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Medical scientists discovered that 2.5 years after mRNA injection, the vaccine peaked protein and found the major peaks of excessive deaths. New research is co


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2025 May 27, 7:18am   50 views  4 comments

by HANrongli   ➕follow (0)   ignore (17)  




🚨 We found vaccine spike protein 2.5 YEARS after mRNA injection — and uncovered major spikes in excess mortality. New studies coming soon.

https://t.me/mcculloughfund/1834

As the government turns its back on mRNA harms and the vaccine-injured, the McCullough Foundation is picking up the pieces.

As the government turns its back on mRNA harms and the vaccine-injured, the McCullough Foundation is picking up the pieces. 🚨我们发现mRNA注射2.5年后,我们发现了疫苗峰值蛋白,并发现了过多死亡的主要峰值。 新研究即将推出。

当政府拒绝mRNA Harms和受疫苗受伤的疫苗时,McCullough Foundation正在捡起碎片。

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1   HANrongli   2025 May 27, 7:41am  




The Spike Protein is One of the Most Dangerous Proteins in the World.

@P_McCulloughMD

https://t.me/mcculloughfund/1833

#MFEducation 尖峰蛋白是世界上最危险的蛋白质之一。

@p_mcculloughmd

#mfeducation
2   HANrongli   2025 May 27, 3:05pm  




GOOD NEWS - Covid Bioweapon Injection Removed From CDC Recommended Immunization Schedule
For children and pregnant women... but it's certainly not enough!
ECCENTRIK
MAY 27

好消息 - 从CDC推荐的免疫时间表中除去的Covid Bioweapon注入
对于儿童和孕妇...但这肯定还不够!
Eccentrik
5月27日
4   HANrongli   2025 May 27, 4:20pm  





Cadaver "Calamari"
Amyloidogenic
Fibrin Aggregates
Spike Protein Pathology from Cadavers Exposed to
Bioengineered SARS-CoV-2

尸体“鱿鱼”

淀粉样蛋白

纤维蛋白聚合物

暴露于尸体的尖峰蛋白病理

生物工程SARS-CoV-2

Kevin W. McCairn, Ph.D., Kevin McKernan Ph.D., Shojiro Kato M.D., Charles Rixey retired (USMC-CBRN)

https://open.substack.com/pub/kevinwmccairnphd282302/p/cadaver-calamari-amyloidogenic-fibrin

Abstract
This report presents a preliminary forensic analysis of anomalous fibrin-like aggregates recovered from postmortem human cadaveric samples. Through a combination of gross morphological inspection, cryosection histology, fluorescent staining, scanning electron microscopy (SEM), elemental analysis (EDX), real-time PCR, Raman spectroscopy, and Real-Time Quaking-Induced Conversion (RT-QuIC), the samples were examined for biochemical and ultrastructural features associated with amyloidogenic and protease-resistant fibrin formation. Findings suggest that the clot samples exhibit hallmarks of abnormal protein aggregation consistent with pathological fibrin remodeling, including enhanced autofluorescence, beta-sheet rich domains, dense fibrillar ultrastructure, and spectral anomalies. PCR confirmed the human origin of the tissues, and preliminary evidence of molecular markers associated with recombinant spike protein exposure (SV40 & Ori) was observed. Limitations of provenance, sample control, and chain-of-custody are acknowledged, and further investigation is recommended to establish clinical, pathological, and etiological relevance.

These fibrils display nodular topography and branching interconnections, consistent with pathological protein assembly. Notably, a rotational twist and lateral aggregation features were observed, hallmarks of amyloid fibrin architecture. These ultrastructural findings support the hypothesis that the observed material is not simple polymerized fibrin but instead a protease-resistant, misfolded protein aggregate.

Elemental mapping via EDX revealed high abundance of carbon, nitrogen, oxygen, and sulfur—consistent with proteinaceous material. No significant signal was detected for heavy metals (e.g., Fe, Zn, Cu), ruling out mineral-based aggregation or contamination. The absence of inorganic nucleation points supports an endogenous biochemical origin.

Section 4: PCR and Raman Spectroscopy for Tissue and Molecular Signature Image: Slides 18-20
PCR using primers for the human RNaseP transcript confirmed that the clot-derived samples were of human origin. Additional assays targeting spike protein coding sequences and plasmid-related markers (SV40, Ori) revealed late-cycle amplification, consistent with trace residual presence of recombinant vaccine components. These findings are preliminary and require cautious interpretation.
Raman spectroscopy revealed a major spectral peak at ~1720 cm⁻¹, diverging from the canonical amyloid beta-sheet signature near 1670 cm⁻¹. This spectral upshift may reflect altered secondary structure, ester linkage formation, or protonation of acidic residues. The results point to an atypical fibril composition that may represent a novel polymorph or hybrid aggregate class.

Section 5: RT-QuIC Seeding Activity in Plasma Extracts
RT-QuIC analysis was used to assess seeding potential of the clot-associated material. 3D bar plot visualization of fluorescence intensity across a 96-well plate revealed elevated ThT signal in experimental wells, consistent with fibril formation, when challenged against human plasma.
However, background signal, handling artifacts, and absence of dilution series limit interpretation. Without kinetic rate modeling and control seeding, the data remain suggestive but inconclusive for prion-like activity.

Conclusion
The clot structures described herein exhibit abnormal morphological, histological, ultrastructural, and spectroscopic features. Their dense fibrillar architecture, autofluorescence, ThT reactivity, spectral shifts, and preliminary RT-QuIC activity suggest amyloidogenic remodeling of fibrin under unknown conditions.
While the findings are not definitive, they raise substantial biosafety and pathophysiological questions that warrant immediate, controlled follow-up. The uncertain provenance and unstandardized collection methodology underscore the need for independent replication with verified chain-of-custody.
In the current context of vaccine-induced spike protein exposure and post-infectious complications, these results may point to a novel or under-recognized pathology. As such, they constitute a call for interdisciplinary scientific inquiry, clinical vigilance, and transparent investigation.

Slides

抽象的
该报告对从死后人尸体样品中回收的异常纤维蛋白样聚集体进行了初步法医分析。 通过总体形态检查,冷冻组织学,荧光染色,扫描电子显微镜(SEM),元素分析(EDX),实时PCR,Raman光谱和实时Quaking诱导的转换(RT-Quic)的结合,研究了与膜片和蛋白酶型的样品相关的样品。 研究结果表明,凝块样品表现出与病理纤维蛋白重塑一致的异常蛋白质聚集的标志,包括增强的自动荧光,富含β-片富含β型结构域,密集的原纤维超微结构和光谱异常。 PCR证实了组织的人类起源,并观察到与重组峰值蛋白暴露(SV40&ORI)相关的分子标记的初步证据。 承认出处,样本控制和抑制链的局限性,并建议进一步研究以建立临床,病理和病因学相关性。


这些纤维表现出结膜地形和分支互连,与病理蛋白质组装一致。值得注意的是,观察到旋转扭曲和横向聚集特征,是淀粉样纤维蛋白结构的标志。这些超结构发现支持了这样的假设,即观察到的材料不是简单的聚合纤维蛋白,而是抗蛋白酶、错误折叠的蛋白质聚集体。

通过EDX的元素测绘显示,碳、氮、氧和硫含量很高——与蛋白质物质一致。没有检测到重金属(例如铁、锌、铜)的显著信号,排除了基于矿物的聚集或污染。无机成核点的缺失支持了内源性生化起源。

第4节:组织和分子特征图像的PCR和拉曼光谱:幻灯片18-20

使用引物对人类RNaseP转录物的PCR证实了凝块衍生样本是人类来源的。针对尖峰蛋白编码序列和质粒相关标记(SV40,Ori)的额外测定揭示了晚期周期扩增,与重组疫苗成分的微量残留存在一致。这些发现是初步的,需要谨慎解释。

拉曼光谱学揭示了一个主要光谱峰值,位于~1720厘米−¹,与1670厘米−¹附近的规范淀粉样β片特征不同。这种光谱上升可能会反映二次结构的改变、酯键的形成或酸性残基的质子化。结果表明,非典型纤维成分可能代表一种新的多态或杂交聚合类。

第5节:血浆提取物中的RT-QuIC播种活动

RT-QuIC分析用于评估凝块相关材料的播种潜力。 跨96孔板荧光强度的3D条状图可视化显示,当挑战人类血浆时,实验井中的ThT信号升高,与纤维形成一致。

然而,背景信号、处理伪影和没有稀释系列限制了解释。 在没有动力学速率建模和控制播种的情况下,数据仍然具有暗示性,但对类似朌呋的活性没有定论。

缔结

此处描述的凝块结构表现出异常的形态学、组织学、超微结构和光谱特征。 它们密集的纤维结构、自荧光、ThT反应性、光谱转移和初步的RT-QuIC活性表明,在未知条件下纤维蛋白的淀粉样原重塑。

虽然这些发现不是确定的,但它们提出了大量生物安全和病理生理学问题,需要立即进行有控制的随访。 不确定的来源和不标准化的收集方法凸显了通过经过验证的监管链进行独立复制的必要性。

在当前疫苗诱导的尖峰蛋白暴露和感染后并发症的背景下,这些结果可能表明一种新的或未被认可的病理。 因此,它们构成了跨学科科学探究、临床警惕和透明调查的呼吁。

幻灯片

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