Results 41 to 50 of about 29,707,281 (129)

Global Brain Transcriptome Analysis of a Neuronal Ceroid Lipofuscinoses Mouse Model

open access: yesASN Neuro, 2019
In humans, homozygous mutations in the TPP1 gene results in loss of tripeptidyl peptidase 1 (TPP1) enzymatic activity, leading to late infantile neuronal ceroid lipofuscinoses disease.
Miriam S. Domowicz   +7 more
doaj   +1 more source

Characterization of the endopeptidase activity of tripeptidyl-peptidase II

open access: yes, 2012
Tripeptidyl-peptidase II (TPP II) is a giant cytosolic peptidase with a proposed role in cellular protein degradation and protection against apoptosis. Beside its well-characterised exopeptidase activity, TPP II also has an endopeptidase activity. Little
Eklund, Sandra,   +4 more
core   +1 more source

Cloning and heterologous expression of bovine pyroglutamyl peptidase type-1 in Escherichia coli : purification , biochemical and kinetic characterisation [PDF]

open access: yes, 2007
We describe the cloning, expression and purification of the bovine XM866409 form of pyroglutamyl-aminopeptidase I. The amino acid sequence, deduced from the nucleotide sequence, revealed that it consists of 209 amino acid residues and showed to have 98 ...
O'Connor, Brendan   +5 more
core   +2 more sources

Molecular characterisation of recombinant human pyroglutamyl peptidase (type I) [PDF]

open access: yes, 2005
Pyroglutamyl Peptidase I (PAP1, EC 3.4.19.3) hydrolytically cleaves pyroglutamic acid (pGlu) from the N-terminal of most pGlu-peptides. In higher organisms Thyrothropin Releasing Hormone is a notable biologically active substrate of PAP1. The sequence of
Vaas, Paul-Roman
core   +2 more sources

Tripeptidyl peptidase II serves as an alternative to impaired proteasome to maintain viral growth in the host cells [PDF]

open access: yes, 2010
The ubiquitin–proteasome system is known to be utilized by coxsackievirus to facilitate its propagation within the host cells. The present study explores the role of tripeptidyl peptidase II (TPPII), a serine peptidase contributing to protein turnover by
Guang Gao   +7 more
core   +1 more source

Structure-function analysis of Sedolisins: evolution of tripeptidyl peptidase and endopeptidase subfamilies in fungi

open access: yesBMC Bioinformatics, 2018
Background Sedolisins are acid proteases that are related to the basic subtilisins. They have been identified in all three superkingdoms but are not ubiquitous, although fungi that secrete acids as part of their lifestyle can have up to six paralogs ...
Facundo Orts, Arjen ten Have
doaj   +1 more source

Inhibitors of Tripeptidyl Peptidase II. 2. Generation of the First Novel Lead Inhibitor of Cholecystokinin-8-Inactivating Peptidase:  A Strategy for the Design of Peptidase Inhibitors

open access: yes, 2016
The cholecystokinin-8 (CCK-8)-inactivating peptidase is a serine peptidase which has been shown to be a membrane-bound isoform of tripeptidyl peptidase II (EC 3.4.14.10).
Ramesh B. Bambal (2381296)   +12 more
core   +1 more source

Exploring the Structural Design, Antibacterial Activity, and Molecular Docking of Newly Synthesized Zn(II) Complexes with NNO-Donor Carbazate Ligands

open access: yesMolecules
The present work reports the synthesis and structural design of three novel Zn(II) complexes [Zn(L1)(CH3COO)(H2O)] (1), [Zn(L2)2] (2), and [Zn(L3)2] (3) with carbazate ligands, 2-acetylpyridine-methylcarbazate (HL1), 2-acetylpyridine-ethylcarbazate (HL2),
Claudia C. Gatto   +7 more
doaj   +1 more source

Temperature modulates the secretome of the phytopathogenic fungus Lasiodiplodia theobromae

open access: yesFrontiers in Plant Science, 2016
Environmental alterations modulate host-microorganism interactions. Little is known about how climate changes can trigger pathogenic features on symbiont or mutualistic microorganisms.
Carina Félix   +8 more
doaj   +1 more source

Structure and function of tripeptidyl peptidase II, a giant cytosolic protease

open access: yes, 2011
Tripeptidyl peptidase II is the largest known eukaryotic peptidase. It has been described as a multi-purpose peptidase, which, in addition to its house-keeping function in intracellular protein degradation, plays a role in several vital cellular ...
Kopec, K. O.   +9 more
core   +1 more source

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