Search Results - "Hoop, Cody L"

Structural Changes and Proapoptotic Peroxidase Activity of Cardiolipin-Bound Mitochondrial Cytochrome c by Mandal, Abhishek, Hoop, Cody L., DeLucia, Maria, Kodali, Ravindra, Kagan, Valerian E., Ahn, Jinwoo, van der Wel, Patrick C.A.

“…The cellular process of intrinsic apoptosis relies on the peroxidation of mitochondrial lipids as a critical molecular signal. Lipid peroxidation is connected…”
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PET-RAFT and SAXS: High Throughput Tools To Study Compactness and Flexibility of Single-Chain Polymer Nanoparticles by Upadhya, Rahul, Murthy, N. Sanjeeva, Hoop, Cody L, Kosuri, Shashank, Nanda, Vikas, Kohn, Joachim, Baum, Jean, Gormley, Adam J

“…From protein science, it is well understood that ordered folding and 3D structure mainly arise from balanced and noncovalent polar and nonpolar interactions,…”
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Huntingtin exon 1 fibrils feature an interdigitated β-hairpin–based polyglutamine core by Hoop, Cody L., Lin, Hsiang-Kai, Kar, Karunakar, Magyarfalvi, Gábor, Lamley, Jonathan M., Boatz, Jennifer C., Mandal, Abhishek, Lewandowski, Józef R., Wetzel, Ronald, van der Wel, Patrick C. A.

“…Polyglutamine expansion within the exon1 of huntingtin leads to protein misfolding, aggregation, and cytotoxicity in Huntington’s disease. This incurable…”
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The Aggregation-Enhancing Huntingtin N-Terminus Is Helical in Amyloid Fibrils by Sivanandam, V. N, Jayaraman, Murali, Hoop, Cody L, Kodali, Ravindra, Wetzel, Ronald, van der Wel, Patrick C. A

“…The 17-residue N-terminus (httNT) directly flanking the polyQ sequence in huntingtin (htt) N-terminal fragments plays a crucial role in initiating and…”
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Polyglutamine Amyloid Core Boundaries and Flanking Domain Dynamics in Huntingtin Fragment Fibrils Determined by Solid-State Nuclear Magnetic Resonance by Hoop, Cody L, Lin, Hsiang-Kai, Kar, Karunakar, Hou, Zhipeng, Poirier, Michelle A, Wetzel, Ronald, van der Wel, Patrick C. A

“…In Huntington’s disease, expansion of a polyglutamine (polyQ) domain in the huntingtin (htt) protein leads to misfolding and aggregation. There is much…”
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Virtual screening of ultra-large chemical libraries identifies cell-permeable small-molecule inhibitors of a "non-druggable" target, STAT3 N-terminal domain by Bonilla, Pedro Andrade, Hoop, Cody L, Stefanisko, Karen, Tarasov, Sergey G, Sinha, Sourav, Nicklaus, Marc C, Tarasova, Nadya I

“…STAT3 N-terminal domain is a promising molecular target for cancer treatment and modulation of immune responses. However, STAT3 is localized in the cytoplasm,…”
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DJ-1 Acts as a Scavenger of α-Synuclein Oligomers and Restores Monomeric Glycated α-Synuclein by Atieh, Tamr B, Roth, Jonathan, Yang, Xue, Hoop, Cody L, Baum, Jean

“…Glycation of α-synuclein (αSyn), as occurs with aging, has been linked to the progression of Parkinson's disease (PD) through the promotion of advanced…”
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Revealing Accessibility of Cryptic Protein Binding Sites within the Functional Collagen Fibril by Hoop, Cody L, Zhu, Jie, Nunes, Ana Monica, Case, David A, Baum, Jean

“…Fibrillar collagens are the most abundant proteins in the extracellular matrix. Not only do they provide structural integrity to all of the connective tissues…”
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CD36‐Binding Amphiphilic Nanoparticles for Attenuation of α‐Synuclein‐Induced Microglial Activation by Zhao, Nanxia, Francis, Nicola L., Song, Shuang, Kholodovych, Vladyslav, Calvelli, Hannah R., Hoop, Cody L., Pang, Zhiping P., Baum, Jean, Uhrich, Kathryn E., Moghe, Prabhas V.

“…Neuroinflammation is one of the hallmarks contributing to Parkinson's disease (PD) pathology, where microglial activation occurs as one of the earliest events,…”
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NMR unveils an N-terminal interaction interface on acetylated-α-synuclein monomers for recruitment to fibrils by Yang, Xue, Wang, Baifan, Hoop, Cody L., Williams, Jonathan K., Baum, Jean

“…Amyloid fibril formation of α-synuclein (αS) is associated with multiple neurodegenerative diseases, including Parkinson’s disease (PD). Growing evidence…”
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Molecular dynamics analysis of a flexible loop at the binding interface of the SARS‐CoV‐2 spike protein receptor‐binding domain by Williams, Jonathan K., Wang, Baifan, Sam, Andrew, Hoop, Cody L., Case, David A., Baum, Jean

“…Since the identification of the SARS‐CoV‐2 virus as the causative agent of the current COVID‐19 pandemic, considerable effort has been spent characterizing the…”
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Probing the effect of glycosaminoglycan depletion on integrin interactions with collagen I fibrils in the native extracellular matrix environment by Roth, Jonathan, Hoop, Cody L., Williams, Jonathan K., Hayes, Robert, Baum, Jean

“…Fibrillar collagen–integrin interactions in the extracellular matrix (ECM) regulate a multitude of cellular processes and cell signalling. Collagen I fibrils…”
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Cryptic binding sites become accessible through surface reconstruction of the type I collagen fibril by Zhu, Jie, Hoop, Cody L., Case, David A., Baum, Jean

“…Collagen fibril interactions with cells and macromolecules in the extracellular matrix drive numerous cellular functions. Binding motifs for dozens of…”
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Collagen I Weakly Interacts with the β‑Sheets of β2‑Microglobulin and Enhances Conformational Exchange To Induce Amyloid Formation by Hoop, Cody L, Zhu, Jie, Bhattacharya, Shibani, Tobita, Caitlyn A, Radford, Sheena E, Baum, Jean

“…Amyloidogenesis is significant in both protein function and pathology. Amyloid formation of folded, globular proteins is commonly initiated by partial or…”
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Extracellular matrix components modulate different stages in β2-microglobulin amyloid formation by Benseny-Cases, Núria, Karamanos, Theodoros K., Hoop, Cody L., Baum, Jean, Radford, Sheena E.

“…Amyloid deposition of WT human β2-microglobulin (WT-hβ2m) in the joints of long-term hemodialysis patients is the hallmark of dialysis-related amyloidosis. In…”
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Collagen I Weakly Interacts with the β-Sheets of β 2 -Microglobulin and Enhances Conformational Exchange To Induce Amyloid Formation by Hoop, Cody L, Zhu, Jie, Bhattacharya, Shibani, Tobita, Caitlyn A, Radford, Sheena E, Baum, Jean

“…Amyloidogenesis is significant in both protein function and pathology. Amyloid formation of folded, globular proteins is commonly initiated by partial or…”
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β-Hairpin-Mediated Nucleation of Polyglutamine Amyloid Formation by Kar, Karunakar, Hoop, Cody L., Drombosky, Kenneth W., Baker, Matthew A., Kodali, Ravindra, Arduini, Irene, van der Wel, Patrick C.A., Horne, W. Seth, Wetzel, Ronald

“…The conformational preferences of polyglutamine (polyQ) sequences are of major interest because of their central importance in the expanded CAG repeat diseases…”
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Molecular underpinnings of integrin binding to collagen-mimetic peptides containing vascular Ehlers–Danlos syndrome–associated substitutions by Hoop, Cody L., Kemraj, Allysa P., Wang, Baifan, Gahlawat, Sonal, Godesky, Madison, Zhu, Jie, Warren, Haley R., Case, David A., Shreiber, David I., Baum, Jean

“…Collagens carry out critical extracellular matrix (ECM) functions by interacting with numerous cell receptors and ECM components. Single glycine substitutions…”
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Structural Characterization of the Caveolin Scaffolding Domain in Association with Cholesterol-Rich Membranes by Hoop, Cody L, Sivanandam, V. N, Kodali, Ravindra, Srnec, Matthew N, van der Wel, Patrick C. A

“…Members of the caveolin protein family are implicated in the formation of caveolae and play important roles in a number of signaling pathways and in the…”
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Backbone Engineering within a Latent β-Hairpin Structure to Design Inhibitors of Polyglutamine Amyloid Formation by Kar, Karunakar, Baker, Matthew A., Lengyel, George A., Hoop, Cody L., Kodali, Ravindra, Byeon, In-Ja, Horne, W. Seth, van der Wel, Patrick C.A., Wetzel, Ronald

“…Candidates for the toxic molecular species in the expanded polyglutamine (polyQ) repeat diseases range from various types of aggregates to “misfolded”…”
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