A5078952328- Protein Structure and Dynamics
- Enzyme Structure and Function
- Force Microscopy Techniques and Applications
- Hippo pathway signaling and YAP/TAZ
- Cellular Mechanics and Interactions
- RNA and protein synthesis mechanisms
- Heat shock proteins research
- Cell Adhesion Molecules Research
- Quantum, superfluid, helium dynamics
- Ion Transport and Channel Regulation
- Cellular transport and secretion
- Protein Kinase Regulation and GTPase Signaling
- Toxin Mechanisms and Immunotoxins
- Proteoglycans and glycosaminoglycans research
- Axon Guidance and Neuronal Signaling
- ATP Synthase and ATPases Research
- Metallurgical Processes and Thermodynamics
- Signaling Pathways in Disease
- Cystic Fibrosis Research Advances
- Coagulation, Bradykinin, Polyphosphates, and Angioedema
- Advanced NMR Techniques and Applications
- Nuclear Physics and Applications
- Proteins in Food Systems
- Erythrocyte Function and Pathophysiology
- Glycosylation and Glycoproteins Research
Beijing Normal University
2025
City University of New York
2015-2024
City College of New York
2013-2024
The Graduate Center, CUNY
2014-2024
Fox Chase Cancer Center
2004-2009
Forschungszentrum Jülich
2005
New York University
2005
University of Connecticut
2003
National Institute of Standards and Technology
2000-2003
NIST Center for Neutron Research
2000-2001
We report experimental data on the mechanical stability of silica mesoporous material MCM-41. Using X-ray diffraction and nitrogen adsorption we show that ordered structure MCM-41 can be affected considerably by compression at pressures as low 86 MPa essentially destroyed 224 MPa.
Long-range conformational changes in proteins are ubiquitous biology for the transmission and amplification of signals; such can be triggered by small-amplitude, nanosecond protein domain motion. Understanding how initiated requires characterization motion on these timescales length scales comparable to dimensions. Using neutron spin-echo spectroscopy (NSE), normal mode analysis, a statistical-mechanical framework, we reveal overdamped, coupled within DNA polymerase I from Thermus aquaticus...
Recombination-activating gene 1 (RAG1), as well asRAG2, are the only lymphoid-specific genes required for V(D)J recombination. RAG1 protein contains a C3HC4zinc-binding motif (zinc ring finger) that binds two zinc ions. We have found additional zinc-binding motifs in form of separate C2H2zinc finger sequences. One fingers, combination with C3HC4subdomain, forms highly specific dimerization domain. A biophysical techniques has been used to determine energetics association, overall shape...
Na(+)/H(+) exchanger regulatory factor (NHERF) is an adapter protein that responsible for organizing a number of cell receptors and channels. NHERF contains two amino-terminal PDZ (postsynaptic density 95/disk-large/zonula occluden-1) domains bind to the cytoplasmic membrane channels or receptors. The carboxyl terminus interacts with FERM domain (a shared by 4.1, ezrin, radixin, moesin) family actin-binding proteins, ezrin-radixin-moesin. was shown previously be capable enhancing channel...
An emerging theme in cell signaling is that membrane-bound channels and receptors are organized into supramolecular complexes for optimum function cross-talk. In this study, we determined how protein kinase C (PKC) phosphorylation influences the scaffolding Na(+)/H(+) exchanger regulatory factor 1 (NHERF) to assemble of cystic fibrosis transmembrane conductance regulator (CFTR), a chloride ion channel controls fluid electrolyte transport across membranes. NHERF directs polarized expression...
The mammalian Na(+)/H(+) exchange regulatory factor 1 (NHERF1) is a multidomain scaffolding protein essential for regulating the intracellular trafficking and macromolecular assembly of transmembrane ion channels receptors. NHERF1 consists tandem PDZ-1, PDZ-2 domains that interact with cytoplasmic membrane proteins C-terminal (CT) domain binds membrane-cytoskeleton linker ezrin. held in an autoinhibited state through intramolecular interactions between PDZ2 CT also includes PDZ-binding motif...
Ezrin is a member of the ezrin-radixin-moesin family (ERM) adapter proteins that are localized at interface between cell membrane and cortical actin cytoskeleton, they regulate variety cellular functions. The structure representing dormant closed conformation an ERM protein has previously been determined by x-ray crystallography. Here, using contrast variation small angle neutron scattering, we reveal structural changes full-length ezrin upon binding to signaling lipid phosphatidylinositol...
Significance Adherens junctions are specialized cell–cell adhesion complexes found in epithelial, endothelial, and neuronal tissues of multicellular organism. The cadherin–catenin complex is the core component adherens junction transmits mechanical stress from cell to cell. This study reveals that displays a wide spectrum flexible structures, which suggests dynamic mechanism for this mechanotransduction adhesion.
The L2 Motivational Self System (L2MSS) determines an individual's motivation in second language learning and influences the experience intended effort. Although physical activity (PA) has been shown to enhance academic efficacy, role of PA whether it promotes efficacy not elucidated. Therefore, present study examined as a mediator explored its ameliorative effects L2MSS. A total 981 international students from different countries were selected 8 universities Beijing research subjects...
The cell adhesion molecule CD44 regulates diverse cellular functions, including cell-cell and cell-matrix interaction, motility, migration, differentiation, growth. In cells, co-localizes with the membrane-cytoskeleton adapter protein Ezrin that links assembled receptor signaling complexes to cytoskeletal actin network, which organizes spatial temporal localization of events. Here we report cytoplasmic tail (CD44ct) is largely disordered. Upon binding lipid phosphatidylinositol...
The amyloid plaque, consisting of beta-peptide (Abeta) fibrils surrounded by dystrophic neurites, is an invariable feature Alzheimer's disease. determination the molecular structure Abeta a significant goal that may lead to structure-based design effective therapeutics for Technical challenges have thus far rendered this impossible. In present study, we develop alternative methodology. Rather than determining directly, conformationally constrained peptides and demonstrate only certain...
We report that the abundant nucleolar protein nucleolin accelerates nucleic acid annealing. Nucleolin annealing of complementary oligonucleotides and contain a limited number mismatches. The activity can be localized to C-terminal region consisting two RNA binding domains (RBD3 RBD4) RGG9 domain (RBD3-RBD4-RGG9). This same mediates self-association nucleolin. nucleolin, believed mediate interactions between several ribosomal proteins, is neither sufficient for self-association, as determined...
Abstract Significantly different m values (1.9–2.7 kcal mol −1 M ) were observed for point mutations at a single, solvent‐exposed site (T53) in variant of the B1 domain streptococcal Protein G using guanidine hydrochloride (GuHCl) as denaturant. This report focuses on elucidating energetic and structural implications these m‐value differences two mutants, containing Ala Thr position 53. These proteins are representative high (m+) low (m − mutants studied. Differential scanning calorimetry...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSelf-Diffusion of Rodlike Polymers in Isotropic SolutionsZimei Bu, Paul S. Russo, Debbie L. Tipton, and Ioan I. NegulescuCite this: Macromolecules 1994, 27, 23, 6871–6882Publication Date (Print):November 1, 1994Publication History Published online1 May 2002Published inissue 1 November 1994https://doi.org/10.1021/ma00101a027RIGHTS & PERMISSIONSArticle Views296Altmetric-Citations41LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum...