GTPBP1

Last update 08 May 2025

Basic Info

Synonyms

G-protein 1, GP-1, GP1

+ [4]

Introduction

Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity (By similarity).

100 Clinical Results associated with GTPBP1

100 Translational Medicine associated with GTPBP1

0 Patents (Medical) associated with GTPBP1

583

Literatures (Medical) associated with GTPBP1

01 Jul 2025·Fish & Shellfish Immunology

Acute hypoxia stress impairs Litopenaeus vannamei resistance to white spot syndrome virus by downregulating chitin-binding proteins

Article

Author: Li, Chaozheng ; Weng, Shaoping ; He, Honghui ; He, Jianguo

Hypoxia stress is a key environmental stressor that can induce white spot syndrome virus (WSSV) outbreaks, but underlying mechanisms remain unclear. Here, transcriptome analysis and RT-PCR were conducted to investigate the impact of acute hypoxia stress on gene expression profiles in shrimp. We revealed that acute hypoxia stress significantly altered the expression profile of genes in shrimp gill, particularly downregulating genes encoding chitin-binding proteins (CBPs), including Mucin-19, GAAP, CP1114, SgAbd-1, pro-Resilin, Obstructor-E, CP, GP1, and AMP1A. Downregulation of Mucin-19, GAAP, CP1114, and SgAbd-1 by RNA interference significantly increased shrimp mortality and viral loads following WSSV infection. Temporal expression analysis further confirmed that Mucin-19, GAAP, CP1114, and SgAbd-1 were involved in WSSV infection. Thus, acute hypoxia stress facilitates WSSV infection by inhibiting CBPs expression. This study provides the first evidence of the role of shrimp CBPs in response to hypoxia stress and antiviral defense, offering novel insights into environmental stress-host-virus interactions.

01 May 2025·International Journal of Biological Macromolecules

A VLP vaccine platform comprising the core protein of hepatitis B virus with N-terminal antigen capture

Article

Author: Rowlands, David J ; Fatema, Kaniz ; Watson, Alexander ; Ranson, Neil A ; Stonehouse, Nicola J ; Snowden, Joseph S ; Sherry, Lee

Nanoparticle presentation systems offer the potential to develop new vaccines rapidly in response to emerging diseases, a public health need that has become increasingly evident in the wake of the COVID-19 pandemic. Previously, we reported a nanoparticle scaffold system termed VelcroVax. This was constructed by insertion of a high affinity SUMO binding protein (Affimer), able to recognise a SUMO peptide tag, into the major immunodominant region of VLPs assembled from a tandem (fused dimer) form of hepatitis B virus (HBV) core protein (HBc). Here we describe an alternative form, termed N-VelcroVax, a VLP vaccine platform assembled from a monomeric HBc protein (N-anti-SUMO Affimer HBc 190) with the Affimer inserted at the N-terminus. In contrast to the tandem form of VelcroVax, N-VelcroVax VLPs were expressed well in E. coli. The VLPs effectively bound SUMO-tagged Junín virus glycoprotein, gp1 as assessed by structural and serological analyses. Cryo-EM characterisation of N-VelcroVax complexed with a SUMO-Junín gp1 showed continuous density attributable to the fused Affimer, in addition to evidence of target antigen capture. Collectively, these data suggest that N-VelcroVax has potential as a versatile next generation vaccine scaffold.

23 Apr 2025·Journal of Agricultural and Food Chemistry

Two Antihypertensive and Antioxidant Peptides Derived from Alaska Pollack (Theragra chalcograma) Skin: In Silico, In Vitro, and In Vivo Investigation

Article

Author: Qu, Jian-Bo ; Zhang, Jian ; Liu, Shi-Hai ; Wu, Chen-Xi ; Liu, Cheng-Lin ; Zhai, Yong-Nian ; Zhang, Hai-Lin ; Cai, Duo ; Li, Jing

This study aimed to identify and characterize two novel dual-functional peptides with antihypertensive and antioxidant activities from byproducts of Alaska pollock skin (APS). Results showed that fifty-nine peptides were identified from APS, of which two peptides, GP1 (GSAGPAGPSGPRGP) and GP2 (LGDARNSPAPP), were predicted to exhibit the highest angiotensin-converting enzyme (ACE) inhibitory and antioxidant activities. GP1 and GP2 demonstrated favorable ACE inhibitory activities (IC₅₀ values of 0.166 and 0.177 mmol/L, respectively) and significantly reduced blood pressure in hypertensive rats. Additionally, both peptides effectively scavenged 2,2'-casino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radicals, with EC₅₀ values of 0.273 and 0.629 mg/mL and protected HepG2 cells against H₂O₂-induced damage. Molecular docking revealed that the peptides interacted with amino acid residues within the active pocket and at the entrance channel of ACE, displaying mixed-competitive inhibition patterns. These peptides could also bind to the Kelch domain of Kelch-like ECH associating protein (Keap1), thereby promoting nuclear factor erythroid 2-related factor 2 (Nrf2)-mediated transcriptional activation of antioxidant enzymes through the Keap1-Nrf2 pathway. The dual ACE inhibitory and antioxidant properties of APS peptides, coupled with high gastrointestinal stability, validated their utilization as multifunctional ingredients in antihypertensive functional foods, nutraceuticals, and peptide-based hydrogel development.

Analysis

Perform a panoramic analysis of this field.

view full example data

AI Agents Built for Biopharma Breakthroughs

Accelerate discovery. Empower decisions. Transform outcomes.

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, PatSnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Start your data trial now!

Synapse data is also accessible to external entities via APIs or data packages. Empower better decisions with the latest in pharmaceutical intelligence.

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

GTPBP1

Basic Info

Related

Analysis