Search Results - "Kreitler, Dale F"

The structural basis of N-acyl-α-amino-β-lactone formation catalyzed by a nonribosomal peptide synthetase by Kreitler, Dale F., Gemmell, Erin M., Schaffer, Jason E., Wencewicz, Timothy A., Gulick, Andrew M.

“…Nonribosomal peptide synthetases produce diverse natural products using a multidomain architecture where the growing peptide, attached to an integrated carrier…”
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Targeting diverse protein–protein interaction interfaces with α/β-peptides derived from the Z-domain scaffold by Checco, James W., Kreitler, Dale F., Thomas, Nicole C., Belair, David G., Rettko, Nicholas J., Murphy, William L., Forest, Katrina T., Gellman, Samuel H.

“…Significance Medium-sized peptides that bind tightly to a specific partner protein can be biomedically useful. However, conventional peptides, comprised…”
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Hepatitis C virus NS3/4A inhibitors and other drug-like compounds as covalent binders of SARS-CoV-2 main protease by Andi, Babak, Kumaran, Desigan, Kreitler, Dale F., Soares, Alexei S., Keereetaweep, Jantana, Jakoncic, Jean, Lazo, Edwin O., Shi, Wuxian, Fuchs, Martin R., Sweet, Robert M., Shanklin, John, Adams, Paul D., Schmidt, Jurgen G., Head, Martha S., McSweeney, Sean

“…Severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2), which causes coronavirus disease 2019 (COVID-19), threatens global public health. The world needs…”
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A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria by Grosjean, Nicolas, Yee, Estella F., Kumaran, Desigan, Chopra, Kriti, Abernathy, Macon, Biswas, Sandeep, Byrnes, James, Kreitler, Dale F., Cheng, Jan-Fang, Ghosh, Agnidipta, Almo, Steven C., Iwai, Masakazu, Niyogi, Krishna K., Pakrasi, Himadri B., Sarangi, Ritimukta, van Dam, Hubertus, Yang, Lin, Blaby, Ian K., Blaby-Haas, Crysten E.

“…Heme has a critical role in the chemical framework of the cell as an essential protein cofactor and signaling molecule that controls diverse processes and…”
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A simple technique to classify diffraction data from dynamic proteins according to individual polymorphs by Nguyen, Thu, Phan, Kim L., Kozakov, Dima, Gabelli, Sandra B., Kreitler, Dale F., Andrews, Lawrence C., Jakoncic, Jean, Sweet, Robert M., Soares, Alexei S., Bernstein, Herbert J.

“…One often observes small but measurable differences in the diffraction data measured from different crystals of a single protein. These differences might…”
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AMX – the highly automated macromolecular crystallography (17‐ID‐1) beamline at the NSLS‐II by Schneider, Dieter K., Soares, Alexei S., Lazo, Edwin O., Kreitler, Dale F., Qian, Kun, Fuchs, Martin R., Bhogadi, Dileep K., Antonelli, Steve, Myers, Stuart S., Martins, Bruno S., Skinner, John M., Aishima, Jun, Bernstein, Herbert J., Langdon, Thomas, Lara, John, Petkus, Robert, Cowan, Matt, Flaks, Leonid, Smith, Thomas, Shea-McCarthy, Grace, Idir, Mourad, Huang, Lei, Chubar, Oleg, Sweet, Robert M., Berman, Lonny E., McSweeney, Sean, Jakoncic, Jean

“…The highly automated macromolecular crystallography beamline AMX/17‐ID‐1 is an undulator‐based high‐intensity (>5 × 1012 photons s−1), micro‐focus (7 µm × 5…”
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High-resolution structures of a heterochiral coiled coil by Mortenson, David E., Steinkruger, Jay D., Kreitler, Dale F., Perroni, Dominic V., Sorenson, Gregory P., Huang, Lijun, Mittal, Ritesh, Yun, Hyun Gi, Travis, Benjamin R., Mahanthappa, Mahesh K., Forest, Katrina T., Gellman, Samuel H.

“…Interactions between polypeptide chains containing amino acid residues with opposite absolute configurations have long been a source of interest and…”
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Biosynthesis, Mechanism of Action, and Inhibition of the Enterotoxin Tilimycin Produced by the Opportunistic Pathogen Klebsiella oxytoca by Alexander, Evan M, Kreitler, Dale F, Guidolin, Valeria, Hurben, Alexander K, Drake, Eric, Villalta, Peter W, Balbo, Silvia, Gulick, Andrew M, Aldrich, Courtney C

“…Tilimycin is an enterotoxin produced by the opportunistic pathogen Klebsiella oxytoca that causes antibiotic-associated hemorrhagic colitis (AAHC). This…”
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Activation of CBASS Cap5 endonuclease immune effector by cyclic nucleotides by Rechkoblit, Olga, Sciaky, Daniela, Kreitler, Dale F., Buku, Angeliki, Kottur, Jithesh, Aggarwal, Aneel K.

“…The bacterial cyclic oligonucleotide-based antiphage signaling system (CBASS) is similar to the cGAS–STING system in humans, containing an enzyme that…”
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Harnessing Aromatic‐Histidine Interactions through Synergistic Backbone Extension and Side Chain Modification by Yu, Zhen, Kreitler, Dale F., Chiu, Yin Ting T., Xu, Ruiwen, Bruchs, Austin T., Bingman, Craig A., Gellman, Samuel H.

“…Peptide engineering efforts have delivered drugs for diverse human diseases. Side chain alteration is among the most common approaches to designing new…”
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Dual Inhibition of Human Parainfluenza Type 3 and Respiratory Syncytial Virus Infectivity with a Single Agent by Outlaw, Victor K, Bottom-Tanzer, Samantha, Kreitler, Dale F, Gellman, Samuel H, Porotto, Matteo, Moscona, Anne

“…Human parainfluenza virus 3 (HPIV3) and respiratory syncytial virus (RSV) cause lower respiratory infection in infants and young children. There are no…”
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The Nitro Group as a Masked Electrophile in Covalent Enzyme Inhibition by Ray, Sneha, Kreitler, Dale F, Gulick, Andrew M, Murkin, Andrew S

“…We report the unprecedented reaction between a nitroalkane and an active-site cysteine residue to yield a thiohydroximate adduct. Structural and kinetic…”
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Effects of Single α‑to‑β Residue Replacements on Structure and Stability in a Small Protein: Insights from Quasiracemic Crystallization by Kreitler, Dale F, Mortenson, David E, Forest, Katrina T, Gellman, Samuel H

“…Synthetic peptides that contain backbone modifications but nevertheless adopt folded structures similar to those of natural polypeptides are of fundamental…”
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Retention of Native Quaternary Structure in Racemic Melittin Crystals by Kurgan, Kathleen W, Kleman, Adam F, Bingman, Craig A, Kreitler, Dale F, Weisblum, Bernard, Forest, Katrina T, Gellman, Samuel H

“…Racemic crystallography has been used to elucidate the secondary and tertiary structures of peptides and small proteins that are recalcitrant to conventional…”
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Use of a Stereochemical Strategy To Probe the Mechanism of Phenol-Soluble Modulin α3 Toxicity by Yao, Zhihui, Cary, Brian P, Bingman, Craig A, Wang, Chenxuan, Kreitler, Dale F, Satyshur, Kenneth A, Forest, Katrina T, Gellman, Samuel H

“…Phenol-soluble modulin α3 (PSMα3) is a cytotoxic peptide secreted by virulent strains of Staphylococcus aureus. We used a stereochemical strategy to examine…”
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Engineering Protease-Resistant Peptides to Inhibit Human Parainfluenza Viral Respiratory Infection by Outlaw, Victor K, Cheloha, Ross W, Jurgens, Eric M, Bovier, Francesca T, Zhu, Yun, Kreitler, Dale F, Harder, Olivia, Niewiesk, Stefan, Porotto, Matteo, Gellman, Samuel H, Moscona, Anne

“…The lower respiratory tract infections affecting children worldwide are in large part caused by the parainfluenza viruses (HPIVs), particularly HPIV3, along…”
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Structural Characterization of Disulfide-Linked p53-Derived Peptide Dimers by DiGiorno, Magdalena C., Vithanage, Nisansala, Victorio, Clara G., Kreitler, Dale F., Outlaw, Victor K., Sawyer, Nicholas

“…Purpose of Review Disulfide bonds provide a convenient method for chemoselective alteration of peptide and protein structure and function. We previously…”
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EstG is a novel esterase required for cell envelope integrity in Caulobacter by Daitch, Allison K., Orsburn, Benjamin C., Chen, Zan, Alvarez, Laura, Eberhard, Colten D., Sundararajan, Kousik, Zeinert, Rilee, Kreitler, Dale F., Jakoncic, Jean, Chien, Peter, Cava, Felipe, Gabelli, Sandra B., Goley, Erin D.

“…Proper regulation of the bacterial cell envelope is critical for cell survival. Identification and characterization of enzymes that maintain cell envelope…”
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A Hendecad Motif Is Preferred for Heterochiral Coiled-Coil Formation by Kreitler, Dale F, Yao, Zhihui, Steinkruger, Jay D, Mortenson, David E, Huang, Lijun, Mittal, Ritesh, Travis, Benjamin R, Forest, Katrina T, Gellman, Samuel H

“…The structural principles that govern interactions between l- and d-peptides are not well understood. Among natural proteins, coiled-coil assemblies formed…”
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Evaluation of β‐Amino Acid Replacements in Protein Loops: Effects on Conformational Stability and Structure by Mortenson, David E., Kreitler, Dale F., Thomas, Nicole C., Guzei, Ilia A., Gellman, Samuel H., Forest, Katrina T.

“…β‐Amino acids have a backbone that is expanded by one carbon atom relative to α‐amino acids, and β residues have been investigated as subunits in protein‐like…”
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