Welcome to LookChem.com Sign In|Join Free

CAS

  • or

113543-30-9

Post Buying Request

113543-30-9 Suppliers

Recommended suppliersmore

  • Product
  • FOB Price
  • Min.Order
  • Supply Ability
  • Supplier
  • Contact Supplier

113543-30-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 113543-30-9 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,1,3,5,4 and 3 respectively; the second part has 2 digits, 3 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 113543-30:
(8*1)+(7*1)+(6*3)+(5*5)+(4*4)+(3*3)+(2*3)+(1*0)=89
89 % 10 = 9
So 113543-30-9 is a valid CAS Registry Number.

113543-30-9Relevant articles and documents

Coupling protein engineering with probe design to inhibit and image matrix metalloproteinases with controlled specificity

Morell, Montse,Nguyen Duc, Thinh,Willis, Amanda L.,Syed, Salahuddin,Lee, Jiyoun,Deu, Edgar,Deng, Yang,Xiao, Junpeng,Turk, Benjamin E.,Jessen, Jason R.,Weiss, Stephen J.,Bogyo, Matthew

, p. 9139 - 9148 (2013)

Matrix metalloproteinases (MMPs) are zinc endopeptidases that play roles in numerous pathophysiological processes and therefore are promising drug targets. However, the large size of this family and a lack of highly selective compounds that can be used for imaging or inhibition of specific MMPs members has limited efforts to better define their biological function. Here we describe a protein engineering strategy coupled with small-molecule probe design to selectively target individual members of the MMP family. Specifically, we introduce a cysteine residue near the active-site of a selected protease that does not alter its overall activity or function but allows direct covalent modification by a small-molecule probe containing a reactive electrophile. This specific engineered interaction between the probe and the target protease provides a means to both image and inhibit the modified protease with absolute specificity. Here we demonstrate the feasibility of the approach for two distinct MMP proteases, MMP-12 and MT1-MMP (or MMP-14).

Discovery of TD-0212, an Orally Active Dual Pharmacology AT1 Antagonist and Neprilysin Inhibitor (ARNI)

McKinnell, R. Murray,Fatheree, Paul,Choi, Seok-Ki,Gendron, Roland,Jendza, Keith,Olson Blair, Brooke,Budman, Joe,Hill, Craig M.,Hegde, Laxminarayan G.,Yu, Cecile,McConn, Donavon,Hegde, Sharath S.,Marquess, Daniel G.,Klein, Uwe

supporting information, p. 86 - 91 (2019/01/04)

Dual inhibition of angiotensin-converting enzyme (ACE) and neprilysin (NEP) by drugs such as omapatrilat produces superior antihypertensive efficacy relative to ACE inhibitors but is associated with a higher risk of life-threatening angioedema due to bradykinin elevations. We hypothesized that dual AT1 (angiotensin II type 1 receptor) blockade and NEP inhibition with a single molecule would produce similar antihypertensive efficacy to omapatrilat without the risk of angioedema since ACE (the rate limiting enzyme in bradykinin metabolism) would remain uninhibited. Merging the structures of losartan (an AT1 antagonist) and thiorphan (a NEP inhibitor) led to the discovery of a novel series of orally active, dual AT1 antagonist/NEP inhibitors (ARNIs) exemplified by compound 35 (TD-0212). In models of renin-dependent and -independent hypertension, 35 produced blood pressure reductions similar to omapatrilat and combinations of AT1 receptor antagonists and NEP inhibitors. Upper airway angioedema risk was assessed in a rat tracheal plasma extravasation (TPE) model. Unlike omapatrilat, 35 did not increase TPE at antihypertensive doses. Compound 35 therefore provides the enhanced activity of dual AT1/NEP inhibition with a potentially lower risk of angioedema relative to dual ACE/NEP inhibition.

CALPAIN MODULATORS AND METHODS OF PRODUCTION AND USE THEREOF

-

Paragraph 00482, (2017/09/27)

The present technology relates to compounds, kits, compositions, and methods useful for the treatment of fibrotic disease. In some aspects, the present technology provides for treatment of various diseases or disorders associated or mediated, at least in part, by calpains, such as CAPN1, CAPN2, and/or CAPN9. The present technology is generally applicable to compounds which inhibit myofibroblast differentiation.

Post a RFQ

Enter 15 to 2000 letters.Word count: 0 letters

Attach files(File Format: Jpeg, Jpg, Gif, Png, PDF, PPT, Zip, Rar,Word or Excel Maximum File Size: 3MB)

1

What can I do for you?
Get Best Price

Get Best Price for 113543-30-9