Results 201 to 210 of about 190,299 (260)

FAP-α is an effective tool to evaluate stroma invasion of lung adenocarcinoma. [PDF]

open access: yesDiagn Pathol
Xiong S   +6 more
europepmc   +1 more source

Engineering Single-Chain Antibody Fragment (scFv) Variants Targeting A Disintegrin and Metalloproteinase-17 (ADAM-17). [PDF]

open access: yesBiomolecules
Kalantar M   +5 more
europepmc   +1 more source

How Rapidly Does the FAPI PET Signal Reverse Following Therapy? Assessing the FAPI PET Signal in Hypertensive Cardiac Injury and Fibrosis in Mice. [PDF]

open access: yesJ Nucl Med
Hosseini A   +13 more
europepmc   +1 more source

Comparative characterization of two serine endopeptidases from Nocardiopsis sp. NCIM 5124

Biochimica et Biophysica Acta (BBA) - General Subjects, 2000
A protease-producing, crude oil degrading marine isolate was identified as Nocardiopsis sp. on the basis of the morphology, cell wall composition, mycolic acid analysis and DNA base composition. The Nocardiopsis produces two extracellular proteases, both of which are alkaline serine endopeptidases.
V S, Dixit, A, Pant
openaire   +3 more sources

Characterization of Serine Endopeptidases in Cotyledons of Germinated Vigna mungo Seeds

Journal of Plant Research, 1999
seeds. SEP activity was separated into two isoforms by CM-cellulose column chromatography. These forms, termed SEP-1 and SEP-II, showed endopeptidase activities even at acidic pH, suggesting that SEPs are unique serine endopeptidases, since most serine proteases are optimum at neutral pH.
Tomoki Hosokawa   +2 more
openaire   +2 more sources

Improved isolation, stability and substrate specificity of cucumisin, a plant serine endopeptidase

open access: closedBiotechnology and Applied Biochemistry, 1995
Cucumisin (EC 3.4.21.25), a serine endopeptidase, was isolated by a simple purification procedure from the prince melon (Cucumis melo ssp. melo, cv. ‘Prince Melon’). The enzyme is stable over a wide pH range (4‐11) and to heat, 80% of its initial activity remaining even at pH 11.1 and at 60 degrees C for 20 min.
M. Kaneda, H. Yonezawa, Tetsuya Uchikoba
openalex   +3 more sources

Polyproline fold—In imparting kinetic stability to an alkaline serine endopeptidase

open access: closedBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2012
Polyproline II (PPII) fold, an unusual structural element was detected in the serine protease from Nocardiopsis sp. NCIM 5124 (NprotI) based on far UV circular dichroism spectrum, structural transitions of the enzyme in presence of GdnHCl and a distinct isodichroic point in chemical and thermal denaturation.
Sonali B. Rohamare   +5 more
openalex   +3 more sources

Yeast KEX2 gene encodes an endopeptidase homologous to subtilisin-like serine proteases

open access: closedBiochemical and Biophysical Research Communications, 1988
Yeast Saccharomyces cerevisiae KEX2 gene previously isolated, was characterized as the gene encoding a calcium-dependent endopeptidase required for processing of precursors of alpha-factor and killer toxin. In this study, we report the amino acid sequence of the KEX2 gene product deduced from nucleotide sequencing.
Kensaku Mizuno   +4 more
openalex   +3 more sources

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