Search Results - "Clare, Daniel K."

ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin by Clare, Daniel K., Vasishtan, Daven, Stagg, Scott, Quispe, Joel, Farr, George W., Topf, Maya, Horwich, Arthur L., Saibil, Helen R.

“…The chaperonin GroEL assists the folding of nascent or stress-denatured polypeptides by actions of binding and encapsulation. ATP binding initiates a series of…”
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Structure and Allostery of the Chaperonin GroEL by Saibil, Helen R., Fenton, Wayne A., Clare, Daniel K., Horwich, Arthur L.

“…Chaperonins are intricate allosteric machines formed of two back-to-back, stacked rings of subunits presenting end cavities lined with hydrophobic binding…”
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Refinement of atomic models in high resolution EM reconstructions using Flex-EM and local assessment by Joseph, Agnel Praveen, Malhotra, Sony, Burnley, Tom, Wood, Chris, Clare, Daniel K., Winn, Martyn, Topf, Maya

“…As the resolutions of Three Dimensional Electron Microscopic reconstructions of biological macromolecules are being improved, there is a need for better…”
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Atomic structure and hierarchical assembly of a cross-β amyloid fibril by Fitzpatrick, Anthony W. P., Debelouchina, Galia T., Bayro, Marvin J., Clare, Daniel K., Caporini, Marc A., Bajaj, Vikram S., Jaroniec, Christopher P., Wang, Luchun, Ladizhansky, Vladimir, Müller, Shirley A., MacPhee, Cait E., Waudby, Christopher A., Mott, Helen R., De Simone, Alfonso, Knowles, Tuomas P. J., Saibil, Helen R., Vendruscolo, Michele, Orlova, Elena V., Griffin, Robert G., Dobson, Christopher M.

“…The cross-β amyloid form of peptides and proteins represents an archetypal and widely accessible structure consisting of ordered arrays of β-sheet filaments…”
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ATP-driven molecular chaperone machines by Clare, Daniel K., Saibil, Helen R.

“…ABSTRACT This review is focused on the mechanisms by which ATP binding and hydrolysis drive chaperone machines assisting protein folding and unfolding. A…”
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Assembly intermediates of orthoreovirus captured in the cell by Sutton, Geoff, Sun, Dapeng, Fu, Xiaofeng, Kotecha, Abhay, Hecksel, Corey W., Clare, Daniel K., Zhang, Peijun, Stuart, David I., Boyce, Mark

“…Traditionally, molecular assembly pathways for viruses are inferred from high resolution structures of purified stable intermediates, low resolution images of…”
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The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants by Liu, Chang, Zhou, Daming, Nutalai, Rungtiwa, Duyvesteyn, Helen M.E., Tuekprakhon, Aekkachai, Ginn, Helen M., Dejnirattisai, Wanwisa, Supasa, Piyada, Mentzer, Alexander J., Wang, Beibei, Case, James Brett, Zhao, Yuguang, Skelly, Donal T., Chen, Rita E., Johnson, Sile Ann, Ritter, Thomas G., Mason, Chris, Malik, Tariq, Temperton, Nigel, Paterson, Neil G., Williams, Mark A., Hall, David R., Clare, Daniel K., Howe, Andrew, Goulder, Philip J.R., Fry, Elizabeth E., Diamond, Michael S., Mongkolsapaya, Juthathip, Ren, Jingshan, Stuart, David I., Screaton, Gavin R.

“…Alpha-B.1.1.7, Beta-B.1.351, Gamma-P.1, and Delta-B.1.617.2 variants of SARS-CoV-2 express multiple mutations in the spike protein (S). These may alter the…”
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CryoEM structure of the super-constricted two-start dynamin 1 filament by Liu, Jiwei, Alvarez, Frances Joan D., Clare, Daniel K., Noel, Jeffrey K., Zhang, Peijun

“…Dynamin belongs to the large GTPase superfamily, and mediates the fission of vesicles during endocytosis. Dynamin molecules are recruited to the neck of…”
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Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation by Carroni, Marta, Kummer, Eva, Oguchi, Yuki, Wendler, Petra, Clare, Daniel K, Sinning, Irmgard, Kopp, Jürgen, Mogk, Axel, Bukau, Bernd, Saibil, Helen R

“…The hexameric AAA+ chaperone ClpB reactivates aggregated proteins in cooperation with the Hsp70 system. Essential for disaggregation, the ClpB middle domain…”
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Basal foot MTOC organizes pillar MTs required for coordination of beating cilia by Clare, Daniel K., Magescas, Jérémy, Piolot, Tristan, Dumoux, Maud, Vesque, Christine, Pichard, Evelyne, Dang, Tien, Duvauchelle, Boris, Poirier, Françoise, Delacour, Delphine

“…Coordination of ciliary beating is essential to ensure mucus clearance in the airway tract. The orientation and synchronization of ciliary motion responds in…”
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Chlamydiae Assemble a Pathogen Synapse to Hijack the Host Endoplasmic Reticulum by Dumoux, Maud, Clare, Daniel K., Saibil, Helen R., Hayward, Richard D.

“…Chlamydiae are obligate intracellular bacterial pathogens that replicate within a specialized membrane‐bound compartment, termed an ‘inclusion’. The inclusion…”
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The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins by El Omari, Kamel, Li, Sai, Kotecha, Abhay, Walter, Thomas S., Bignon, Eduardo A., Harlos, Karl, Somerharju, Pentti, De Haas, Felix, Clare, Daniel K., Molin, Mika, Hurtado, Felipe, Li, Mengqiu, Grimes, Jonathan M., Bamford, Dennis H., Tischler, Nicole D., Huiskonen, Juha T., Stuart, David I., Roine, Elina

“…Lipid membrane fusion is an essential function in many biological processes. Detailed mechanisms of membrane fusion and the protein structures involved have…”
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Template-free 13-protofilament microtubule-MAP assembly visualized at 8 Å resolution by Fourniol, Franck J, Sindelar, Charles V, Amigues, Béatrice, Clare, Daniel K, Thomas, Geraint, Perderiset, Mylène, Francis, Fiona, Houdusse, Anne, Moores, Carolyn A

“…Microtubule-associated proteins (MAPs) are essential for regulating and organizing cellular microtubules (MTs). However, our mechanistic understanding of MAP…”
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Cryo-plasma FIB/SEM volume imaging of biological specimens by Dumoux, Maud, Glen, Thomas, Smith, Jake L R, Ho, Elaine M L, Perdigão, Luis M A, Pennington, Avery, Klumpe, Sven, Yee, Neville B Y, Farmer, David Andrew, Lai, Pui Y A, Bowles, William, Kelley, Ron, Plitzko, Jürgen M, Wu, Liang, Basham, Mark, Clare, Daniel K, Siebert, C Alistair, Darrow, Michele C, Naismith, James H, Grange, Michael

“…Serial focussed ion beam scanning electron microscopy (FIB/SEM) enables imaging and assessment of subcellular structures on the mesoscale (10 nm to 10 µm)…”
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Motor Mechanism for Protein Threading through Hsp104 by Wendler, Petra, Shorter, James, Snead, David, Plisson, Celia, Clare, Daniel K., Lindquist, Susan, Saibil, Helen R.

“…The protein-remodeling machine Hsp104 dissolves amorphous aggregates as well as ordered amyloid assemblies such as yeast prions. Force generation originates…”
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Approaches to Using the Chameleon: Robust, Automated, Fast-Plunge cryoEM Specimen Preparation by Levitz, Talya S, Weckener, Miriam, Fong, Ivan, Naismith, James H, Drennan, Catherine L, Brignole, Edward J, Clare, Daniel K, Darrow, Michele C

“…The specimen preparation process is a key determinant in the success of any cryo electron microscopy (cryoEM) structural study and until recently had remained…”
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Ex vivo mammalian prions are formed of paired double helical prion protein fibrils by Terry, Cassandra, Wenborn, Adam, Gros, Nathalie, Sells, Jessica, Joiner, Susan, Hosszu, Laszlo L. P., Tattum, M. Howard, Panico, Silvia, Clare, Daniel K., Collinge, John, Saibil, Helen R., Wadsworth, Jonathan D. F.

“…Mammalian prions are hypothesized to be fibrillar or amyloid forms of prion protein (PrP), but structures observed to date have not been definitively…”
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Topologies of a Substrate Protein Bound to the Chaperonin GroEL by Elad, Nadav, Farr, George W., Clare, Daniel K., Orlova, Elena V., Horwich, Arthur L., Saibil, Helen R.

“…The chaperonin GroEL assists polypeptide folding through sequential steps of binding nonnative protein in the central cavity of an open ring, via hydrophobic…”
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Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes by Saibil, Helen R, Ranson, Neil A, Clare, Daniel K, Farr, George W, Houldershaw, David, Horwich, Arthur L

“…The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form asymmetric complexes that, in the ATP-bound state, mediate productive folding in a…”
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A review of the approaches used to solve sub-100 kDa membrane proteins by cryo-electron microscopy by Harrison, Peter J., Vecerkova, Tereza, Clare, Daniel K., Quigley, Andrew

“…[Display omitted] •Most sub-100 kDa membrane proteins solved by cryo-EM are encapsulated in detergent.•DDM is the most popular detergent for small membrane…”
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