disease. (2006) (39)
- Routes to active proteins from transformed microorganisms. (1991) (38)
- Single-molecule force spectroscopy reveals folding steps associated with hormone binding and activation of the glucocorticoid receptor (2018) (38)
- Oxidation in the complementarity-determining regions differentially influences the properties of therapeutic antibodies (2016) (38)
- Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90 (2020) (37)
- Principles and engineering of antibody folding and assembly. (2014) (37)
- Scalable Production in Human Cells and Biochemical Characterization of Full-Length Normal and Mutant Huntingtin (2015) (37)
- The Hsp90 co-chaperone p23 of Toxoplasma gondii: Identification, functional analysis and dynamic interactome determination. (2010) (36)
- Regions outside the alpha-crystallin domain of the small heat shock protein Hsp26 are required for its dimerization. (2010) (36)
- Hop/Sti1 phosphorylation inhibits its co-chaperone function (2014) (36)
- Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate (2017) (34)
- Bacterial Hsp90 – desperately seeking clients (2010) (34)
- How GroES Regulates Binding of Nonnative Protein to GroEL* (1997) (33)
- The Cochaperone SGTA (Small Glutamine-rich Tetratricopeptide Repeat-containing Protein Alpha) Demonstrates Regulatory Specificity for the Androgen, Glucocorticoid, and Progesterone Receptors* (2014) (33)
- Catalysis, commitment and encapsulation during GroE-mediated folding. (1999) (32)
- A switch point in the molecular chaperone Hsp90 responding to client interaction (2018) (31)
- A chemical compound inhibiting the Aha1–Hsp90 chaperone complex (2017) (30)
- Targeting the FKBP51/GR/Hsp90 Complex to Identify Functionally Relevant Treatments for Depression and PTSD. (2018) (30)
- Regulation of the Chaperone Function of Small Hsps (2015) (30)
- The structure and oxidation of the eye lens chaperone αA-crystallin (2019) (30)
- Structural and functional diversity in the family of small heat shock proteins from the parasite Toxoplasma gondii. (2009) (29)
- Fatal amyloid formation in a patient’s antibody light chain is caused by a single point mutation (2020) (28)
- The IMiD target CRBN determines HSP90 activity toward transmembrane proteins essential in multiple myeloma (2021) (28)
- Clusterin associates with altered elastic fibers in human photoaged skin and prevents elastin from ultraviolet-induced aggregation in vitro. (2007) (28)
- Wheat FKBP73 functions in vitro as a molecular chaperone independently of its peptidyl prolyl cis-trans isomerase activity (2002) (27)
- GroEL Traps Dimeric and Monomeric Unfolding Intermediates of Citrate Synthase* (1998) (26)
- Synthesis and characterization of a functional intact IgG in a prokaryotic cell-free expression system (2008) (26)
- Oxidative folding of peptides and proteins (2008) (26)
- MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors (2017) (26)
- The regulatory domain stabilizes the p53 tetramer by intersubunit contacts with the DNA binding domain. (2013) (25)
- The Antibody Light-Chain Linker Regulates Domain Orientation and Amyloidogenicity. (2018) (25)
- Analysis of chaperone properties of small Hsp's. (2000) (25)
- Domain interactions stabilize the alternatively folded state of an antibody Fab fragment (1995) (25)
- The folding pathway of the antibody V(L) domain. (2009) (25)
- Molecular chaperones and protein quality control: an introduction to the JBC Reviews thematic series (2019) (24)
- Limits of Protein Folding Inside GroE Complexes* (2000) (23)
- Global analysis of phosphoproteome regulation by the Ser/Thr phosphatase Ppt1 in Saccharomyces cerevisiae. (2012) (23)
- Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy. (2018) (23)
- The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range (2019) (23)
- Evidence for an "active serine" in each fatty acid synthetase peptide. (1976) (23)
- A Grp on the Hsp90 mechanism. (2007) (23)
- Structural and Functional Analysis of the DEAF-1 and BS69 MYND Domains (2012) (22)
- Purification of Hsp90 partner proteins Hop/p60, p23, and FKBP52. (1998) (22)
- Purification and characterization of prokaryotic and eukaryotic Hsp90. (1998) (22)
- Characterization of a quaternary‐structured folding intermediate of an antibody Fab‐fragment (1995) (22)
- Glycosylation inhibits the interaction of invertase with the chaperone GroEL (1992) (22)
- Correlation between the stability of the GroEL-protein ligand complex and the release mechanism. (1994) (22)
- p23 and Aha1. (2015) (22)
- Breakdown of supersaturation barrier links protein folding to amyloid formation (2021) (22)
- A Stable Mutant Predisposes Antibody Domains to Amyloid Formation through Specific Non-Native Interactions. (2016) (21)
- Rapid Matrix‐Assisted Refolding of Histidine‐Tagged Proteins (2009) (21)
- Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle (2021) (21)
- Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains (2017) (21)
- Recombinant expression and purification of Ssa1p (Hsp70) from Saccharomyces cerevisiae using Pichia pastoris. (2003) (21)
- Imbalances in the eye lens proteome are linked to cataract formation (2021) (20)
- Hsp90 Co-chaperones Form Plastic Genetic Networks Adapted to Client Maturation. (2020) (20)
- GroE dependence of refolding and holoenzyme formation of 6-hydroxy-D-nicotine oxidase. (1992) (20)
- The Antibody Light-Chain Linker Is Important for Domain Stability and Amyloid Formation. (2015) (20)
- Hsp90 dependence of a kinase is determined by its conformational landscape (2017) (20)
- Structural and mechanical hierarchies in the alpha-crystallin domain dimer of the hyperthermophilic small heat shock protein Hsp16.5. (2010) (20)
- Interaction of the chaperone BiP with an antibody domain: implications for the chaperone cycle. (2002) (20)
- Determinants of the assembly and function of antibody variable domains (2017) (19)
- Hsp90‐mediated regulation of DYRK3 couples stress granule disassembly and growth via mTORC1 signaling (2021) (19)
- The Crystal Structure of the Fab Fragment of the Monoclonal Antibody MAK33 (2001) (19)
- Contribution of N‐ and C‐terminal domains to the function of Hsp90 in Saccharomyces cerevisiae (1999) (19)
- DISASSEMBLING PROTEIN AGGREGATES IN THE YEAST CYTOSOL: THE COOPERATION OF HSP26 WITH SSA1 AND HSP104. (2005) (19)
- Dissecting the alternatively folded state of the antibody Fab fragment. (2010) (19)
- Assays to characterize molecular chaperone function in vitro. (2015) (18)
- Analysis of GroE-assisted Folding under Nonpermissive Conditions* (1999) (17)
- Unique proline-rich domain regulates the chaperone function of AIPL1. (2013) (17)
- The Co-chaperone Cns1 and the Recruiter Protein Hgh1 Link Hsp90 to Translation Elongation via Chaperoning Elongation Factor 2. (2019) (17)
- A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 (2020) (16)
- A peptide extension dictates IgM assembly (2017) (16)
- A Residue-specific Shift in Stability and Amyloidogenicity of Antibody Variable Domains* (2014) (16)
- Artificial accelerators of the molecular chaperone Hsp90 facilitate rate-limiting conformational transitions. (2014) (16)
- Regulation of small heat-shock proteins by hetero-oligomer formation (2019) (16)
- Molecular mechanism of amyloidogenic mutations in hypervariable regions of antibody light chains (2021) (16)
- Mechanical stability of the antibody domain CH3 homodimer in different oxidation states. (2013) (16)
- Closing in on the Hsp90 chaperone-client relationship. (2011) (15)
- Cross-Linking GPVI-Fc by Anti-Fc Antibodies Potentiates Its Inhibition of Atherosclerotic Plaque- and Collagen-Induced Platelet Activation (2016) (15)
- Interaction of human heat shock protein 70 with tumor-associated peptides (2009) (14)
- Induction of Heat Shock Proteins and the Proteasome System by Casein‐Nɛ‐(Carboxymethyl)lysine and Nɛ‐(Carboxymethyl)lysine in Caco‐2 Cells (2008) (14)
- Hierarchical Formation of Disulfide Bonds in the Immunoglobulin Fc Fragment Is Assisted by Protein-disulfide Isomerase* (2004) (13)
- Picomolar inhibition of SARS-CoV-2 variants of concern by an engineered ACE2-IgG4-Fc fusion protein (2021) (13)
- Intradomain disulfide bonds impede formation of the alternatively folded state of antibody chains. (2002) (13)
- Influence of the oxidoreductase ER57 on the folding of an antibody fab fragment. (2004) (12)
- Experimental optimization of protein refolding with a genetic algorithm (2010) (11)
- Autophosphorylation activates c-Src kinase through global structural rearrangements (2019) (11)
- Characterization of oligomeric species in the fibrillization pathway of the yeast prion Ure2p (2005) (11)
- Domain interactions determine the amyloidogenicity of antibody light chain mutants. (2020) (10)
- Fungal and bacterial colonies growing on weathered wood surfaces (2019) (10)
- The HsP90 Family : an overview (1997) (10)
- The phosphatase Ppt 1 is a dedicated regulator of the molecular chaperone Hsp 90 (2013) (10)
- Folding and association of beta-Galactosidase. (1998) (9)
- Stability and Design of alpha-Helices (2005) (9)
- GET two for one. (2014) (9)
- Folding pathway enigma (1990) (8)
- Stratigraphy, sedimentology, paleontology, and paleomagnetism of Pliocene-early Pleistocene lacustrine deposits in two cores from western Utah (1995) (8)
- Surface Quality of Planed Beech Wood (Fagus sylvatica L.) Thermally Treated for Different Durations of Time (2017) (8)
- Efficient inhibition of SARS-CoV-2 strains by a novel ACE2-IgG4-Fc fusion protein with a stabilized hinge region (2020) (8)
- Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble (2021) (8)
- Biogenesis of secretory immunoglobulin M requires intermediate non‐native disulfide bonds and engagement of the protein disulfide isomerase ERp44 (2021) (8)
- Dissection of the amyloid formation pathway in AL amyloidosis (2021) (8)
- Regulation of small heat-shock proteins by hetero-oligomer formation. (2020) (7)
- The crystal structure of the Fab fragment of the monoclonal antibody MAK33 Implications for folding and interaction with the chaperone BiP (2000) (7)
- CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF THE MONOCLONAL ANTIBODY MAK33 (2000) (7)
- Hsp90: From Dispensable Heat Shock Protein to Global Player (2008) (7)
- Analysis of Chaperone Function in Vitro (2008) (7)
- Introduction: the cellular protein folding machinery (2002) (7)
- The network of molecular chaperones: insights in the cellular proteostasis machinery. (2015) (6)
- Assisted protein folding (1999) (6)
- An alternative splice variant of human αA-crystallin modulates the oligomer ensemble and the chaperone activity of α-crystallins (2017) (6)
- Mechanistic aspects of the Hsp90 phosphoregulation (2012) (6)
- The switch from client holding to folding in the Hsp70/Hsp90 chaperone machineries is regulated by a direct interplay between co-chaperones. (2022) (6)
- Small Heat‐Shock Proteins (2002) (6)
- The charged region of Hsp 90 modulates the function of the N-terminal domain ( heat shock proteins y antitumor drugs y peptide binding y steroid receptors y titration calorimetry ) (1999) (6)
- Collagen’s primary structure determines collagen:HSP47 complex stoichiometry (2021) (4)
- Nucleotide-Dependent Dimer Association and Dissociation of the Chaperone Hsp90. (2018) (4)
- Mechanistic principles of an ultra-long bovine CDR reveal strategies for antibody design (2021) (4)
- Active unfolding of the glucocorticoid receptor by the Hsp70/Hsp40 chaperone system in single-molecule mechanical experiments (2022) (4)
- A single residue switch reveals principles of antibody domain integrity (2018) (4)
- Antibodies gone bad – the molecular mechanism of light chain amyloidosis (2022) (3)
- Hygienic Perspectives of Wood in Healthcare Buildings (2021) (3)
- Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae (2020) (3)
- Peptides in proteins (2019) (3)
- Post-translational modification and conformational state of Heat Shock Protein 90 differentially affect binding of chemically diverse small molecule inhibitors (2013) (3)
- A network of cytosolic (co)chaperones promotes the biogenesis of mitochondrial signal-anchored outer membrane proteins (2022) (2)
- Acidification activates ERp44--a molecular litmus test for protein assembly. (2013) (2)
- The in vitro catalysis of protein folding by endoplasmic reticulum luminal peptidyl prolyl cis-trans isomerase. (1995) (2)
- p53 — A Natural Cancer Killer: Structural Insights and Therapeutic Concepts (2007) (1)
- Influence of geotechnical parameters on dust potential of sulphate bearing clay-siltstone in tunnelling works (2020) (1)
- The Chaperone Activity of the Developmental Small Heat Shock Protein Sip 1 Is Regulated by pH-Dependent Conformational Changes Graphical (2015) (1)
- Murine unglycosylated IgG Fc fragment (2009) (1)
- Thermospray liquid chromatography mass spectrometry of thiol radioprotective agents: characteristic spectra. (1988) (1)
- Protein folding by interaction. (2014) (1)
- The growing world of small heat shock proteins: from structure to functions (2017) (1)
- Multimeric ACE2-IgM fusions as broadly active antivirals that potently neutralize SARS-CoV-2 variants (2022) (1)
- A constant domain mutation in a patient-derived antibody light chain reveals principles of AL amyloidosis (2023) (1)
- Molecular architectures of the 24meric eye lens chaperone alphaB- crystallin elucidated by a triple hybrid approach (2011) (1)
- FEBS Open Bio: past, present and future (2021) (1)
- Surface roughness of heat treated and untreated beech (Fagus sylvatica L.) wood after sanding (2019) (1)
- Unravelling the Mechanics of a Molecular Chaperone (2018) (0)
- The permanently chaperone-active small heat shock protein Hsp17 from Caenorhabditis elegans exhibits topological separation of its N-terminal regions (2022) (0)
- Backbone 1H, 15N, 13C chemical shift assignments for MAK33 EV-CH2-SK antibody domain extended variant (2018) (0)
- The IMiD-Target Cereblon Determines Transmembrane Protein Quality Control Promoting Tumor Metabolism (2019) (0)
- In memoriam—Rainer Jaenicke (2017) (0)
- Book Review: Methods in Molecular Biology, Vol. 232: Protein Misfolding and Disease: Principles and Methods. Edited by Peter Bross and Niels Gregerson. (2004) (0)
- Extrinsic stabilization of antiviral ACE2-Fc fusion proteins targeting SARS-CoV-2 (2023) (0)
- IgM C4-domain from mouse (2013) (0)
- The Hsp90 machinery facilitates the transport of diphtheria toxin into human cells (2017) (0)
- Solution structure of the yeast Sti1 DP1 domain (2012) (0)
- The Hsp90 Family of Molecular Chaperones (2008) (0)
- Mutant immunoglobulin light chain causing amyloidosis (Pat-1) (2020) (0)
- Chapter 2:Oxidative Folding of Proteins in vitro (2008) (0)
- Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate (2018) (0)
- TPR2AB-domain:pHSP90-complex of yeast Sti1 (2012) (0)
- Chaperone function on Crete: a meeting report. (1996) (0)
- The structure and oxidation of the eye lens chaperone αA-crystallin (2019) (0)
- Author response: Fatal amyloid formation in a patient’s antibody light chain is caused by a single point mutation (2020) (0)
- Role of host cell chaperones in cellular uptake of binary clostridial enterotoxins (2016) (0)
- IgNAR antibody domain C2 (2014) (0)
- Solution structure of the yeast Sti1 DP2 domain (2012) (0)
- Solid- and solution-state nuclear magnetic resonance spectroscopic studies on antibody light chain amyloid formation and interactions with epigallocatechin gallate (2017) (0)
- Table of Contents (1994) (0)
- Breakdown of supersaturation barrier links protein folding to amyloid formation (2021) (0)
- Erratum to “Interaction of the Chaperone BiP with an Antibody Domain: Implications for the Chaperone Cycle” (2002) (0)
- The Anfinsen machinery (2003) (0)
- Backbone 1H, 13C, and 15N Chemical Shift Assignments for the yeast Hsp90 Middle Domain (2011) (0)
- NMR Assignment of the C-terminal Domain of yeast Aha-1 (2009) (0)
- CHAPTER 2.2:In vitro Refolding of Proteins (2018) (0)
- The Plasticity of the Hsp 90 Co-chaperone System Graphical Abstract Highlights (2017) (0)
- Heat Shock Proteins Regulate Structure of Intermediate Filament Networks (2012) (0)
- Backbone 1H, 15N, 13C chemical shift assignments for the MAK33 CH2 antibody domain (2018) (0)
- High resolution NMR structure of the C mu3 domain from IgM (2013) (0)
- Coordination between N- and C-terminal Kinetics of Hsp90 Investigated by SmFRET (2010) (0)
- Author Correction: A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 (2020) (0)
- Determinants of the assembly and function of antibody variable domains (2017) (0)
- antibody generation expressed activation of gene-technologically produced, in prokaryotic (1988) (0)
- 13C, 15N chemical shift assignments of MAK33 VL S20N amyloid fibrils (2017) (0)
- Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90 (2020) (0)
- Hsp17.7 from Deinococcus radiodurans (2012) (0)
- CRYSTAL STRUCTURE OF THE CH3 DOMAIN FROM THE MAK33 ANTIBODY (1999) (0)
- A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 (2020) (0)
- Stress-induced protein 1 from Caenorhabditis elegans (2015) (0)
- A process for the expression of proteins in an in vitro translation system with co-expression of helper proteins fold (2002) (0)
- Stress-induced protein 1 truncation mutant (43 - 140) from Caenorhabditis elegans (2015) (0)
- 3.10 Chaperones and Protein Folding (2012) (0)
- An alternative splice variant of human αA-crystallin modulates the oligomer ensemble and the chaperone activity of α-crystallins (2017) (0)
- Response to Corcos: exceptions to the rules (2010) (0)
- IgNAR antibody domain C1 (2014) (0)
- Pseudo-atomic model of a 16-mer assembly of reduced recombinant human alphaA-crystallin (non domain swapped configuration) (2019) (0)
- p23 and Aha1: Distinct Functions Promote Client Maturation. (2023) (0)
- Details of the Conformational Cycle of Hsp90 Probed using Optical Tweezers (2020) (0)
- Chaperone Function in Vitro (2008) (0)
- IgNAR antibody domain C3 (2014) (0)
- Studying the Function of BAP in the Nucleotide Cycle of BIP by spFRET using MFD-PIE (2016) (0)
- Hsp90 Delta24-N210 mutant (2006) (0)
- PNAS Plus Significance Statements (2015) (0)
- Observing the Regulation of the Hsp90 Chaperone by Co-Chaperones and Nucleotides (2021) (0)
- Solution-state NMR assignment of the flexible C-terminal domain of the human eye lens molecular chaperone alphaA-crystallin (2019) (0)
- A switch point in the molecular chaperone Hsp90 responding to client interaction (2018) (0)
- Small heat shock proteins: multifaceted proteins with important implications for life (2019) (0)
- IgM C2-domain from mouse (2013) (0)
- Combining Electron Microscopy (EM) and Cross-Linking Mass Spectrometry (XL-MS) for Structural Characterization of Protein Complexes. (2021) (0)
- Highly functional nanocellulose-reinforced thermoplastic starch-based nanocomposites (2023) (0)
- The Protection of Beech Wood (”Fagus Sylvatic”a) against the brown Rot ”Postia Placenta” using Clove (”Eugenia Caryophyllata”) Essential Oil in a Linseed Oil Medium (2021) (0)
- Chaperones and protein folding (2012) (0)
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