Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText.
Kick-your-searchterm to multiple Engines kick-your-query now !>
A dictionary by aggregated review articles of nephrology, medicine and the life sciences
Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

suck abstract from ncbi


10.1021/acs.jmedchem.5c02037

http://scihub22266oqcxt.onion/10.1021/acs.jmedchem.5c02037
suck pdf from google scholar
41319234!?!41319234

Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=41319234&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215

suck abstract from ncbi

pmid41319234      J+Med+Chem 2025 ; ? (?): ?
Nephropedia Template TP

gab.com Text

Twit Text FOAVip

Twit Text #

English Wikipedia


  • CD160-Derived Peptide as a Bidirectional Inhibitor Toward Immune Checkpoints BTLA/HVEM and HVEM/LIGHT #MMPMID41319234
  • Lipinska M; Ciura P; Gumpelmair S; Sikorska E; Kuncewicz K; Sieradzan AK; Steinberger P; Wardowska A; Spodzieja M
  • J Med Chem 2025[Nov]; ? (?): ? PMID41319234show ga
  • BTLA and HVEM are key immune checkpoint proteins involved in regulating immune responses. Since HVEM also binds to CD160 at a site that overlaps with the BTLA binding site, CD160-derived fragments were used to design peptide inhibitors targeting this interface. Several peptides were synthesized and assessed for HVEM binding using SpS analysis, and their inhibitory activity was evaluated in ELISA and cell-based assays. One peptide, namely A5, demonstrated strong HVEM binding and effectively blocked the BTLA/HVEM interaction. Molecular docking results revealed that peptide A5 binds to HVEM not only at the BTLA interaction site but also at the region involved in LIGHT binding. Consistent with these findings, ELISA and cell-based assays confirmed that A5 effectively disrupts both BTLA/HVEM and HVEM/LIGHT complex formation. These results suggest that A5 acts as a dual inhibitor of HVEM interactions, with potential therapeutic implications for immune-related disorders.
  • ?


  • DeepDyve
  • Pubget Overpricing
  • suck abstract from ncbi

    Linkout box