Search results for: Jean Baum

Items from 1 to 20 out of 46 results

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Probing the effect of glycosaminoglycan depletion on integrin interactions with collagen I fibrils in the native extracellular matrix environment

Jonathan Roth, Cody L. Hoop, Jonathan K. Williams, Robert Hayes, more

Fibrillar collagen–integrin interactions in the extracellular matrix (ECM) regulate a multitude of cellular processes and cell signalling. Collagen I fibrils serve as the molecular scaffolding for connective tissues throughout the human body and are the most abundant protein building blocks in the ECM. The ECM environment is diverse, made up of several ECM proteins, enzymes, and proteoglycans. In...

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Evolution of the SARS‐CoV‐2 proteome in three dimensions (3D) during the first 6 months of the COVID‐19 pandemic

Joseph H. Lubin, Christine Zardecki, Elliott M. Dolan, Changpeng Lu, more

Proteins: Structure, Function, and Bioinformatics > 90 > 5 > 1054 - 1080

Understanding the molecular evolution of the SARS‐CoV‐2 virus as it continues to spread in communities around the globe is important for mitigation and future pandemic preparedness. Three‐dimensional structures of SARS‐CoV‐2 proteins and those of other coronavirusess archived in the Protein Data Bank were used to analyze viral proteome evolution during the first 6 months of the COVID‐19 pandemic....

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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

Jonathan K. Williams, Baifan Wang, Andrew Sam, Cody L. Hoop, more

Proteins: Structure, Function, and Bioinformatics > 90 > 5 > 1044 - 1053

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 interaction between the Spike protein receptor‐binding domain (RBD) and the human angiotensin converting enzyme 2 (ACE2) receptor. This has provided a detailed picture of the end point structure of the RBD‐ACE2 binding event, but what remains...

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Interactions between the Intrinsically Disordered Proteins β‐Synuclein and α‐Synuclein

Jonathan K. Williams, Xue Yang, Jean Baum

PROTEOMICS > 18 > 21-22 > n/a - n/a

Several intrinsically disordered proteins have been implicated in the process of amyloid fibril formation in neurodegenerative disease, and developing approaches to inhibit the aggregation of these intrinsically disordered proteins is critical for establishing effective therapies against disease progression. The aggregation pathway of the intrinsically disordered protein alpha‐synuclein, which is...

article

Magnesium Activates Microsecond Dynamics to Regulate Integrin-Collagen Recognition

Ana Monica Nunes, Conceição A.S.A. Minetti, David P. Remeta, Jean Baum

Structure > 2018 > 26 > 8 > 1080-1090.e5

Integrin receptors bind collagen via metal-mediated interactions that are modulated by magnesium (Mg²⁺) levels in the extracellular matrix. Nuclear magnetic resonance-based relaxation experiments, isothermal titration calorimetry, and adhesion assays reveal that Mg²⁺ functions as both a structural anchor and dynamic switch of the α₁β₁ integrin I domain (α₁I). Specifically, Mg²⁺ binding activates micro-...

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Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein

Jonathan K. Williams, Xue Yang, Tamr B. Atieh, Michael P. Olson, more

Journal of Molecular Biology > 2018 > 430 > 16 > 2360-2371

The intrinsically disordered protein β-synuclein is known to inhibit the aggregation of its intrinsically disordered homolog, α-synuclein, which is implicated in Parkinson's disease. While β-synuclein itself does not form fibrils at the cytoplasmic pH 7.4, alteration of pH and other environmental perturbations are known to induce its fibrilization. However, the sequence and structural determinants...

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Protein Aggregation

Jean Baum, Daniel Raleigh

Protein Science > 27 > 7 > 1149 - 1150

article

Polymer brain-nanotherapeutics for multipronged inhibition of microglial α-synuclein aggregation, activation, and neurotoxicity

Neal K. Bennett, Rebecca Chmielowski, Dalia S. Abdelhamid, Jonathan J. Faig, more

Biomaterials > 2016 > 111 > C > 179-189

Neuroinflammation, a common neuropathologic feature of neurodegenerative disorders including Parkinson disease (PD), is frequently exacerbated by microglial activation. The extracellular protein α-synuclein (ASYN), whose aggregation is characteristic of PD, remains a key therapeutic target, but the control of synuclein trafficking and aggregation within microglia has been challenging. First, we established...

article

Intrinsic local destabilization of the C‐terminus predisposes integrin α1 I domain to a conformational switch induced by collagen binding

Ana Monica Nunes, Jie Zhu, Jacqueline Jezioro, Conceição A.S.A. Minetti, more

Protein Science > 25 > 9 > 1672 - 1681

Integrin–collagen interactions play a critical role in a myriad of cellular functions that include immune response, and cell development and differentiation, yet their mechanism of binding is poorly understood. There is increasing evidence that conformational flexibility assumes a central role in the molecular mechanisms of protein–protein interactions and here we employ NMR hydrogen–deuterium exchange...

article

The loss of inhibitory C‐terminal conformations in disease associated P123H β‐synuclein

Maria K. Janowska, Jean Baum

Protein Science > 25 > 1 > 286 - 294

β‐synuclein (βS) is a homologue of α‐synuclein (αS), the major protein component of Lewy bodies in patients with Parkinson's disease. In contrast to αS, βS does not form fibrils, mitigates αS toxicity in vivo and inhibits αS fibril formation in vitro. Previously a missense mutation of βS, P123H, was identified in patients with Dementia with Lewy Body disease. The single P123H mutation at the C‐terminus...

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Local amino acid sequence patterns dominate the heterogeneous phenotype for the collagen connective tissue disease Osteogenesis Imperfecta resulting from Gly mutations

Jianxi Xiao, Zhangfu Yang, Xiuxia Sun, Rayna Addabbo, more

Journal of Structural Biology > 2015 > 192 > 1 > 127-137

Osteogenesis Imperfecta (OI), a hereditary connective tissue disease in collagen that arises from a single Gly→X mutation in the collagen chain, varies widely in phenotype from perinatal lethal to mild. It is unclear why there is such a large variation in the severity of the disease considering the repeating (Gly-X-Y)n sequence and the uniform rod-like structure of collagen. We systematically evaluate...

article

Accessible Conformations of N-Terminal Acetylated Alpha-Synuclein: Implications for Fibril Formation

Jean Baum

Biophysical Journal > 2014 > 106 > 2 Supplement 1 > 5a

article

Proteins special issue of biopolymers

Alfred Wittinghofer, Jean Baum Martin, Stephen Blacklow

Biopolymers > 99 > 11 > 807 - 808

article

Exploring the accessible conformations of N-terminal acetylated α-synuclein

Gina M. Moriarty, Maria K. Janowska, Lijuan Kang, Jean Baum

FEBS Letters > 2013 > 587 > 8 > 1128-1138

Alpha synuclein (αsyn) fibrils are found in the Lewy Bodies of patients with Parkinson’s disease (PD). The aggregation of the αsyn monomer to soluble oligomers and insoluble fibril aggregates is believed to be one of the causes of PD. Recently, the view of the native state of αsyn as a monomeric ensemble was challenged by a report suggesting that αsyn exists in its native state as a helical tetramer...

article

Fast hydrogen exchange affects ¹⁵N relaxation measurements in intrinsically disordered proteins

Seho Kim, Kuen-Phon Wu, Jean Baum

Journal of Biomolecular NMR > 2013 > 55 > 3 > 249-256

Unprotected amide protons can undergo fast hydrogen exchange (HX) with protons from the solvent. Generally, NMR experiments using the out-and-back coherence transfer with amide proton detection are affected by fast HX and result in reduced signal intensity. When one of these experiments, ¹H–¹⁵N HSQC, is used to measure the ¹⁵N transverse relaxation rate (R₂), the measured R₂ rate is convoluted with...

article

A peptide study of the relationship between the collagen triple‐helix and amyloid

Avanish S. Parmar, Ana Monica Nunes, Jean Baum, Barbara Brodsky

Biopolymers > 97 > 10 > 795 - 806

Type XXV collagen, or collagen‐like amyloidogenic component, is a component of amyloid plaques, and recent studies suggest this collagen affects amyloid fibril elongation and has a genetic association with Alzheimer's disease. The relationship between the collagen triple helix and amyloid fibrils was investigated by studying peptide models, including a very stable triple helical peptide (Pro‐Hyp‐Gly)...

article

Osteogenesis Imperfecta Missense Mutations in Collagen: Structural Consequences of a Glycine to Alanine Replacement at a Highly Charged Site

Jianxi Xiao, Haiming Cheng, Teresita Silva, Jean Baum, more

Biochemistry > 2011 > 50 > 50 > 10771 - 10780

article

The A53T Mutation is Key in Defining the Differences in the Aggregation Kinetics of Human and Mouse α-Synuclein

Lijuan Kang, Kuen-Phon Wu, Michele Vendruscolo, Jean Baum

Journal of the American Chemical Society > 2011 > 133 > 34 > 13465 - 13470

article

Osteogenesis Imperfecta Model Peptides: Incorporation of Residues Replacing Gly within a Triple Helix Achieved by Renucleation and Local Flexibility

Jianxi Xiao, Balaraman Madhan, Yingjie Li, Barbara Brodsky, more

Biophysical Journal > 2011 > 101 > 2 > 449-458

Missense mutations, which replace one Gly with a larger residue in the repeating sequence of the type I collagen triple helix, lead to the hereditary bone disorder osteogenesis imperfecta (OI). Previous studies suggest that these mutations may interfere with triple-helix folding. NMR was used to investigate triple-helix formation in a series of model peptides where the residue replacing Gly, as well...

article

Transient Protein-Protein Interactions in the IDP Alpha-Synuclein Detected by NMR: Implications for Protein Aggregation

Kuen-Phon Wu, Jean Baum

Biophysical Journal > 2011 > 100 > 3 Supplement 1 > 519a

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INFONA - science communication portal

Search results for: Jean Baum

Probing the effect of glycosaminoglycan depletion on integrin interactions with collagen I fibrils in the native extracellular matrix environment

Evolution of the SARS‐CoV‐2 proteome in three dimensions (3D) during the first 6 months of the COVID‐19 pandemic

Molecular dynamics analysis of a flexible loop at the binding interface of the SARS‐CoV‐2 spike protein receptor‐binding domain

Interactions between the Intrinsically Disordered Proteins β‐Synuclein and α‐Synuclein

Magnesium Activates Microsecond Dynamics to Regulate Integrin-Collagen Recognition

Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein

Protein Aggregation

Polymer brain-nanotherapeutics for multipronged inhibition of microglial α-synuclein aggregation, activation, and neurotoxicity

Intrinsic local destabilization of the C‐terminus predisposes integrin α1 I domain to a conformational switch induced by collagen binding

The loss of inhibitory C‐terminal conformations in disease associated P123H β‐synuclein

Local amino acid sequence patterns dominate the heterogeneous phenotype for the collagen connective tissue disease Osteogenesis Imperfecta resulting from Gly mutations

Accessible Conformations of N-Terminal Acetylated Alpha-Synuclein: Implications for Fibril Formation

Proteins special issue of biopolymers

Exploring the accessible conformations of N-terminal acetylated α-synuclein

Fast hydrogen exchange affects ¹⁵N relaxation measurements in intrinsically disordered proteins

A peptide study of the relationship between the collagen triple‐helix and amyloid

Osteogenesis Imperfecta Missense Mutations in Collagen: Structural Consequences of a Glycine to Alanine Replacement at a Highly Charged Site

The A53T Mutation is Key in Defining the Differences in the Aggregation Kinetics of Human and Mouse α-Synuclein

Osteogenesis Imperfecta Model Peptides: Incorporation of Residues Replacing Gly within a Triple Helix Achieved by Renucleation and Local Flexibility

Transient Protein-Protein Interactions in the IDP Alpha-Synuclein Detected by NMR: Implications for Protein Aggregation

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