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1.
Prog Transplant ; 25(1): 26-34, 2015 Mar.
Article in English | MEDLINE | ID: mdl-25758797

ABSTRACT

CONTEXT: Dialysis patients' lifestyles are associated with low levels of physical activity, increasing the chances of being removed from kidney waiting lists or dying while awaiting transplant because of increased cardiovascular risk factors and deteriorating health conditions. Personalized mobile health (mHealth) delivered programs may support their engagement in healthier lifestyles, maintain transplant eligibility, and reduce premature mortality. OBJECTIVE: To explore barriers and perceptions of physical activity behaviors and gauge interest in using mHealth in a physical activity wellness program for dialysis patients on the kidney transplant waiting list. PARTICIPANTS AND DESIGN: In-depth key informant interviews were conducted with 22 randomly selected dialysis patients during dialysis treatment in an urban Southeastern coastal city. A theory-guided community-based participatory research approach was used to develop the interview content. Constructivist grounded theory guided the data analysis using NVIVO 10 (QSR Int). The 32-item checklist from the Consolidated Criteria for Reporting Qualitative Studies was used in the qualitative reporting. RESULTS: Dialysis patients had a mean age of 46 (SD, 10.7) years, 45% were female, and 82% were African American. Their mean duration on transplant waiting lists was 6.7 (SD 4.3) years, and 73% owned smartphones. After saturation was reached, predominant themes included (1) physical activity was perceived as optional, (2) social support both encouraged and limited physical activity, (3) chronic stress and coping influenced physical activity, (4) spirituality provided strength to engage in physical activity, (5) self-care management practices varied considerably, and (6) high interest (95%) for using mHealth to promote physical activity was found. Patients preferred their home and neighborhood environments to intradialytic settings for engaging in physical activity.


Subject(s)
Attitude to Computers , Attitude to Health , Cell Phone , Exercise , Kidney Transplantation/psychology , Kidney Transplantation/rehabilitation , Waiting Lists , Attitude to Death , Checklist , Community-Based Participatory Research , Female , Humans , Interviews as Topic , Male , Middle Aged , Quality of Life , Renal Dialysis , Risk Factors , Self Care , Social Determinants of Health , Social Support , Stress, Psychological
2.
Biochemistry ; 44(43): 14217-30, 2005 Nov 01.
Article in English | MEDLINE | ID: mdl-16245938

ABSTRACT

The Sso10b (or Alba) family of proteins is a conserved group of archaeal and eukaryotic proteins which are thought to play a role in both chromatin organization and RNA metabolism. We describe here the solution structure and properties of Sso10b2 from Sulfolobus solfataricus. NMR data including residual dipolar couplings and (15)N relaxation data demonstrated that the protein adopts a beta(1)alpha(1)beta(2)alpha(2)beta(3)beta(4) topology with an IF-3-like fold. The protein dimerizes in solution at 30 degrees C via a hydrophobic surface defined by the C-terminal alpha(2)beta(3)beta(4) elements with a structure similar to one of the putative dimers indicated by previous crystal structures. DSC and circular dichroism data demonstrated an unusual two-state structural transition near the growth temperature which led to an increase in beta-sheet content without dissociation of the dimer. The cooperativity of the transition exceeded that of a dimer at pH 7, demonstrating the presence of higher order oligomers near the growth temperature at pH 7. Reverse titrations of Sso10b2 with nucleic acid showed that the protein binds single-stranded DNA (K(d) of 3 x 10(-)(7) M) with higher affinity than RNA (1.3 x 10(-)(6) M) or double-stranded DNA (1.5 x 10(-)(5) M) in 10 mM KH(2)PO(4) (pH 7.0, 20 degrees C). NMR chemical shift perturbation data indicated that single-stranded DNA and RNA binding occurred across the same dimer interface and encompassed a surface defined by the C-terminal ends of the beta(1), beta(2), and beta(3) strands of each monomer.


Subject(s)
Archaeal Proteins/chemistry , Archaeal Proteins/metabolism , DNA-Binding Proteins/chemistry , DNA-Binding Proteins/metabolism , Nucleic Acids/metabolism , Protein Conformation , Sulfolobus acidocaldarius/chemistry , Amino Acid Sequence , Archaeal Proteins/genetics , Crystallography, X-Ray , DNA-Binding Proteins/genetics , Dimerization , Hydrogen-Ion Concentration , Hydrophobic and Hydrophilic Interactions , Magnetic Resonance Spectroscopy , Molecular Sequence Data , Protein Folding , Thermodynamics
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