Bioaccumulation and distribution of cadmium by Burkholderia cepacia GYP1 under oligotrophic condition and mechanism analysis at proteome level

2019 ◽  
Vol 176 ◽  
pp. 162-169 ◽  
Author(s):  
Junhui Zhang ◽  
Qi Li ◽  
Yufei Zeng ◽  
Jian Zhang ◽  
Guining Lu ◽  
...  
2018 ◽  
Vol 28 (2) ◽  
pp. 161-172
Author(s):  
JUNHUI LUO ◽  
XIANLIN LIU ◽  
HAIFENG HUANG ◽  
DECAI MI ◽  
DEQIANG CHE

2020 ◽  
Vol 02 ◽  
Author(s):  
Masood Ghori ◽  
Nadya O. Al Matrooshi ◽  
Samir Al Jabbari ◽  
Ahmed Bafadel ◽  
Gopal Bhatnagar

: Infective Endocarditis (IE), a known complication of hemodialysis (HD), has recently been categorized as Healthcare-Associated Infective Endocarditis (HAIE). Single pathogen bacteremia is common, polymicrobial endocardial infection is rare in this cohort of the patients. We report a case of endocarditis caused by Enterococcus faecalis (E. faecalis) and Burkholderia cepacia (B. cepacia), a first ever reported combination of a usual and an unusual organism, respectively, in a patient on HD. Clinical presentation of the patient, its complicated course ,medical and surgical management ,along with microbial and echocardiographic findings is presented herein. The authors believe that presentation of this case of HAIE may benefit and contribute positively to cardiac science owing to the rare encounter of this organism as a pathogen in infective endocarditis and the difficulties in treating it.


Author(s):  
Rocco J. Rotello ◽  
Timothy D. Veenstra

: In the current omics-age of research, major developments have been made in technologies that attempt to survey the entire repertoire of genes, transcripts, proteins, and metabolites present within a cell. While genomics has led to a dramatic increase in our understanding of such things as disease morphology and how organisms respond to medications, it is critical to obtain information at the proteome level since proteins carry out most of the functions within the cell. The primary tool for obtaining proteome-wide information on proteins within the cell is mass spectrometry (MS). While it has historically been associated with the protein identification, developments over the past couple of decades have made MS a robust technology for protein quantitation as well. Identifying quantitative changes in proteomes is complicated by its dynamic nature and the inability of any technique to guarantee complete coverage of every protein within a proteome sample. Fortunately, the combined development of sample preparation and MS methods have made it capable to quantitatively compare many thousands of proteins obtained from cells and organisms.


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