beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange.

No abstract is available for this paper.

• Publication year

  1996

• Venue

  Proceedings of the National Academy of Sciences of the United States of America

• Publication date

  1996-10-29

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.1073/PNAS.93.22.12189PMID 8901555PMCID PMC37965
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Investigation of protein folding by mass spectrometry

  1996cited by this paper
• Mechanisms and uses of hydrogen exchange.

  1996cited by this paper
• Catalysis of Amide Proton Exchange by the Molecular Chaperones GroEL and SecB

  1996cited by this paper
• A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo

  1996cited by this paper
• Protein folding in the cell: competing models of chaperonin function

  1996cited by this paper
• Relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase.

  1995cited by this paper
• Investigation of the folding pathway of the TEM-1 beta-lactamase.

  1995cited by this paper
• Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding.

  1995cited by this paper
• The Hydrophobic Nature of GroEL-Substrate Binding (*)

  1995cited by this paper
• The chaperonin GroEL does not recognize apo-alpha-lactalbumin in the molten globule state.

  1994cited by this paper
• Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES

  1994cited by this paper
• "Partly folded" state, a new equilibrium state of protein molecules: four-state guanidinium chloride-induced unfolding of beta-lactamase at low temperature.

  1994cited by this paper
• Residues in chaperonin GroEL required for polypeptide binding and release

  1994cited by this paper
• The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

  1994cited by this paper
• Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha‐lactalbumin.

  1994cited by this paper
• Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature beta-lactamase.

  1994cited by this paper
• Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of beta-lactamase precursor.

  1994cited by this paper
• Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

  1994cited by this paper
• Destabilization of the complete protein secondary structure on binding to the chaperone GroEL

  1994cited by this paper
• Isotope effects in peptide group hydrogen exchange

  1993cited by this paper
• Detection of transient protein folding populations by mass spectrometry.

  1993cited by this paper
• Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule.

  1993cited by this paper
• Crystal structure of Escherichia coli TEM1 β‐lactamase at 1.8 Å resolution

  1993cited by this paper
• Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways.

  1993cited by this paper
• A standard numbering scheme for the class A beta-lactamases.

  1991cited by this paper
• Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

  1991cited by this paper
• Binding of a chaperonin to the folding intermediates of lactate dehydrogenase.

  1991cited by this paper
• Acid-induced folding of proteins.

  1990cited by this paper
• Mechanism of acid-induced folding of proteins.

  1990cited by this paper
• Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high salt.

  1989cited by this paper
• The precursor of beta‐lactamase: purification, properties and folding kinetics.

  1989cited by this paper
• Effects of sulphate and urea on the stability and reversible unfolding of beta-lactamase from Staphylococcus aureus. Implications for the folding pathway of beta-lactamase.

  1985cited by this paper
• Purification of beta-lactamases by affinity chromatography on phenylboronic acid-agarose.

  1984cited by this paper
• Partial amino acid sequence of penicillinase coded by Escherichia coli plasmid R6K.

  1978cited by this paper
• Primary structure effects on peptide group hydrogen exchange.

  1972cited by this paper

• Defining Gas-Phase Fragmentation Propensities of Intact Proteins During Native Top-Down Mass Spectrometry

  2017cites this paper
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  2013cites this paper
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  2013cites this paper
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• Mass Spectrometry on the Frontiers of Molecular Biophysics and Structural Biology: Perspectives and Challenges

  2012cites this paper
• Protein chaperones and non-protein substrates: on substrate promiscuity of GroEL

  2011cites this paper
• Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding

  2009cites this paper
• GroEL can unfold late intermediates populated on the folding pathways of monellin.

  2009cites this paper
• Chaperone Function in Vitro

  2008cites this paper
• GroEL-Mediated Protein Folding: Making the Impossible, Possible

  2006cites this paper
• Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution.

  2003cites this paper
• Chaperonin-mediated protein folding: fate of substrate polypeptide

  2003cites this paper
• Identification of the interface of a large protein-protein complex using H/D exchange and Fourier transform ion cyclotron resonance mass spectrometry.

  2002cites this paper
• GroEL Binds Artificial Proteins with Random Sequences*

  2000cites this paper
• Secondary structure forming propensity coupled with amphiphilicity is an optimal motif in a peptide or protein for association with chaperonin 60 (GroEL).

  1999cites this paper
• Chaperone-percolator model: a possible molecular mechanism of Anfinsen-cage-type chaperones.

  1999cites this paper
• Interaction with GroEL destabilises non‐amphiphilic secondary structure in a peptide

  1999cites this paper
• Disassembly of intact multiprotein complexes in the gas phase.

  1999cites this paper
• The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

  1999cites this paper
• The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins.

  1999cites this paper
• Hydrogen exchange studies of protein structure.

  1998cites this paper
• Two conformational states of beta-lactamase bound to GroEL: a biophysical characterization.

  1998cites this paper
• Hydrogen exchange and protein folding.

  1998cites this paper
• Partitioning of Rhodanese onto GroEL

  1998cites this paper
• The Hsp70 and Hsp60 chaperone machines.

  1998cites this paper
• Identification of the binding surface on beta-lactamase for GroEL by limited proteolysis and MALDI-mass spectrometry.

  1998cites this paper
• Molten globule unfolding monitored by hydrogen exchange in urea.

  1998cites this paper
• Insight into the Conformation of Protein Folding Intermediate(s) Trapped by GroEL*

  1998cites this paper
• Structural aspects of GroEL function.

  1998cites this paper
• How chaperones fold proteins.

  1998cites this paper
• Protein folding assisted by the GroEL/GroES chaperonin system.

  1998cites this paper
• Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL.

  1998cites this paper
• Conformation of Aspartate Aminotransferase Isozymes Folding under Different Conditions Probed by Limited Proteolysis*

  1998cites this paper
• The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

  1998cites this paper
• Application of electrospray mass spectrometry in biology

  1998cites this paper
• Mass spectrometry.

  1998cites this paper
• The chaperonin cycle cannot substitute for prolyl isomerase activity, but GroEL alone promotes productive folding of a cyclophilin‐sensitive substrate to a cyclophilin‐resistant form

  1997influential citation
• Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR.

  1997cites this paper
• Biochemie und Molekulargenetik 1996

  1997cites this paper
• Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.

  1997cites this paper
• How GroES Regulates Binding of Nonnative Protein to GroEL*

  1997cites this paper
• Structural and mechanistic consequences of polypeptide binding by GroEL.

  1997cites this paper
• GroEL-mediated folding of structurally homologous dihydrofolate reductases.

  1997cites this paper
• Protein folding: how the mechanism of GroEL action is defined by kinetics.

  1997cites this paper
• GroEL‐Mediated protein folding

  1997cites this paper