In my previous blog, I talked about creating a footprint using an existing template in Allegro ECAD-MCAD Library Creator and explained how easily you can access an existing template and create a package from it by just clicking a button. In this blog...(read more)

Hi Guys,

Anyone know equivalent skill for create detail.

Eugene

Currently I tried this:

axlDBCreateShape(recPolyPlanes t "BOUNDARY/L02" netName sym1)

I get a atom error on car(sym1)

I can do this "static" using ETCH/L02 with out an issue, but I am trying to avoid doing an axlShapeChangeDynamicType().

Thanks,

Jerry

Hi guys,

eDave,

I need to call (replay) a skill to combine some skills to ONE UI for more convenience and using as more easier.

Please help me to find the command to execute this.(code for example as more good)

HT,

I would like to add these components to the component bank in ORCAD simulation. Even an accessible or free course that explained how to create these components.

When in Constraint Manager, Physical Domain, one can create a new Physical Constraint Class defining specific attributes for a custom rule set. One can then assing this new rule set to a set of nets. To do that it is instructed to create a new Net Class with menu Objects > Create > Net Class. Also on that same menu is available Net Group. Both options create a group that appear in the Constraint Manager Objects Name Column. I have triied both  options and cant really see the difference. 

The Question: What is the difference between creating a Net Class and a Net Group ?  What are the implications ?

Thanks for your help.

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This is a summary only. Click the title for the full article, or visit www.EastWestCenter.org/Research-Wire for more.

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Title: Health Tip: Create a Space for Sleep
Category: Health News
Created: 4/30/2008 2:00:00 AM
Last Editorial Review: 4/30/2008 12:00:00 AM

Title: Researchers Develop Quick Way to Create Human Antibodies
Category: Health News
Created: 5/1/2008 2:00:00 AM
Last Editorial Review: 5/1/2008 12:00:00 AM

Title: Health Tip: Create a Sick-Day Plan for Diabetes
Category: Health News
Created: 5/5/2017 12:00:00 AM
Last Editorial Review: 5/5/2017 12:00:00 AM

ABSTRACT

Humans encode proteins, called restriction factors, that inhibit replication of viruses such as HIV-1. The members of one family of antiviral proteins, apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3 (APOBEC3; shortened here to A3), act by deaminating cytidines to uridines during the reverse transcription reaction of HIV-1. The A3 locus encodes seven genes, named A3A to A3H. These genes have either one or two cytidine deaminase domains, and several of these A3s potently restrict HIV-1. A3C, which has only a single cytidine deaminase domain, however, inhibits HIV-1 only very weakly. We tested novel double domain protein combinations by genetically linking two A3C genes to make a synthetic tandem domain protein. This protein created a "super restriction factor" that had more potent antiviral activity than the native A3C protein, which correlated with increased packaging into virions. Furthermore, disabling one of the active sites of the synthetic tandem domain protein resulted in an even greater increase in the antiviral activity—recapitulating a similar evolution seen in A3F and A3G (double domain A3s that use only a single catalytically active deaminase domain). These A3C tandem domain proteins do not have an increase in mutational activity but instead inhibit formation of reverse transcription products, which correlates with their ability to form large higher-order complexes in cells. Finally, the A3C-A3C super restriction factor largely escaped antagonism by the HIV-1 viral protein Vif.

IMPORTANCE As a part of the innate immune system, humans encode proteins that inhibit viruses such as HIV-1. These broadly acting antiviral proteins do not protect humans from viral infections because viruses encode proteins that antagonize the host antiviral proteins to evade the innate immune system. One such example of a host antiviral protein is APOBEC3C (A3C), which weakly inhibits HIV-1. Here, we show that we can improve the antiviral activity of A3C by duplicating the DNA sequence to create a synthetic tandem domain and, furthermore, that the proteins thus generated are relatively resistant to the viral antagonist Vif. Together, these data give insights about how nature has evolved a defense against viral pathogens such as HIV.