CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article.
Totally new to the CAZy classification? Read this first.

Difference between revisions of "User:Wei Peng"

From CAZypedia
Jump to navigation Jump to search
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
 
[[Image:Wei-Peng.jpeg|200px|right]]
 
[[Image:Wei-Peng.jpeg|200px|right]]
Wei Peng obtained his Ph.D. at Tsinghua University in China with Prof. Yigong Shi and Prof. Nieng Yan, where he was trained as a structural biologist using protein crystallography/cryo-EM and other tools to investigate protein functions. As a postdoc with Prof. Kim Orth at UT Southwestern Medical Center, he has discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase (with a fold called '''Fido''') that catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate <cite>Peng2024</cite>. AvrB represents a novel family of glycosyltransferase ([[GT138]]).
+
Wei Peng obtained his Ph.D. at Tsinghua University (Beijing, China) with Prof. Yigong Shi and Prof. Nieng Yan. He was trained as a structural biologist using protein crystallography/cryo-EM and other tools to investigate protein functions. Currently as a postdoctoral scholar with Prof. Kim Orth at UT Southwestern Medical Center (Dallas, USA), he has been focusing on host-pathogen interactions.  
  
Wei contributed to investigations into:
+
Wei and colleagues discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase (with a fold called Fido) <cite>Peng2024</cite>. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells. '''AvrB is the founding member of glycosyltransferases with Fido fold''' ([[GT138]]).
  
* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase <cite>Peng2024</cite>
+
Wei contributed to studies on:
 +
* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite>
  
  

Latest revision as of 15:02, 18 December 2024

Wei-Peng.jpeg

Wei Peng obtained his Ph.D. at Tsinghua University (Beijing, China) with Prof. Yigong Shi and Prof. Nieng Yan. He was trained as a structural biologist using protein crystallography/cryo-EM and other tools to investigate protein functions. Currently as a postdoctoral scholar with Prof. Kim Orth at UT Southwestern Medical Center (Dallas, USA), he has been focusing on host-pathogen interactions.

Wei and colleagues discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase (with a fold called Fido) [1]. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells. AvrB is the founding member of glycosyltransferases with Fido fold (GT138).

Wei contributed to studies on:

  • GT138 Pseudomonas syringae rhamnosyltransferase AvrB [1]



  1. Peng W, Garcia N, Servage KA, Kohler JJ, Ready JM, Tomchick DR, Fernandez J, and Orth K. (2024). Pseudomonas effector AvrB is a glycosyltransferase that rhamnosylates plant guardee protein RIN4. Sci Adv. 2024;10(7):eadd5108. DOI:10.1126/sciadv.add5108 | PubMed ID:38354245 [Peng2024]