SERBP1

Last update 08 May 2025

Basic Info

Synonyms

CGI-55, CHD3IP, DKFZP564M2423

+ [8]

Introduction

Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (PubMed:36691768). Acts via its association with EEF2/eEF2 factor, sequestering EEF2/eEF2 at the A-site of the ribosome and promoting ribosome stabilization and storage in an inactive state (By similarity). May also play a role in the regulation of mRNA stability: binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay (PubMed:11001948). Seems to play a role in PML-nuclear bodies formation (PubMed:28695742).

100 Clinical Results associated with SERBP1

100 Translational Medicine associated with SERBP1

0 Patents (Medical) associated with SERBP1

127

Literatures (Medical) associated with SERBP1

01 Apr 2025·Tissue and Cell

Clinical and immunohistochemical effects of OncoTherad (MRB-CFI-1) nanoimmunotherapy on SERBP1, HABP4, CD44 and Ki-67 in BCG-unresponsive non-muscle invasive bladder cancer

Article

Author: Lestingi, Jean Felipe Prodocimo ; Bottene, Martim Corrêa ; da Silva Santos, André ; Alonso, João Carlos Cardoso ; Caria, Paulo Henrique Ferreira ; de Freitas, Leandro Luiz Lopes ; Salmazo, Maria Izabel de Barros Frazão ; Fávaro, Wagner José ; Roberto, Isadora Manzato ; Kobarg, Jörg ; de Arruda Camargo, Gabriela Cardoso ; Durán, Nelson ; Ávila, Monaliza ; de Oliveira, Gabriela

Non-muscle-invasive bladder cancer (NMIBC) is a malignancy with a high recurrence and progression rate, particularly in patients who fail to respond to standard Bacillus Calmette-Guérin (BCG) therapy. OncoTherad (MRB-CFI-1) nanoimmunotherapy has emerged as a promising therapeutic option, with potential to modulate immune responses and inhibit tumor progression. This study evaluated the clinical efficacy of OncoTherad (MRB-CFI-1) nanoimmunotherapy in patients with BCG-unresponsive NMIBC and investigated correlations between therapeutic outcomes and histopathological and molecular findings. In this retrospective cross-sectional study, 20 patients with BCG-unresponsive NMIBC were treated with OncoTherad (MRB-CFI-1) across two clinical centers. Bladder tissue samples were collected before and after treatment, and immunohistochemical analyses were performed to assess the expression of SERBP1, HABP4, CD44, and Ki-67. Primary endpoints included pathological complete response (pCR), recurrence-free survival (RFS), and duration of response (DoR), which were analyzed in relation to immunohistochemical biomarker findings. Our results demonstrated that high Ki-67 proliferative index and elevated immunoreactivity for CD44 and SERBP1 were associated with shorter RFS. Treatment with OncoTherad (MRB-CFI-1) significantly reduced (p < 0.05) the immunoreactivity of SERBP1 and CD44, which was accompanied by a marked decrease in Ki-67 proliferative index, indicating effective suppression of tumor activity. Conversely, a significant increase (p < 0.05) in HABP4 immunoreactivity was observed, suggesting a protective role against NMIBC recurrence and progression. A pCR was achieved in 65 % of patients, with a median RFS of 21.1 months and a median DoR of 15.7 months, underscoring the clinical efficacy of OncoTherad (MRB-CFI-1). These findings suggest that OncoTherad (MRB-CFI-1) nanoimmunotherapy offers a novel and effective treatment strategy for patients with BCG-unresponsive NMIBC, providing a promising alternative to radical cystectomy and significantly improving patient outcomes.

01 Jan 2025·Journal of Proteomics

Protein degradation patterns as biomarkers for post-mortem interval estimation: A comprehensive review of proteomic approaches in forensic science

Review

Author: Kumari, Pallavi ; Chhikara, Anjali ; Kumari, Kiran ; Dalal, Jyoti

The determination of post-mortem interval (PMI) is a critical process for forensic medical-legal investigations. Proteomic techniques are gaining prominence in analysing forensic biological samples. After death, studying the proteins present in human bodies could be critical in discovering important new biomarkers that can serve as reliable indicators of various factors. A literature review is conducted on estimating PMI through protein degradation analysis using PubMed, NCBI, SCOPUS, Research Gate, Science Direct, and Google Scholar. A total of 32 studies were identified and studied. It is found that the most commonly studied tissue type is the skeleton muscle (15 studies), followed by others. The kinetics of several proteins and proteases were particularly correlated with PMI. Different proteins degrade differently after death: alpha-actinin, GAPDH, and alpha-tubulin breakdown slowly, but meta-vinculin breaks down early. Tropomyosin does not change for a long time after death, up to 10 days. Certain markers had a positive correlation with PMI, meaning that their amount increased as PMI hours increased, while other markers showed a negative correlation, suggesting that their number decreased with time. The level of several biological markers, such as SERBP1, COX7B, and SOD2, changed gradually and consistently as the PMI increased. The information gathered from this analysis provides new opportunities for precise PMI measurements in legal contexts by expanding the research area's use in human skeletal tissue.

01 Dec 2024·European Journal of Cell Biology

Salmonella infection impacts host proteome thermal stability

Article

Author: Vervoorts, Jörg ; Mateus, André ; Savitski, Mikhail M ; Sefried, Stephanie ; Walch, Philipp ; Selkrig, Joel ; Typas, Athanasios ; Amelang, Jan ; Birk, Marlène S ; Baykara, Tarik ; Breuer, Ingrid ; Buerova, Elena

Intracellular bacterial pathogens hijack the protein machinery of infected host cells to evade their defenses and cultivate a favorable intracellular niche. The intracellular pathogen Salmonella enterica subsp. Typhimurium (STm) achieves this by injecting a cocktail of effector proteins into host cells that modify the activity of target host proteins. Yet, proteome-wide approaches to systematically map changes in host protein function during infection have remained challenging. Here we adapted a functional proteomics approach - Thermal-Proteome Profiling (TPP) - to systematically assess proteome-wide changes in host protein abundance and thermal stability throughout an STm infection cycle. By comparing macrophages treated with live or heat-killed STm, we observed that most host protein abundance changes occur independently of STm viability. In contrast, a large portion of host protein thermal stability changes were specific to infection with live STm. This included pronounced thermal stability changes in proteins linked to mitochondrial function (Acod1/Irg1, Cox6c, Samm50, Vdac1, and mitochondrial respiratory chain complex proteins), as well as the interferon-inducible protein with tetratricopeptide repeats, Ifit1. Integration of our TPP data with a publicly available STm-host protein-protein interaction database led us to discover that the secreted STm effector kinase, SteC, thermally destabilizes and phosphorylates the ribosomal preservation factor Serbp1. In summary, this work emphasizes the utility of measuring protein thermal stability during infection to accelerate the discovery of novel molecular interactions at the host-pathogen interface.

Analysis

Perform a panoramic analysis of this field.

view full example data

Hiro LS Researcher

The AI Search Engine Built to Accelerate Biopharma Decisions

Search across billion-scale life sciences data to uncover signals, validate evidence, and act with confidence.

Ask any biopharma research question→

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.

Discover Synapse Data Servers

Synapse data is now integrated into the PatSnap LS Model Context Protocol (MCP) service. Customize your LLM agent now using our MCP server!

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

SERBP1

Basic Info

Related

Analysis