Results 161 to 170 of about 27,067 (198)

Diagnostic Decision Points of Specific Immunoglobulin E Concentrations for Seafood Allergies in Korean Children: A Nationwide Multicenter Study. [PDF]

open access: yesAllergy Asthma Immunol Res
Kim M   +17 more
europepmc   +1 more source

Crystal structures of cables formed by the acetylated and unacetylated forms of the Schizosaccharomyces pombe tropomyosin ortholog TpmCdc8. [PDF]

open access: yesJ Biol Chem
Reinke PYA   +10 more
europepmc   +1 more source

Diagnostic Accuracy of Novel Protein Biomarkers in Saliva to Detect Periodontitis Using Untargeted 'SWATH' Mass Spectrometry. [PDF]

open access: yesJ Clin Periodontol
Blanco-Pintos T   +6 more
europepmc   +1 more source
Some of the next articles are maybe not open access.

Related searches:

On the polymerization of tropomyosin

Archives of Biochemistry and Biophysics, 1962
Abstract The polymerization of tropomyosin was studied by light scattering, covering a wide range of protein and salt concentrations. Depolymerization of tropomyosin molecules with dilution was found at very dilute protein concentration, a phenomenon which had not been observed.
Tatsuo Ooi   +2 more
openaire   +3 more sources

Tryptic Digestion of Tropomyosin A, Tropomyosin B and Myosin [PDF]

open access: possibleNature, 1966
Two types of tropomyosins co-exist in lamellibranch adductors and in cephalopod muscle1: TMA and TMB, TMA being the protein referred to as invertebrate tropomyosin, or water-insoluble tropomyosin, by Bailey, and TMB the water-soluble variety.
openaire   +2 more sources

β‐Tropomyosin mutations alter tropomyosin isoform composition

European Journal of Neurology, 2008
Background and purpose:  Tropomyosin (TM) is an actin‐binding protein, which is localized head to tail along the length of the actin filament. There are three major TM isoforms in human striated muscle. Mutations in β‐tropomyosin (TPM2) have recently been identified as an important cause of neuromuscular disorders.
Homa Tajsharghi, J. Nilsson
openaire   +3 more sources

Home - About - Disclaimer - Privacy