Published in J Biol Chem on April 21, 2017
On the costs of scientific publishing. J Biol Chem (2017) 0.75
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
Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. Mol Cell (2007) 2.39
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
Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones. Proc Natl Acad Sci U S A (2011) 1.55
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
Cross-strand split tetra-Cys motifs as structure sensors in a beta-sheet protein. Chem Biol (2008) 1.07
Mapping the signal sequence-binding site on SRP reveals a significant role for the NG domain. J Biol Chem (2002) 1.07
Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs. PLoS Comput Biol (2010) 1.07
Roles of beta-turns in protein folding: from peptide models to protein engineering. Biopolymers (2008) 1.06
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
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
Exploring the interactions between signal sequences and E. coli SRP by two distinct and complementary crosslinking methods. Biopolymers (2009) 0.87
Site-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteine. Chem Biol Drug Des (2007) 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
A well-defined amphipathic conformation for the calcium-free cyclic lipopeptide antibiotic, daptomycin, in aqueous solution. Biopolymers (2005) 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
Orthogonal cross-seeding: an approach to explore protein aggregates in living cells. Biochemistry (2008) 0.82
Disorder breathes life into a DEAD motor. Nat Struct Mol Biol (2006) 0.80
How bacteria survive an acid trip. Proc Natl Acad Sci U S A (2013) 0.80
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
The structure of Escherichia coli signal recognition particle revealed by scanning transmission electron microscopy. Mol Biol Cell (2006) 0.79
Early folding events protect aggregation-prone regions of a β-rich protein. Structure (2013) 0.78
Using a low denaturant model to explore the conformational features of translocation-active SecA. Biochemistry (2012) 0.78
A method for direct measurement of protein stability in vivo. Methods Mol Biol (2009) 0.77
Chapter 3: A fluorescent window into protein folding and aggregation in cells. Methods Cell Biol (2008) 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
You got to know when to hold (or unfold) 'em…. Mol Cell (2012) 0.75
A new twist for an Hsp70 chaperone. Nat Struct Biol (2002) 0.75
A Loyal Friend of ASBMB and JBC: Howard Schachman, 1918-2016. J Biol Chem (2016) 0.75
Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein. Biochemistry (2013) 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
On the costs of scientific publishing. J Biol Chem (2017) 0.75
The Journal of Biological Chemistry: 2016 Onward. J Biol Chem (2016) 0.75
Finding the fittest fold: using the evolutionary record to design new proteins. Cell (2005) 0.75
Our field is in good hands. Biopolymers (2008) 0.75
What's in a Name? J Biol Chem (2016) 0.75
What Happens When You Submit a Paper to JBC? J Biol Chem (2017) 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
Celebrating the scientific legacy of Elkan R. Blout. Biopolymers (2008) 0.75