Published in Proc Natl Acad Sci U S A on April 11, 2011
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Using ¹⁵N-ammonium to characterise and map potassium binding sites in proteins by NMR spectroscopy. Chembiochem (2014) 0.82
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Computational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and Communication. PLoS Comput Biol (2017) 0.77
The specialized Hsp70 (HscA) interdomain linker binds to its nucleotide-binding domain and stimulates ATP hydrolysis in both cis and trans configurations. Biochemistry (2014) 0.77
Structure of GPN-Loop GTPase Npa3 and Implications for RNA Polymerase II Assembly. Mol Cell Biol (2015) 0.77
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Biochemical characterization of the interaction between HspA1A and phospholipids. Cell Stress Chaperones (2015) 0.77
Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes? Biophys J (2015) 0.77
Glutathionylation of the Bacterial Hsp70 Chaperone DnaK Provides a Link between Oxidative Stress and the Heat Shock Response. J Biol Chem (2016) 0.76
Identification of key hinge residues important for nucleotide-dependent allostery in E. coli Hsp70/DnaK. PLoS Comput Biol (2013) 0.76
Dancing through Life: Molecular Dynamics Simulations and Network-Centric Modeling of Allosteric Mechanisms in Hsp70 and Hsp110 Chaperone Proteins. PLoS One (2015) 0.76
Novel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities. Mol Cell Proteomics (2016) 0.75
Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines. Biophys Rev (2015) 0.75
Disordered Regions Flanking Ordered Domains Modulate Signaling Transduction. Biophys J (2015) 0.75
An atomistic view of Hsp70 allosteric crosstalk: from the nucleotide to the substrate binding domain and back. Sci Rep (2016) 0.75
Therapeutic Strategies for Restoring Tau Homeostasis. Cold Spring Harb Perspect Med (2017) 0.75
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The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange. Structure (2010) 1.00
NMR chemical shift data and ab initio shielding calculations: emerging tools for protein structure determination. Chem Soc Rev (2009) 1.00
Energetics of nucleotide-induced DnaK conformational states. Biochemistry (2010) 0.93
Segmental isotopic labeling of the Hsp70 molecular chaperone DnaK using expressed protein ligation. Biopolymers (2010) 0.88
Sending signals dynamically. Science (2009) 3.64
The changing landscape of protein allostery. Curr Opin Struct Biol (2006) 2.90
Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. Proc Natl Acad Sci U S A (2003) 2.43
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Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant. Proc Natl Acad Sci U S A (2006) 1.81
From the test tube to the cell: exploring the folding and aggregation of a beta-clam protein. Biopolymers (2007) 1.67
An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell (2012) 1.67
Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA. J Biol Chem (2002) 1.50
Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state. J Am Chem Soc (2010) 1.45
Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP. Mol Biol Cell (2003) 1.43
An interdomain sector mediating allostery in Hsp70 molecular chaperones. Mol Syst Biol (2010) 1.42
Extended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein. J Biol Chem (2006) 1.37
Protein folding in the cell: challenges and progress. Curr Opin Struct Biol (2010) 1.32
Aggregation of a slow-folding mutant of a beta-clam protein proceeds through a monomeric nucleus. Biochemistry (2005) 1.29
Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states. J Biol Chem (2005) 1.27
Unique physical properties and interactions of the domains of methylated DNA binding protein 2. Biochemistry (2010) 1.25
In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence. J Biol Chem (2007) 1.19
Rett syndrome-causing mutations in human MeCP2 result in diverse structural changes that impact folding and DNA interactions. J Biol Chem (2008) 1.12
Exploring weak, transient protein--protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy. Biochemistry (2011) 1.11
Sequence and structural analysis of cellular retinoic acid-binding proteins reveals a network of conserved hydrophobic interactions. Proteins (2004) 1.10
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Mapping the signal sequence-binding site on SRP reveals a significant role for the NG domain. J Biol Chem (2002) 1.07
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Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization. Nat Struct Mol Biol (2011) 1.04
Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state. Biochemistry (2004) 1.02
Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activity. J Biol Chem (2011) 0.99
The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA. J Biol Chem (2005) 0.99
FoldEco: a model for proteostasis in E. coli. Cell Rep (2012) 0.98
Evolutionary coupling of structural and functional sequence information in the intracellular lipid-binding protein family. Proteins (2006) 0.95
JBC is on a mission to facilitate scientific discovery. J Biol Chem (2017) 0.95
Role of local sequence in the folding of cellular retinoic abinding protein I: structural propensities of reverse turns. Biochemistry (2003) 0.93
Functionally significant mobile regions of Escherichia coli SecA ATPase identified by NMR. J Biol Chem (2002) 0.91
Nature's molecular sponges: small heat shock proteins grow into their chaperone roles. Proc Natl Acad Sci U S A (2010) 0.90
Electrophysiological studies in Xenopus oocytes for the opening of Escherichia coli SecA-dependent protein-conducting channels. J Membr Biol (2007) 0.89
Segmental isotopic labeling of the Hsp70 molecular chaperone DnaK using expressed protein ligation. Biopolymers (2010) 0.88
Effects of osmolytes on protein folding and aggregation in cells. Methods Enzymol (2007) 0.87
Site-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteine. Chem Biol Drug Des (2007) 0.87
Exploring the interactions between signal sequences and E. coli SRP by two distinct and complementary crosslinking methods. Biopolymers (2009) 0.87
Natural polypeptide scaffolds: beta-sheets, beta-turns, and beta-hairpins. Biopolymers (2006) 0.85
Use of synthetic signal sequences to explore the protein export machinery. Biopolymers (2008) 0.82
The Role of Aromatic-Aromatic Interactions in Strand-Strand Stabilization of β-Sheets. J Mol Biol (2013) 0.82
Orthogonal cross-seeding: an approach to explore protein aggregates in living cells. Biochemistry (2008) 0.82
First glimpses of a chaperonin-bound folding intermediate. Proc Natl Acad Sci U S A (2005) 0.82
Local sequence information in cellular retinoic acid-binding protein I: specific residue roles in beta-turns. Biopolymers (2003) 0.82
A well-defined amphipathic conformation for the calcium-free cyclic lipopeptide antibiotic, daptomycin, in aqueous solution. Biopolymers (2005) 0.82
How bacteria survive an acid trip. Proc Natl Acad Sci U S A (2013) 0.80
Disorder breathes life into a DEAD motor. Nat Struct Mol Biol (2006) 0.80
The structure of Escherichia coli signal recognition particle revealed by scanning transmission electron microscopy. Mol Biol Cell (2006) 0.79
Native structural propensity in cellular retinoic acid-binding protein I 64-88: the role of locally encoded structure in the folding of a beta-barrel protein. Biophys Chem (2003) 0.79
Using a low denaturant model to explore the conformational features of translocation-active SecA. Biochemistry (2012) 0.78
Early folding events protect aggregation-prone regions of a β-rich protein. Structure (2013) 0.78
A method for direct measurement of protein stability in vivo. Methods Mol Biol (2009) 0.77
The molecular dating game: an antibody heavy chain hangs loose with a chaperone while waiting for its life partner. Mol Cell (2009) 0.77
Chapter 3: A fluorescent window into protein folding and aggregation in cells. Methods Cell Biol (2008) 0.77
A Loyal Friend of ASBMB and JBC: Howard Schachman, 1918-2016. J Biol Chem (2016) 0.75
A new twist for an Hsp70 chaperone. Nat Struct Biol (2002) 0.75
You got to know when to hold (or unfold) 'em…. Mol Cell (2012) 0.75
Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein. Biochemistry (2013) 0.75
What Happens When You Submit a Paper to JBC? J Biol Chem (2017) 0.75
On the costs of scientific publishing. J Biol Chem (2017) 0.75
Our field is in good hands. Biopolymers (2008) 0.75
Finding the fittest fold: using the evolutionary record to design new proteins. Cell (2005) 0.75
The Journal of Biological Chemistry: 2016 Onward. J Biol Chem (2016) 0.75
The Sixth Peptide Engineering Meeting PEM6, Emory University Conference Center, Atlanta, Georgia, October 2 to 5, 2012. Biopolymers (2013) 0.75
A tribute to the career of a gentle giant of peptide science. Biopolymers (2008) 0.75
The Herbert Tabor Best Paper Awards: Celebrating young authors who contribute top content to JBC. J Biol Chem (2017) 0.75
Editorial: Passing of a gentle giant of peptide science: in memoriam, R. Bruce Merrifield. Biopolymers (2006) 0.75
What's in a Name? J Biol Chem (2016) 0.75
Celebrating the scientific legacy of Elkan R. Blout. Biopolymers (2008) 0.75