Results 21 to 30 of about 18,795 (277)

The multifaceted proprotein convertases: their unique, redundant, complementary, and opposite functions. [PDF]

open access: yesJ Biol Chem, 2013
The secretory proprotein convertase (PC) family comprises nine members: PC1/3, PC2, furin, PC4, PC5/6, PACE4, PC7, SKI-1/S1P, and PCSK9. The first seven PCs cleave their substrates at single or paired basic residues, and SKI-1/S1P cleaves its substrates ...
Seidah NG   +3 more
europepmc   +2 more sources

Mechanism of Fine-tuning pH Sensors in Proprotein Convertases: IDENTIFICATION OF A pH-SENSING HISTIDINE PAIR IN THE PROPEPTIDE OF PROPROTEIN CONVERTASE 1/3. [PDF]

open access: yesJ Biol Chem, 2015
Background: Propeptides regulate the organelle-specific, pH-dependent activation of proprotein convertases. Results: A histidine residue pair in the propeptide cooperatively defines the activation pH for proprotein convertase 1/3.
Williamson DM, Elferich J, Shinde U.
europepmc   +2 more sources

Relative expression of proprotein convertases in rat ovaries during pregnancy. [PDF]

open access: yesJ Ovarian Res, 2013
BackgroundProprotein convertases are a family of serine proteinases that are related to bacterial subtilisin and yeast kexin. They are involved in posttranslational processing of the precursors of a vast number of cellular proteins. With the exception of
Kwok SC   +3 more
europepmc   +2 more sources

Hysteretic behavior of proprotein convertase 1/3 (PC1/3). [PDF]

open access: yesPLoS ONE, 2011
The proprotein convertases (PCs) are calcium-dependent proteases responsible for processing precursor proteins into their active forms in eukariotes.
Marcelo Y Icimoto   +9 more
doaj   +6 more sources

The proprotein convertase furin in tumour progression [PDF]

open access: yesInternational Journal of Cancer, 2017
Proprotein convertases are proteases that have been implicated in the activation of a wide variety of proteins. These proteins are generally synthesised as precursor proteins and require limited proteolysis for conversion into their mature bioactive counterparts.
Michele Bernasconi
exaly   +5 more sources

Inhibition of proprotein convertases abrogates processing of the middle eastern respiratory syndrome coronavirus spike protein in infected cells but does not reduce viral infectivity. [PDF]

open access: yesJ Infect Dis, 2015
Middle East respiratory syndrome coronavirus (MERS-CoV) infection is associated with a high case-fatality rate, and the potential pandemic spread of the virus is a public health concern. The spike protein of MERS-CoV (MERS-S) facilitates viral entry into
Gierer S   +9 more
europepmc   +2 more sources

Repression of liver colorectal metastasis by the serpin Spn4A a naturally occurring inhibitor of the constitutive secretory proprotein convertases. [PDF]

open access: yesOncotarget, 2014
Liver is the most common site of metastasis from colorectal cancers, and liver of patients with liver colorectal metastasis have abnormal levels of the proprotein convertases (PCs).
Sfaxi F   +9 more
europepmc   +2 more sources

Implications of Proprotein Convertases in Ovarian Cancer Cell Proliferation and Tumor Progression: Insights for PACE4 as a Therapeutic Target. [PDF]

open access: yesTransl Oncol, 2014
Proprotein convertases are a family of kexin-like serine proteases that process proteins at single and multiple basic residues. Among the predicted and identified PC substrates, an increasing number of proteins having functions in cancer progression ...
Longuespée R   +10 more
europepmc   +3 more sources

Prediction of proprotein convertase cleavage sites [PDF]

open access: bronzeProtein Engineering, Design and Selection, 2004
Many secretory proteins and peptides are synthesized as inactive precursors that in addition to signal peptide cleavage undergo post-translational processing to become biologically active polypeptides. Precursors are usually cleaved at sites composed of single or paired basic amino acid residues by members of the subtilisin/kexin-like proprotein ...
Peter Duckert   +2 more
openalex   +4 more sources

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