Ultimate Process Killer is a small Windows application whose purpose is to help you kill running processes on the breeze.

The advantages of being portable

Since this is a portable program, it is important to mention that it doesn’t leave any traces in the Windows Registry.

You can copy it on any USB flash drive or other devices, and take it with you whenever you need to terminate running processes on the breeze, without having to go through installation steps.

Clean feature lineup

The primary panel lists all running processes and provides comprehensive information about each one, such as process name, ID, file path, parent process ID, thread count, priority, processor time, page file size, creation date, handle, creation class name, kernel mode time, OS name, private page count, Windows version, read and write operation count, virtual size, and many others.

Main features

Ultimate Process Killer gives you the possibility to kill the selected process, terminate only the selected processes, and refresh the current list with just one click.

What’s more, you can view the total number of detected processes, delete parent file, as well as make the app terminate a process when you perform a double-click mouse operation on the desired one. Tests revealed that the utility carries out a task quickly without eating up a lot of CPU and memory.

Bottom line

To sum things up, Ultimate Process Killer comes packed with a handy set of features for helping you manage running processes. The deletion option comes in handy especially if you have detected a malicious process running on your system, as it allows you to delete the parent virus file.

Download latest version of Ultimate Process Killer latest version is 2.0, with new features and important fixes.

Powerful Utilities for Windows

Our team of enthusiastic developers has collected the most common software applications used in Windows and you can download it without any problems. All software files are easy to use and install. All you need to do is just download and run a.exe file. Downloading them is completely free. You can also choose from a number of most popular software categories to get more options.Let’s see if this works…

Let’s see if this works…



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You’re reading Proglematist, a blog about software development and human factors. It was born on May 2012, its goal is to provide a simple place to read about software development, specifically the human factors involved.Porphyromonas gingivalis is the primary etiologic agent of severe and persistent periodontitis and has been implicated in the development of other systemic disorders such as cardiovascular disease, rheumatoid arthritis, diabetes, Alzheimer’s disease, and respiratory diseases. The ability of P. gingivalis to cause these diseases is due, in part, to its pathogenicity factors that facilitate colonization and infection of host tissues. These include the Arg-gingipain (Rgp) family of proteins that are capable of degrading host proteins such as hemoglobin, fibronectin, and laminin, and the fimbrial serotype 2 and type 9 that promote attachment to host cells. Although much is known about P. gingivalis virulence, the genes encoding the proteins that promote pathogenicity and infectivity remain largely unknown. Over the past 4 years, we identified a number of virulence-associated genes in the P. gingivalis genome including the rgp-encoding genes rgpA and rgpB. The expression of rgpA and rgpB has been shown to be controlled by the regulatory genes bglR and bglG, respectively. In this project, we will further investigate the mechanisms involved in the regulation of rgpA and rgpB gene expression. We have made progress in the cloning of rgpB using as a probe an internal fragment of the gene. Using this probe, we have screened a P. gingivalis genomic DNA library and have obtained a P. gingivalis genomic DNA fragment of 2.7 kb that hybridizes with the bglG probe. This 2.7 kb fragment contains a gene, designated tgps1, that encodes a putative amino acid-rich protein. The gene tgps1 is predicted to be 21 amino acids in length and contains repeated sequences at its 3′-end. Preliminary data indicate that the transcription of tgps1 is regulated by a putative HspR binding site upstream of the gene. Mutations in the putative HspR binding site significantly increase the expression of tgps1, and the disruption of the putative HspR binding site reduces the


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