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Difference between revisions of "User:Wei Peng"

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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 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 or cryo-EM and biochemical methods to investigate protein functions. As a postdoc with Prof. Kim Orth at UT Southwestern Medical Center, he has discovered 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 of its protein substrate.
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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]]).
  
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Wei contributed to studies on:
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.
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* [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite>
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<biblio>
 
<biblio>
#Gilbert2008 pmid=18430603
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#Peng2024 pmid=38354245
  
 
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</biblio>

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]