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Biomedical subjects

Weijie Wang

Publications and source records attributed to Weijie Wang.

17 recordsLinked to original sources
PubMed2026

Association between youth athletes' sports specialization and injuries: a systematic review and meta-analysis.

INTRODUCTION: The purpose of this study was to conduct a systematic review and meta-analysis to examine the specialization-injury relationship, and explore whether the specialization-injury relationship is moderated by study design, sport type, age, sex, and injury measurement type, injury mechanism, and anatomical location. METHODS: We searched eight databases by related keywords and assessed the quality of the included studies using the JBI Critical Appraisal Checklist for Analytical Cross-Sectional Studies and the Newcastle-Ottawa Scale. The Comprehensive Meta-Analysis (CMA) statistical software 3.7 examined heterogeneity, sensitivity, publication bias, overall effect size of specialization-injury relationship, and moderation effects. This review was prospectively registered in PROSPERO (CRD420251233318). Searches were conducted in eight electronic databases from inception to March, 2026. RESULTS: The 15 included studies showed moderate heterogeneity, stable sensitivity analyses, and no publication bias. The overall odds ratio of the sports specialization-injury relationship was 2.00 (95% confidence interval [1.58-2.55], p&#xa0;<&#xa0;.001). Moderation analyses indicated that sport type significantly influenced the specialization-injury relationship, whereas no significant moderation effects were observed for study design, sex, age, injury measurement type, injury mechanism, and injury anatomical location. CONCLUSIONS: The findings indicate a positive association between sport specialization and injury risk among youth athletes, with variation across sport participation contexts. Specifically, athletes in both contact and non-contact sports demonstrated higher pooled odds of injury than those involved in multiple sports. Although the evidence is heterogeneous and should be interpreted with caution, these findings highlight the potential role of diversified sport participation in relation to injury.

Humans↗
PubMed2026

Disentangling the association between chronic pain and sarcopenia-related traits: A bidirectional Mendelian randomization study.

ObjectiveThis study aimed to investigate the potential causal relationships between chronic pain and three key sarcopenia-related quantitative traits: (a) hand grip strength; (b) usual walking pace; and (c) appendicular lean mass, using bidirectional two-sample Mendelian randomization.MethodsWe conducted bidirectional two-sample Mendelian randomization using summary-level data from large-scale genome-wide association studies to assess the genetically predicted associations between chronic pain, including multisite chronic pain and chronic widespread musculoskeletal pain, and the aforementioned sarcopenia-related traits.ResultsMendelian randomization revealed that multisite chronic pain was significantly associated with an increased risk of low hand grip strength (odds ratio = 1.70; p&#x2009;<&#x2009;0.001) and decreased usual walking pace (odds ratio = 0.81; p&#x2009;<&#x2009;0.001); chronic widespread musculoskeletal pain was also significantly associated with decreased usual walking pace (odds ratio = 0.15; p&#x2009;<&#x2009;0.001). Additionally, higher left hand grip strength was significantly associated with a lower risk of multisite chronic pain (odds ratio = 0.90; p<&#x2009;0.001) and chronic widespread musculoskeletal pain (odds ratio = 0.99; p&#x2009;=&#x2009;0.002); higher right hand grip strength was significantly associated with a lower risk of multisite chronic pain (odds ratio = 0.91; p&#x2009;=&#x2009;0.002); and higher usual walking pace was significantly associated with a lower risk of multisite chronic pain (odds ratio = 0.49; p&#x2009;<&#x2009;0.001) and chronic widespread musculoskeletal pain (odds ratio = 0.92; p&#x2009;<&#x2009;0.001). No significant causal associations were detected for appendicular lean mass in either direction (all p&#x2009;>&#x2009;0.05).ConclusionThis study provides genetic evidence supporting potential causal links between chronic pain and key phenotypic components of sarcopenia.

Humans↗
PubMed2006

Cloning and characterization of 40S ribosomal protein S4 gene from Culex pipiens pallens.

The 40S ribosomal protein S4 gene (RPS4) has been cloned from Culex pipiens pallens. An open reading frame (ORF) of 789 bp was found to encode a putative 262 amino acid protein. The deduced amino acid sequence shares 96% and 91% identity with RPS4 genes from Aedes and Anopheles respectively. Transcript expression of RPS4 was determined by real-time PCR in all life stages of deltamethrin-susceptible and -resistant strains. The results demonstrated that this gene is expressed at all developmental stages. Meanwhile, in pupae and adults, RPS4 is overexpressed in deltamethrin-resistant strain than in -susceptible strain. Our data for the first time suggests that increased expression of the RPS4 gene may play some role in the development of deltamethrin resistance in C. pipiens pallens.

Amino Acid Sequence↗
PubMed2006

Cloning and overexpression of ribosomal protein L39 gene from deltamethrin-resistant Culex pipiens pallens.

The complete sequence of ribosomal protein L39 has been cloned from deltamethrin-resistant strain of Culex pipiens pallens (DR1 strain). Quantitative RT-PCR analysis indicated that the RPL39 transcription level was 23.4 times higher in DR1 strain than in susceptible strain at 4th instar larvae. The RPL39 expression was also found to be consistently higher throughout the life cycle of DR1 strain. A protein of predicted size 17 kDa has been detected by Western blotting in RPL39-transfected mosquito C6/36 cells. These RPL39-transfected cells also showed enhanced deltamethrin resistance compared to plasmid vector-transfected cells as determined by methyl tritiated thymidine ((3)H-TdR) incorporation. These results indicate that RPL39 is expressed at higher levels in DR1 strain, and may confer some insecticide resistance in Cx. pipiens pallens.

Actins↗
PubMed2006

Method for distinguishing specific from nonspecific protein-ligand complexes in nanoelectrospray ionization mass spectrometry.

A new methodology for distinguishing between specific and nonspecific protein-ligand complexes in nanoelectrospray ionization mass spectrometry (nanoES-MS) is described. The method involves the addition of an appropriate reference protein (P(ref)), which does not bind specifically to any of the solution components, to the nanoES solution containing the protein(s) and ligand(s) of interest. The occurrence of nonspecific protein-ligand binding is monitored by the appearance of nonspecific (P(ref) + ligand) complexes in the nanoES mass spectrum. Furthermore, the fraction of P(ref) undergoing nonspecific ligand binding provides a quantitative measure of the contribution of nonspecific binding to the measured intensities of protein and specific protein-ligand complexes. As a result, errors introduced into protein-ligand association constants, K(assoc), as determined with nanoES-MS, by nonspecific ligand binding can be corrected. The principal assumptions on which this methodology is based, namely, that the fraction of proteins and protein complexes that engage in nonspecific ligand binding during the nanoES process is determined by the number of free ligand molecules in the offspring droplets leading to gaseous ions and is independent of the size and structure of the protein or protein complex, are shown to be generally valid. The application of the method for the determination of K(assoc) for two protein-carbohydrate complexes, under conditions where nonspecific ligand binding is prevalent, is demonstrated.

Binding Sites↗
PubMed2006

Capillary separations enabling tissue proteomics-based biomarker discovery.

Development of the capability to enable large-scale proteome studies, analogous to comprehensive gene expression analysis, will clearly have far-reaching impacts on protein biomarker investigations of human diseases such as cancer through interrogation of the archived fresh frozen and formalin-fixed and paraffin-embedded tissue collections. This review therefore focuses on the most recent advances in microdissection techniques and proteome platforms for procuring homogeneous subpopulations of tumor cells or structures and performing comprehensive analysis of protein profiles within tissue specimens, respectively. Developments in capillary separations capable of providing extremely high resolving power and selective analyte enrichment are particularly highlighted for their roles within the broader context of a state-of-the-art integrated tissue proteome effort. The capabilities of CIEF-based multidimensional separations for performing proteome analysis from minute samples create new opportunities in the pursuit of biomarker discovery using enriched and selected cell populations procured from tissue specimens. These proteome technological advances combined with recently developed tissue microdissection techniques provide powerful tools for those seeking to gain a greater understanding at the global level of the cellular machinery associated with human diseases such as cancer.

Biomarkers↗
PubMed2006

Characterization of the human salivary proteome by capillary isoelectric focusing/nanoreversed-phase liquid chromatography coupled with ESI-tandem MS.

Saliva is a readily available body fluid with great diagnostic potential. The foundation for saliva-based diagnostics, however, is the development of a complete catalog of secreted and "leaked" proteins detectable in saliva. By employing a capillary isoelectric focusing-based multidimensional separation platform coupled with electrospray ionization tandem mass spectrometry (MS), a total of 5338 distinct peptides were sequenced, leading to the identification of 1381 distinct proteins. A search of bacterial protein sequences also identified many peptides unique to several organisms and unique to the NCBI nonredundant database. To the best of our knowledge, this proteome study represents the largest catalog of proteins measured from a single saliva sample to date. Data analysis was performed on individual MS/MS spectra using the highly specific peptide identification algorithm, OMSSA. Searches were conducted against a decoyed SwissProt human database to control the false-positive rate at 1%. Furthermore, the well-curated SwissProt sequences represent perhaps the least redundant human protein sequence database (12,484 records versus the 50,009 records found in the International Protein Index human database), therefore minimizing multiple protein inferences from single peptides. This combined bioanalytical and bioinformatic approach has established a solid foundation for building up the human salivary proteome for the realization of the diagnostic potential of saliva.

Chromatography, Liquid↗
PubMed2005

Stride lengths, speed and energy costs in walking of Australopithecus afarensis: using evolutionary robotics to predict locomotion of early human ancestors.

This paper uses techniques from evolutionary robotics to predict the most energy-efficient upright walking gait for the early human relative Australopithecus afarensis, based on the proportions of the 3.2 million year old AL 288-1 'Lucy' skeleton, and matches predictions against the nearly contemporaneous (3.5-3.6 million year old) Laetoli fossil footprint trails. The technique creates gaits de novo and uses genetic algorithm optimization to search for the most efficient patterns of simulated muscular contraction at a variety of speeds. The model was first verified by predicting gaits for living human subjects, and comparing costs, stride lengths and speeds to experimentally determined values for the same subjects. Subsequent simulations for A. afarensis yield estimates of the range of walking speeds from 0.6 to 1.3 m s-1 at a cost of 7.0 J kg-1 m-1 for the lowest speeds, falling to 5.8 J kg-1 m-1 at 1.0 m s-1, and rising to 6.2 J kg-1 m-1 at the maximum speed achieved. Speeds previously estimated for the makers of the Laetoli footprint trails (0.56 or 0.64 m s-1 for Trail 1, 0.72 or 0.75 m s-1 for Trail 2/3) may have been underestimated, substantially so for Trail 2/3, with true values in excess of 0.7 and 1.0 m s-1, respectively. The predictions conflict with suggestions that A. afarensis used a 'shuffling' gait, indicating rather that the species was a fully competent biped.

Animals↗
PubMed2005

Nonspecific protein-carbohydrate complexes produced by nanoelectrospray ionization. Factors influencing their formation and stability.

Factors influencing the formation of nonspecific protein-carbohydrate complexes during the nanoelectrospray (nanoES) process have been investigated. Protonated and deprotonated nonspecific complexes of ubiquitin (Ubq) and protonated complexes of carbonic anhydrase (CA) with carbohydrates, ranging in size from mono- to tetrasaccharide, were produced by nanoES and detected with a Fourier transform ion cyclotron resonance mass spectrometer. Both the fraction of protein engaged in nonspecific binding with the carbohydrates and the number of carbohydrates bound to the protein increase with increasing carbohydrate concentration. At a given concentration of protein and carbohydrate, nonspecific binding is favored for small (mono- and disaccharide) or hydrophilic carbohydrates over larger or more hydrophobic molecules, which tend to form gaseous monomer or cluster ions by nanoES. However, the extent of nonspecific binding is insensitive to the structure of the protein, with similar distributions of nonspecific complexes observed for both CA and Ubq. Nonspecific association is also insensitive to the charge state of the complex. A comparable degree of binding is observed for complexes in their protonated and deprotonated forms. Furthermore, the number of bound ligands can exceed significantly the charge state of the complex. Thermal dissociation experiments performed on the gaseous nonspecific complexes reveal that their kinetic stability is sensitive to both the structure of the carbohydrate (i.e., mono- < di- < tri- < tetrasaccharide) and the protein (Ubq < CA) and to the charge state, although no simple relationship between stability and charge state was identified. Taken together, the results of this study suggest that neutral protein-carbohydrate interactions (e.g., hydrogen bonds) contribute significantly and, perhaps, predominantly to the formation and stabilization of the nonspecific complexes. A strategy to minimize the formation of the nonspecific complexes, which is based on the enhancement of gaseous carbohydrate ion formation through the addition of metal salts (e.g., CaCl2) to the nanoES solution, is demonstrated.

Carbohydrates↗
PubMed2005

Blackbody infrared radiative dissociation of nonspecific protein-carbohydrate complexes produced by nanoelectrospray ionization: the nature of the noncovalent interactions.

Gas-phase thermal dissociation experiments, implemented with blackbody infrared radiative dissociation (BIRD) and Fourier transform ion cyclotron resonance mass spectrometry, have been performed on a series of protonated and deprotonated 1:1 and protonated 1:2 protein-carbohydrate complexes formed by nonspecific interactions during the nanoflow electrospray (nanoES) ionization process. Nonspecific interactions between the proteins bovine carbonic anhydrase II (CA), bovine ubiquitin (Ubq), and bovine pancreatic trypsin inhibitor and several carbohydrates, ranging in size from mono- to tetrasaccharides, have been investigated. Over the range of temperatures studied (60-190 degrees C), BIRD of the protonated and deprotonated complexes proceeds exclusively by the loss of the carbohydrate in its neutral form. The rates of dissociation of the 1:1 complexes containing a mono- or disaccharide decrease with reaction time, suggesting the presence of two or more kinetically distinct structures produced during nanoES or by gas-phase processes. In contrast, the 1:1 complexes of the tri- and tetrasaccharides exhibit simple first-order dissociation kinetics, a result that, on its own, is suggestive of a single preferred carbohydrate binding site or multiple equivalent sites in the gas phase. A comparative analysis of the dissociation kinetics measured for protonated 1:1 and 1:2 complexes of Ubq with alphaTal[alphaAbe]alphaMan further supports the presence of a single preferred binding site. However, a similar analysis performed on the complexes of CA and alphaTal[alphaAbe]alphaMan suggests that equivalent but dependent carbohydrate binding sites exist in the gas phase. Analysis of the Arrhenius activation parameters (E(a) and A) determined for the dissociation of 1:1 complexes of CA with structurally related trisaccharides provides evidence that neutral intermolecular hydrogen bonds contribute, at least in part, to the stability of the gaseous complexes. Surprisingly, the E(a) values for the complexes of the same charge state are not sensitive to the structure (primary or higher order) of the protein, suggesting that the carbohydrates are able to form energetically equivalent interactions with the various functional groups presented by the protein. For a given protein-carbohydrate complex, the dissociation E(a) is sensitive to charge state, initially increasing and then decreasing with increasing charge. It is proposed that both ionic and neutral hydrogen bonds stabilize the nonspecific protein-carbohydrate complexes in the gas phase and that the relative contribution of the neutral and ionic interactions is strongly influenced by the charge state of the complex, with neutral interactions dominating at low charge states and ionic interactions dominating at high charge states.

Binding Sites↗
PubMed2004

Comparison of inverse-dynamics musculo-skeletal models of AL 288-1 Australopithecus afarensis and KNM-WT 15000 Homo ergaster to modern humans, with implications for the evolution of bipedalism.

Size and proportions of the postcranial skeleton differ markedly between Australopithecus afarensis and Homo ergaster, and between the latter and modern Homo sapiens. This study uses computer simulations of gait in models derived from the best-known skeletons of these species (AL 288-1, Australopithecus afarensis, 3.18 million year ago) and KNM-WT 15000 (Homo ergaster, 1.5-1.8 million year ago) compared to models of adult human males and females, to estimate the required muscle power during bipedal walking, and to compare this with those in modern humans. Skeletal measurements were carried out on a cast of KNM-WT 15000, but for AL 288-1 were taken from the literature. Muscle attachments were applied to the models based on their position relative to the bone in modern humans. Joint motions and moments from experiments on human walking were input into the models to calculate muscle stress and power. The models were tested in erect walking and 'bent-hip bent-knee' gait. Calculated muscle forces were verified against EMG activity phases from experimental data, with reference to reasonable activation/force delays. Calculated muscle powers are reasonably comparable to experimentally derived metabolic values from the literature, given likely values for muscle efficiency. The results show that: 1) if evaluated by the power expenditure per unit of mass (W/kg) in walking, AL 288-1 and KNM-WT 15000 would need similar power to modern humans; however, 2) with distance-specific parameters as the criteria, AL 288-1 would require to expend relatively more muscle power (W/kg.m(-1)) in comparison to modern humans. The results imply that in the evolution of bipedalism, body proportions, for example those of KNM-WT 15000, may have evolved to obtain an effective application of muscle power to bipedal walking over a long distance, or at high speed.

Adult↗
PubMed2003

Bioactive recognition sites may not be energetically preferred in protein-carbohydrate complexes in the gas phase.

Arrhenius parameters, obtained with the blackbody infrared radiative dissociation technique, are reported for the dissociation of a gaseous protonated complex of an antibody single chain fragment and its native trisaccharide antigen originating from nonspecific interactions during the nanoelectrospray process. It is shown that the nonspecific complex is kinetically more stable and, at the +10 charge state, energetically more stable than the corresponding specific complex originating from interactions in solution. This is the first demonstration that a bioactive recognition site is not energetically preferred in a protein-ligand complex in the gas phase.

Antibodies, Monoclonal↗
PubMed2003

Influence of solution and gas phase processes on protein-carbohydrate binding affinities determined by nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry.

The influence of solution pH, analyte concentration and in-source dissociation on the measurement of the association constant for a single chain variable fragment of a monoclonal antibody (scFv) and its native trisaccharide ligand by nanoelectrospray-Fourier transform ion cyclotron resonance mass spectrometery has been systematically investigated. From the results of this study, experimental conditions that preserve the original distribution of bound and unbound protein in solution into the gas phase, such that the nanoES mass spectrum provides a quantitative measure of the solution composition, were identified. These include the use of short spray durations (<10 min) to minimize pH changes, equimolar concentrations of protein and ligand to minimize the formation of nonspecific complexes, and short accumulation times (<2 s) in the hexapole of the ion source to avoid collisional heating and dissociation of the gaseous complex. Application of this methodology to the scFv and a series of carbohydrate ligands yields results that are in agreement with values previously determined by isothermal titration calorimetry. Competitive binding experiments performed on solutions containing the scFv and a mixture of carbohydrate ligands were also found to yield accurate association constants.

Fourier Analysis↗
PubMed2003

Determination of protein-oligosaccharide binding by nanoelectrospray fourier-transform ion cyclotron resonance mass spectrometry.

The two studies presented here demonstrate that nanoES-FT-ICR MS is a powerful method for studying the association of oligosaccharide ligands with monomeric and multimeric proteins. It permits the facile identification of the occupancy of binding sites, information that is not readily available by other techniques. Its high-resolution capability is ideally suited to the observation of interactions between a large protein receptor and a relatively small oligosaccharide ligand. The sensitive and rapid determination of association constants for protein carbohydrate complexes is expected to find wide application.

Fourier Analysis↗
PubMed2003

An acoustic wave sensor incorporated with a microfluidic chip for analyzing muscle cell contraction.

We report the fabrication of a microfluidic chip or lab-on-a-chip integrated with a thickness-shear mode (TSM) acoustic wave sensor for muscle cell analysis. The sensor, essentially an AT-cut quartz crystal, serves as a detector for recording changes in acoustic wave properties occurring in an attached cardiomyocyte (single heart muscle cell) during its contraction and relaxation. Presumably, the changes resulted from alterations in viscoelastic properties (e.g. stiffness) of the cells. The effects of excitation electrode size, the presence of a microfluidic channel plate, and liquid loading on the sensor were first examined. Thereafter, muscle cell contraction analysis upon chemical stimuli were described. The potential of the chip for screening of cardiovascular drugs is discussed.

Animals↗
PubMed2002

Retention of bioactive ligand conformation in a gaseous protein-trisaccharide complex.

Arrhenius parameters, obtained with the blackbody infrared radiative dissociation technique, are reported for the dissociation of gaseous protonated complexes of a single-chain variable fragment (scFv) of the monoclonal antibody Se155-4 with structurally constrained trisaccharide ligands that resemble the bioactive conformer. The similarity in the dissociation activation energies measured for the +10 charge-state complexes of the constrained ligands and the native trisaccharide is evidence that the bioactive conformation of the native ligand is retained in the gas phase.

Antibodies, Monoclonal↗