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UnknownHydrogen-Bonding-Directed Ordered Assembly of Carboxylated Poly(3-Alkylthiophene)s.
Not available
S-EPMC6645037 | biostudies-literature
UnknownFactors Influencing Patients' Sleep in the Intensive Care Unit: Perceptions of Patients and Clinical Staff.
Not available
S-EPMC5559223 | biostudies-literature
UnknownAnxiety Symptoms After Orthopedic Injury: A Systematic Review.
Not available
S-EPMC7799444 | biostudies-literature
ProteomicsDifferential impact of phosphate availability on primary and specialized metabolism of Streptomyces lividans and Streptomyces coelicolor.
In order to define the impact of phosphate (Pi) availability on cellular metabolism the project aimed to perform a comparative analysis of the proteomes of two Streptomyces strains with different abilities to produce antibiotics, S. coelicolor and S. lividans as well as of the pptA mutant of S. livi...
ORGANISM(S): Streptomyces coelicolor Streptomyces lividans TK24 
2022-02-04 | PXD029263 | Pride
Label-free protein quantification Antibiotics Proteomics Streptomyces Phosphate Respiratory chain Oxidative stress Central carbon metabolism 
UnknownLatent Transition Analysis of the Symptom Experience of Cancer Patients Undergoing Chemotherapy.
Not available
S-EPMC6399048 | biostudies-literature
UnknownBiomarkers as Common Data Elements for Symptom and Self-Management Science.
Not available
S-EPMC5945303 | biostudies-literature
ProteomicsStructural mapping of the surfaces of fibrillar 1N3R and 1N4R human tau
The structural characterization of pathogenic tau filaments that accumulate in tauopathies, including Alzheimer disease, is key for understanding their pathogenic function and identify the structural determinants of distinct tau filaments involved in distinct tauopathies. Fibrillar tau surfaces play...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD027403 | Pride
Structural proteomics  proteolysis  chemical surface modification  nhs-biotin  nanolc-msms Tau fibrils 
ProteomicsIdentification of proteins interacting with extracellularly applied α-syn assemblies, Condition 3 - controls (5/8)
Fibrillar α-Synuclein (α-Syn) is the principal component of Lewy bodies which are evident in individuals affected by Parkinson disease (PD). This neuropathologic form of α-Syn contributes to PD progression and propagation of exogeneous α-Syn between neurons has been demonstrated. In order to identif...
ORGANISM(S): Rattus norvegicus (Rat) 
2015-09-07 | PXD002260 | Pride
Lc-msms Oligomers Fibrils Pull-down Protein-protein interactions Proteomics Alpha-synuclein 
ProteomicsIdentification of proteins interacting with extracellularly applied α-syn assemblies, Condition 1 - biological replicates (2/8)
Fibrillar α-Synuclein (α-Syn) is the principal component of Lewy bodies which are evident in individuals affected by Parkinson disease (PD). This neuropathologic form of α-Syn contributes to PD progression and propagation of exogeneous α-Syn between neurons has been demonstrated. In order to identif...
ORGANISM(S): Rattus norvegicus (Rat) 
2015-09-07 | PXD002257 | Pride
Lc-msms Oligomers Fibrils Pull-down Protein-protein interactions Proteomics Alpha-synuclein 
ProteomicsIdentification of proteins interacting with extracellularly applied α-syn assemblies, Condition 2 - controls (3/8)
Fibrillar α-Synuclein (α-Syn) is the principal component of Lewy bodies which are evident in individuals affected by Parkinson disease (PD). This neuropathologic form of α-Syn contributes to PD progression and propagation of exogeneous α-Syn between neurons has been demonstrated. In order to identif...
ORGANISM(S): Rattus norvegicus (Rat) 
2015-09-07 | PXD002258 | Pride
Lc-msms Oligomers Fibrils Pull-down Protein-protein interactions Proteomics Alpha-synuclein 
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