Abdulmalek T Algarni

Dr. Abdulmalek T Algarni

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Research Focus & Metrics

Academic Career Length

10Years (2017-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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14 November 2019 in Mammal Research
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Manee ManeeManee Manee
Manee Manee
AAAbdulmalek T Algarni
Abdulmalek T Algarni
SASultan Alharbi
Sultan Alharbi
BABadr Alshomrani
Badr Alshomrani
MIMohanad A Ibrahim
Mohanad A Ibrahim
MAMohamed B. Al-Fageeh
Mohamed B. Al-Fageeh
Microsatellites or simple sequence repeats (SSRs) are among the genetic markers most widely utilized in research. This includes applications in numerous fields such as genetic conservation, paternity testing, and molecular breeding. Though ordered draft genome assemblies of camels have been announced, including for the Arabian camel, systemic analysis of camel SSRs is still limited. The identification and development of informative and robust molecular SSR markers are essential for marker assisted breeding programs and paternity testing. Here we searched and compared perfect SSRs with 1–6 bp nucleotide motifs to characterize microsatellites for draft genome sequences of the Camelidae. We analyzed and compared the occurrence, relative abundance, relative density, and guanine-cytosine (GC) content in four taxonomically different camelid species:Camelus dromedarius,C. bactrianus,C. ferus, andVicugna pacos. A total of 546762, 544494, 547974, and 437815 SSRs were mined, respectively. Mononucleotide SSRs were the most frequent in the four genomes, followed in descending order by di-, tetra-, tri-, penta-, and hexanucleotide SSRs. GC content was highest in dinucleotide SSRs and lowest in mononucleotide SSRs. Our results provide further evidence that SSRs are more abundant in noncoding regions than in coding regions. Similar distributions of microsatellites were found in all four species, which indicates that the pattern of microsatellites is conserved in family Camelidae.

29 December 2017 in PLOS ONE
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Journal Article
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Manee ManeeManee Manee
Manee Manee
SASultan Alharbi
Sultan Alharbi
AAAbdulmalek T Algarni
Abdulmalek T Algarni
WAWaleed M Alghamdi
Waleed M Alghamdi
MAMusaad A Altammami
Musaad A Altammami
BABasel M Alnafjan
Basel M Alnafjan
Small heat shock protein beta-1 (HSPB-1) plays an essential role in the protection of cells against environmental stress.Elucidation of its molecular, structural, and biological characteristics in a naturally wild-type model is essential. Although the sequence information of the HSPB-1 gene is available for many mammalian species, the HSPB-1 gene of Arabian camel (Arabian camel HSPB-1) has not yet been structurally characterized. We cloned and functionally characterized a full-length of Arabian camel HSPB-1 cDNA. It is 791 bp long, with a 5′-untranslated region (UTR) of 34 bp, a 3′-UTR of 151 bp with a poly(A) tail, and an open reading frame (ORF) of 606 bp encoding a protein of 201 amino acids (accession number: MF278354). The tissue-specific expression analysis of Arabian camel HSPB-1 mRNA was examined using quantitative real-time PCR (qRT-PCR); which suggested that Arabian camel HSPB-1 mRNA was constitutionally expressed in all examined tissues of Arabian camel, with the predominately level in the esophagus tissue. Peptide mass fingerprint-mass spectrometry (PMF-MS) analysis of the purified Arabian camel HSPB-1 protein confirmed the identity of this protein. Phylogenetic analysis showed that the HSPB-1 protein of Arabian camel is grouped together with those of Bactrian camel and Alpaca. Comparing the modelled 3D structure of Arabian camel HSPB-1 protein with the available protein 3D structure of HSPB-1 from human confirmed the presence of α-crystallin domain, and high similarities were noted between the two structures by using super secondary structure prediction.

27 June 2026 in Pharmaceutics
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HAHadi Alasmari
Hadi Alasmari
SAShouq Fahad Alghannam
Shouq Fahad Alghannam
HAHassan Almoammar
Hassan Almoammar
DADimah K Alrabiah
Dimah K Alrabiah
SASeham Alharthy
Seham Alharthy
AAAhmad Mohammad Aldossary
Ahmad Mohammad Aldossary
Ribonucleic acid-based vaccines have emerged as one of the most significant advances in modern vaccine development, demonstrating remarkable clinical success and enabling rapid responses to emerging infectious diseases. Despite their therapeutic potential, the development of these vaccines remains challenging because of the inherent instability of ribonucleic acid molecules, their susceptibility to degradation, and the complexity of formulation design. Ensuring product quality, stability, and biological performance therefore requires comprehensive analytical characterization throughout development, manufacturing, storage, and quality control. This review provides a comprehensive overview of current analytical strategies used to evaluate ribonucleic acid-based vaccine formulations. Key analytical approaches for assessing molecular integrity, purity, encapsulation efficiency, particle morphology, size distribution, surface characteristics, structural attributes, and biological potency are discussed. The review also examines the influence of formulation composition, lipid nanoparticle design, manufacturing processes, and storage conditions on vaccine stability and performance. In addition, major degradation pathways, critical quality attributes, and analytical challenges associated with quality assessment are highlighted. Furthermore, current regulatory considerations and limitations of existing analytical methodologies are discussed, particularly the challenges associated with establishing robust relationships between physicochemical properties and biological efficacy. The review emphasizes the importance of integrated multi-method analytical approaches for comprehensive characterization and quality assurance. Continued advances in analytical technologies and standardization efforts will be essential for supporting the development of safe, effective, and stable ribonucleic acid-based vaccines and for facilitating their broader pharmaceutical applications.