{"id":7,"date":"2013-09-10T12:21:41","date_gmt":"2013-09-10T12:21:41","guid":{"rendered":"https:\/\/sites.krieger.jhu.edu\/template-research\/?page_id=7"},"modified":"2024-09-11T10:07:09","modified_gmt":"2024-09-11T14:07:09","slug":"publications","status":"publish","type":"page","link":"https:\/\/sites.krieger.jhu.edu\/cmb\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"\n

Please let us know when you publish papers that utilized our instrumentation.<\/p>\n\n\n\n

2024<\/h2>\n\n\n\n
Barrick Lab<\/td>Unraveling paralog-specific Notch signaling through thermodynamics of ternary complex formation and transcriptional activation of chimeric receptors<\/a> <\/td><\/tr><\/tbody><\/table><\/figure>\n\n\n\n

2023<\/h2>\n\n\n\n
Lecomte Lab<\/td>Architectural digest: Thermodynamic stability and domain structure of a consensus monomeric globin<\/a><\/td><\/tr>
Kavran lab<\/td>Dimerization and autophosphorylation of the MST family of kinases are controlled by the same set of residues<\/a><\/td><\/tr>
Barrick Lab<\/td>Cooperativity of a seven-repeat array from topoisomerase V<\/a><\/td><\/tr>
Fleming Lab<\/td>FkpA enhances membrane protein folding using an extensive interaction surface<\/a><\/td><\/tr><\/tbody><\/table><\/figure>\n\n\n\n
Lecomte Lab<\/td>Architectural digest: Thermodynamic stability and domain structure of a consensus monomeric globin<\/a><\/td><\/tr>
Kavran lab<\/td>Dimerization and autophosphorylation of the MST family of kinases are controlled by the same set of residues<\/a><\/td><\/tr>
Barrick Lab<\/td>Cooperativity of a seven-repeat array from topoisomerase V<\/a><\/td><\/tr>
Fleming Lab<\/td>FkpA enhances membrane protein folding using an extensive interaction surface<\/a><\/td><\/tr><\/tbody><\/table><\/figure>\n\n\n\n

2022<\/h2>\n\n\n\n
Bowman Lab<\/td>Nucleosome recognition and DNA distortion by the Chd1 remodeler in a nucleotide-free state<\/a><\/td><\/tr>
Frueh Lab<\/td>Global protein dynamics as communication sensors in peptide synthetase domains<\/a><\/td><\/tr>
Mao Lab<\/td>\u03b1-Synuclein fibril-specific nanobody reduces prion-like \u03b1-synuclein spreading in mice<\/a><\/td><\/tr>
Huang Lab<\/td>Directed evolution of nonheme iron enzymes to access abiological radical-relay C(sp3<\/sup>)-H azidation<\/a><\/td><\/tr>
Kokkoli Lab<\/td>A localized enantioselective catalytic site on short DNA sequences and their amphiphiles<\/a><\/td><\/tr>
Kokkoli Lab<\/td>Supramolecular assembly of Single-uail ssDNA-amphiphiles through \u03c0-\u03c0 Interactions<\/a><\/td><\/tr><\/tbody><\/table><\/figure>\n\n\n\n

2021<\/h2>\n\n\n\n
Barrick Lab<\/td>Surface residues and nonadditive interactions stabilize a consensus homeodomain protein<\/a><\/td><\/tr>
Barman Lab<\/td>Molecular radiative energy shifts under strong oscillating fields<\/a><\/td><\/tr>
Barman Lab<\/td>Role of Aqueous-Phase Calcination in Synthesis of Ultra-Stable Dye-Embedded Fluorescent Nanoparticles for Cellular Probing<\/a><\/td><\/tr>
Fried Lab<\/td>Nonrefoldability is pervasive across the E. coli proteome<\/a><\/td><\/tr>
Greenberg Lab<\/td>Protein domain specific covalent inhibition of human DNA polymerase \u00df<\/a><\/td><\/tr>
Greenberg Lab<\/td>Selective inhibition of DNA polymerase \u00df by a covalent inhibitor<\/a><\/td><\/tr>
Hilser Lab<\/td>Tumor susceptibility gene 101 regulates the glucocorticoid receptor through disorder-mediated allostery<\/a><\/td><\/tr>
Hilser Lab<\/td>Conserved allosteric ensembles in disordered proteins using TROSY\/anti-TROSY R2<\/sub>-filtered spectroscopy<\/td><\/tr><\/tbody><\/table><\/figure>\n\n\n\n

2020<\/h2>\n\n\n\n
Fleming Lab<\/td>SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins<\/a><\/td><\/tr>
Cui Lab<\/td>Selective capture and recovery of monoclonal antibodies by self-assembling supramolecular polymers of high affinity for protein binding<\/a><\/td><\/tr>
Culotta Lab<\/td>Copper-Only Superoxide Dismutase Enzymes and Iron Starvation Stress in Candida Fungal Pathogens<\/a><\/td><\/tr>
Fleming Lab<\/td>Domain interactions determine the conformational ensemble of the periplasmic chaperone SurA<\/a><\/td><\/tr>
Kavran Lab<\/td>Biophysical characterization fo SARAH domain-mediated multimerization of Hippo pathway complexes in Drosophila<\/td><\/tr>
Tovar Lab<\/td>Computationally guided tuning of amino acid configuration influences the chiroptical properties of supramolecular peptide-pi-peptide nanostructures<\/a><\/td><\/tr><\/tbody><\/table><\/figure>\n\n\n\n

2019<\/h2>\n\n\n\n
Barrick Lab<\/td>A second backbone: The contribution of a buried asparagine ladder to the global and local stability of a leucine-rich repeat protein<\/a><\/td><\/tr>
Tovar Lab<\/td>Controlling supramolecular chirality in peptide-pi-peptide networks by variation of the alkyl spacer length<\/a><\/td><\/tr>
Meyers Lab<\/td>X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-D-xylulose 5-phosphate synthase reaction coordinate<\/a><\/td><\/tr>
Barrick Lab<\/td>Consensus sequence design as a general strategy to create hyperstable, biologically active proteins<\/a><\/td><\/tr>
Ha Lab<\/td>Extreme mechanical diversity of human telomeric DNA revealed by fluorescence-force spectroscopy<\/a><\/td><\/tr>
Barrick and Ha Labs<\/td>Functional instability allows access to DNA in longer transcription Activator-Like effector (TALE) arrays<\/a><\/td><\/tr>
Barrick Lab<\/td>Extreme stability in de novo-designed repeats arrays is determined by unusually stable short-range interactions<\/a><\/td><\/tr>
Tovar Lab<\/td>Torsional impacts on quaterthiophene segments confined within peptidic nanostructures<\/a><\/td><\/tr><\/tbody><\/table><\/figure>\n\n\n\n

2018<\/h2>\n\n\n\n
Garcia-Moreno Lab<\/td>Dielectric properties of a protein probed by reversal of a buried ion pair<\/a><\/td><\/tr>
Greenberg Lab<\/td>Expanded substrate scope of DNA polymerase theta and DNA polymerase beta: Lyase activity on the 5′-overhangs and clustered lesions<\/a><\/td><\/tr>
Elisseeff Lab<\/td>Cyclodextrin Modulated Type I Collagen Self-Assembly to Engineer Biomimetic Cornea Implants<\/a><\/td><\/tr>
Greenberg Lab<\/td>Mechanistic insight through irreversible inhibition:DNA polymerase theta uses a common active site for polymerase and lyase activities<\/a><\/td><\/tr>
Hilser Lab<\/td>Assessing allostery in intrinsically disordered protein with ensemble allosteric model<\/a><\/td><\/tr>
Hilser Lab<\/td>Dynamic allostery can drive cold adaptation in enzymes<\/a><\/td><\/tr>
Lecomte Lab<\/td>Lysine as a heme iron ligand: A property common to three truncated hemoglobins from Chlamydomonas reinhardtii<\/a><\/td><\/tr>
Lecomte Lab<\/td>Replacement of the distal histidine reveals a noncanonical heme binding site in a 2-on-2 hemoglobin<\/a><\/td><\/tr>
Meyers Lab<\/td>Oxidative decarboxylation of pyruvate by 1-deoxy-D-xyulose 5-phosphate synthase, a central metabolic enzyme in bacteria<\/a><\/td><\/tr><\/tbody><\/table><\/figure>\n\n\n\n

2017<\/h2>\n\n\n\n
Barrick Lab<\/td>Control of transcriptional activity by design of charge patterning in the intrinsically disordered RAM region of the Notch receptor<\/a><\/td><\/tr>
Barrick Lab<\/td>Creating a homeodomain with high stability and DNA binding affinity by sequence averaging<\/a><\/td><\/tr>
Frueh Lab<\/td>Molecular cross-talk between nonribosomal peptide synthetase carrier proteins and unstructured linker regions<\/a><\/td> <\/td><\/tr>
Hilser Lab<\/td>Structural stability of the coiled-coil domain of tumor susceptibility<\/a><\/td><\/tr>
Tovar Lab<\/td>Nonresonant and local field effects in peptidic nanostructures bearing oligo (p-phenylenevinylene) units<\/a><\/td><\/tr>
Tovar Lab<\/td>Kinetically controlled coassembly of multichromophoric peptide hydrogelators and the impacts on energy transport<\/a><\/td><\/tr><\/tbody><\/table><\/figure>\n\n\n\n

2016<\/h2>\n\n\n\n
Barrick Lab<\/td>Broken TALEs: transcription activator-like effectors populate partly folded states<\/a><\/td><\/tr>
Tovar Lab<\/td>Cross-linking approaches to tuning the mechanical properties of peptide \u03c0\u2011electrom hyrdogels<\/a><\/td><\/tr><\/tbody><\/table><\/figure>\n\n\n\n

2015<\/h2>\n\n\n\n
Barrick Lab<\/td>Effects of linker length and transient secondary structure elements in the intrinsically disordered Notch RAM region on Notch signaling<\/a><\/td><\/tr>
Barrick Lab<\/td>A naturally occurring repeat protein with high internal sequence identity defines a new class of TPR-like proteins<\/a><\/td><\/tr>
Bortvan Lab<\/td>A unique HMG-Box domain of mouse maelstrom binds structured RNA but not double stranded DNA<\/a><\/td><\/tr>
Tovar Lab<\/td>Sequence-dependent mechanical, photophysical and electrical properties of pi-conjugated peptide hydrogelators<\/a><\/td><\/tr>
Ostermeier Lab<\/td>Design of protein switches based on an ensemble model of allostery<\/a><\/td><\/tr><\/tbody><\/table><\/figure>\n\n\n\n

2014<\/h2>\n\n\n\n
Lecomte Lab<\/td>Characterization of THB1, a Chlamydomonas reinhardtii truncated hemoglobin: linkage to nitrogen metabolism and identification of lysine as the distal heme ligand<\/a><\/td><\/tr>
Stivers Lab<\/td>GTP activator and dNTP substrates of HIV-1 restriction factor and SAMHD1 generate a long-lived activated state<\/a><\/td><\/tr><\/tbody><\/table><\/figure>\n","protected":false},"excerpt":{"rendered":"

Please let us know when you publish papers that utilized our instrumentation. 2024 Barrick Lab Unraveling paralog-specific Notch signaling through thermodynamics of ternary complex formation and transcriptional activation of chimeric receptors 2023 Lecomte Lab Architectural digest: Thermodynamic stability and domain structure of a consensus monomeric globin Kavran lab Dimerization and autophosphorylation of the MST family […]<\/p>\n","protected":false},"author":40,"featured_media":0,"parent":0,"menu_order":5,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_acf_changed":false,"footnotes":""},"class_list":["post-7","page","type-page","status-publish","hentry"],"acf":[],"_links":{"self":[{"href":"https:\/\/sites.krieger.jhu.edu\/cmb\/wp-json\/wp\/v2\/pages\/7","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/sites.krieger.jhu.edu\/cmb\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/sites.krieger.jhu.edu\/cmb\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/sites.krieger.jhu.edu\/cmb\/wp-json\/wp\/v2\/users\/40"}],"replies":[{"embeddable":true,"href":"https:\/\/sites.krieger.jhu.edu\/cmb\/wp-json\/wp\/v2\/comments?post=7"}],"version-history":[{"count":5,"href":"https:\/\/sites.krieger.jhu.edu\/cmb\/wp-json\/wp\/v2\/pages\/7\/revisions"}],"predecessor-version":[{"id":386,"href":"https:\/\/sites.krieger.jhu.edu\/cmb\/wp-json\/wp\/v2\/pages\/7\/revisions\/386"}],"wp:attachment":[{"href":"https:\/\/sites.krieger.jhu.edu\/cmb\/wp-json\/wp\/v2\/media?parent=7"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}