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Stroke patients have reduced aerobic capacity. Therefore, intensive structured exercise programs are needed. We report the case of a patient with stroke and cardiac disease who underwent early inpatient cardiac rehabilitation (CR). A 38-year-old male patient with atrial fibrillation, heart failure, and cerebral infarction underwent a symptom-limited exercise tolerance test (ETT) without any problems on day 45 after admission. He completed a 2-week inpatient program and an 8-week home-based CR program. Follow-up ETT showed increased exercise capacity. The present case might be the first to report a safely performed CR program in a patient with stroke and cardiac comorbidity in Korea. Systematic guidance is needed for post-stroke patients to receive safe and effective CR for the secondary prevention of stroke and cardiovascular risk.

Additional file 2: Figure S1. MS/MS spectra of tryptic peptides derived from the N protein in serum samples from patients infected with severe fever with thrombocytopenia syndrome virus (SFTSV). MS/MS spectra for each peptide in medium from cultured cells or in serum from SFTS patients were compared. A: IAVEFGEQQLNLTELEDFAR (7–26th); B: ELAYEGLDPALIIK (27–40th); C: LSITPVR (100–106th); D: GILGPDGVPSR (223–233th).

Additional file 4: Figure S2. Qualitative characteristics of the PRM assay. The representative chromatograms of target peptides used in the PRM assay. a) Upper rows designated native peptides in serum specimens and b) lower rows designated heavy peptides of them. Mass error and retention times are annotated on the peak. c) Retention time of two target native peptides (light) and their synthetic peptides (heavy). The red bar denoted light peptides and blue bar denoted heavy peptides.

Additional file 5: Figure S3. 3D structure of the N protein and peptides detected by MS/MS analysis. Each peptide is assigned a different color: red (7–26th), orange (100–136th), yellow (165–179th), green (191–215th), or blue (223–233th).

Additional file 3: Table S2. Target peptides and transitions used for the LC-PRM MS Analysis.

Additional file 1: Table S1. Results of molecular diagnostic using RT-PCR of SFTS patients.

Additional file 1. CONSORT 2010 Flow Diagram

Additional file 1: Supplementary Materials.

Supplemental Material, sj-pdf-1-mrj-10.1177_00222437211013781 for Improving Business-to-Business Customer Satisfaction Programs: Assessment of Asymmetry, Heterogeneity, and Financial Impact by Vikas Mittal, Kyuhong Han, Ju-Yeon Lee and Shrihari Sridhar in Journal of Marketing Research

Additional file 7:Figure S3. Down-regulation of asymmetric arginine methylation in MS023-treated CRC cells. DLD1 and HCT116 cells were treated with increasing concentrations of MS023 for 48 h as indicated above. Equal amounts of total protein (20 μg) were loaded to polyacrylamide gel followed by Western blot using anti-ADMA antibodies.

Additional file 8:Figure S4. Representative flow cytometry plots of control and MS023-treated CRC cells. DLD1 (A) and HCT116 cells (B) were treated with or without MS023 (200 μM) for 48 h. Detached and adherent cells were collected and stained with Annexin V and propidium iodide as described in Methods.

Glycosylation is a topic of intense current interest in the development of biopharmaceuticals because it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submitted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of analytical methods presently used in the glycosylation analysis of mAbs. Therefore, participation was unrestricted, with laboratories choosing their own measurement techniques. Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification. Consequently, the diversity of results was enormous, with the number of glycan compositions identified by each laboratory ranging from 4 to 48. In total, one hundred sixteen glycan compositions were reported, of which 57 compositions could be assigned consensus abundance values. These consensus medians provide community-derived values for NISTmAb PS. Agreement with the consensus medians did not depend on the specific method or laboratory type. The study provides a view of the current state-of-the-art for biologic glycosylation measurement and suggests a clear need for harmonization of glycosylation analysis methods.

Glycosylation is a topic of intense current interest in the development of biopharmaceuticals because it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submitted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of analytical methods presently used in the glycosylation analysis of mAbs. Therefore, participation was unrestricted, with laboratories choosing their own measurement techniques. Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification. Consequently, the diversity of results was enormous, with the number of glycan compositions identified by each laboratory ranging from 4 to 48. In total, one hundred sixteen glycan compositions were reported, of which 57 compositions could be assigned consensus abundance values. These consensus medians provide community-derived values for NISTmAb PS. Agreement with the consensus medians did not depend on the specific method or laboratory type. The study provides a view of the current state-of-the-art for biologic glycosylation measurement and suggests a clear need for harmonization of glycosylation analysis methods.

Additional file 6:Figure S2. Venn diagram showing overlaps of MMA and ADMA sites between CRC tissues and HCT116 cells. Overlap between arginine methylation sites identified by (A) MMA and (B) ADMA antibodies using protein extracts from CRC tissues and HCT116 cells.

Additional file 8:Figure S4. Representative flow cytometry plots of control and MS023-treated CRC cells. DLD1 (A) and HCT116 cells (B) were treated with or without MS023 (200 μM) for 48 h. Detached and adherent cells were collected and stained with Annexin V and propidium iodide as described in Methods.

Additional file 5:Figure S1. Venn diagram showing overlaps of monomethylated and asymmetric dimethylated proteins between CRC tissues and HCT116 cells. Overlap between proteins identified by (A) MMA and (B) ADMA antibodies using protein extracts from CRC tissues and HCT116 cells. The Venn diagram was generated using online program VENNY (http://bioinfogp.cnb.csic.es/tools/venny/ index.html).

Additional file 7:Figure S3. Down-regulation of asymmetric arginine methylation in MS023-treated CRC cells. DLD1 and HCT116 cells were treated with increasing concentrations of MS023 for 48 h as indicated above. Equal amounts of total protein (20 μg) were loaded to polyacrylamide gel followed by Western blot using anti-ADMA antibodies.