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  1. Article: MicroRNA, Proteins, and Metabolites as Novel Biomarkers for Prediabetes, Diabetes, and Related Complications.

    Vaishya, Suniti / Sarwade, Rucha D / Seshadri, Vasudevan

    Frontiers in endocrinology

    2018  Volume 9, Page(s) 180

    Abstract: Type 2 diabetes mellitus (T2DM) is no more a lifestyle disease of developed countries. It has emerged as a major health problem worldwide including developing countries. However, how diabetes could be detected at an early stage (prediabetes) to prevent ... ...

    Abstract Type 2 diabetes mellitus (T2DM) is no more a lifestyle disease of developed countries. It has emerged as a major health problem worldwide including developing countries. However, how diabetes could be detected at an early stage (prediabetes) to prevent the progression of disease is still unclear. Currently used biomarkers like glycated hemoglobin and assessment of blood glucose level have their own limitations. These classical markers can be detected when the disease is already established. Prognosis of disease at early stages and prediction of population at a higher risk require identification of specific markers that are sensitive enough to be detected at early stages of disease. Biomarkers which could predict the risk of disease in people will be useful for developing preventive/proactive therapies to those individuals who are at a higher risk of developing the disease. Recent studies suggested that the expression of biomolecules including microRNAs, proteins, and metabolites specifically change during the progression of T2DM and related complications, suggestive of disease pathology. Owing to their omnipresence in body fluids and their association with onset, progression, and pathogenesis of T2DM, these biomolecules can be potential biomarker for prognosis, diagnosis, and management of disease. In this article, we summarize biomolecules that could be potential biomarkers and their signature changes associated with T2DM and related complications during disease pathogenesis.
    Language English
    Publishing date 2018-04-23
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2592084-4
    ISSN 1664-2392
    ISSN 1664-2392
    DOI 10.3389/fendo.2018.00180
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Translation in Organelles of Apicomplexan Parasites.

    Habib, Saman / Vaishya, Suniti / Gupta, Kirti

    Trends in parasitology

    2016  Volume 32, Issue 12, Page(s) 939–952

    Abstract: The protein translation machineries of the apicoplast and mitochondrion-the two actively translating organelles of apicomplexan parasites-have potential sites for drug intervention against diseases caused by these organisms. Work in the past few years, ... ...

    Abstract The protein translation machineries of the apicoplast and mitochondrion-the two actively translating organelles of apicomplexan parasites-have potential sites for drug intervention against diseases caused by these organisms. Work in the past few years, particularly on Plasmodium falciparum and Toxoplasma gondii, has shown that a reduced machinery of enzymes and factors is sufficient for organellar translation, which is also supported by components shared with the cytosolic translation system. This interplay between eukaryotic and prokaryotic-like components for mRNA translation in organelles is reviewed here. We also discuss functional and structural aspects of factors mediating initiation, elongation, and termination of polypeptides, and recycling of the reduced ribosomes of the apicoplast and mitochondrion.
    MeSH term(s) Animals ; Apicomplexa/genetics ; Apicoplasts/genetics ; Drug Delivery Systems ; Humans ; Mitochondria/genetics ; Protein Biosynthesis ; Protozoan Infections/drug therapy ; Protozoan Infections/parasitology ; RNA, Protozoan/genetics
    Chemical Substances RNA, Protozoan
    Language English
    Publishing date 2016
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2036227-4
    ISSN 1471-5007 ; 1471-4922
    ISSN (online) 1471-5007
    ISSN 1471-4922
    DOI 10.1016/j.pt.2016.07.005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Translation in Organelles of Apicomplexan Parasites

    Habib, Saman / Kirti Gupta / Suniti Vaishya

    Trends in parasitology. 2016 Dec., v. 32, no. 12

    2016  

    Abstract: The protein translation machineries of the apicoplast and mitochondrion–the two actively translating organelles of apicomplexan parasites–have potential sites for drug intervention against diseases caused by these organisms. Work in the past few years, ... ...

    Abstract The protein translation machineries of the apicoplast and mitochondrion–the two actively translating organelles of apicomplexan parasites–have potential sites for drug intervention against diseases caused by these organisms. Work in the past few years, particularly on Plasmodium falciparum and Toxoplasma gondii, has shown that a reduced machinery of enzymes and factors is sufficient for organellar translation, which is also supported by components shared with the cytosolic translation system. This interplay between eukaryotic and prokaryotic-like components for mRNA translation in organelles is reviewed here. We also discuss functional and structural aspects of factors mediating initiation, elongation, and termination of polypeptides, and recycling of the reduced ribosomes of the apicoplast and mitochondrion.
    Keywords drugs ; enzymes ; messenger RNA ; mitochondria ; Plasmodium falciparum ; polypeptides ; ribosomes ; Toxoplasma gondii
    Language English
    Dates of publication 2016-12
    Size p. 939-952.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 2036227-4
    ISSN 1471-5007 ; 1471-4922
    ISSN (online) 1471-5007
    ISSN 1471-4922
    DOI 10.1016/j.pt.2016.07.005
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  4. Article ; Online: Polypeptide release factors and stop codon recognition in the apicoplast and mitochondrion of Plasmodium falciparum.

    Vaishya, Suniti / Kumar, Vikash / Gupta, Ankit / Siddiqi, Mohammad Imran / Habib, Saman

    Molecular microbiology

    2016  Volume 100, Issue 6, Page(s) 1080–1095

    Abstract: Correct termination of protein synthesis would be a critical step in translation of organellar open reading frames (ORFs) of the apicoplast and mitochondrion of the malaria parasite. We identify release factors (RFs) responsible for recognition of the ... ...

    Abstract Correct termination of protein synthesis would be a critical step in translation of organellar open reading frames (ORFs) of the apicoplast and mitochondrion of the malaria parasite. We identify release factors (RFs) responsible for recognition of the UAA and UGA stop-codons of apicoplast ORFs and the sole UAA stop-codon that terminates translation from the three mitochondrial ORFs. A single nuclear-encoded canonical RF2, PfRF2Api , localizes to the apicoplast. It has a conserved tripeptide motif (SPF) for stop-codon recognition and is sufficient for peptidyl-tRNA hydrolysis (PTH) from both UAA and UGA. Two RF family proteins are targeted to the parasite mitochondrion; a canonical RF1, PfRF1Mit , with a variant codon-recognition motif (PxN instead of the conserved RF1 PxT) is the major peptidyl-hydrolase with specific recognition of the UAA codon relevant to mitochondrial ORFs. Mutation of the N residue of the PfRF1Mit PxN motif and two other conserved residues of the codon recognition domain lowers PTH activity from pre-termination ribosomes indicating their role in codon-recognition. The second RF imported by the mitochondrion is the non-canonical PfICT1 that functions as a dimer and mediates codon nonspecific peptide release. Our results help delineate a critical step in organellar translation in Plasmodium, which is an important target for anti-malarials.
    MeSH term(s) Apicoplasts/genetics ; Apicoplasts/metabolism ; Codon, Terminator ; Erythrocytes/parasitology ; Humans ; Mitochondria/genetics ; Mitochondria/metabolism ; Models, Molecular ; Mutation ; Peptide Termination Factors/genetics ; Peptide Termination Factors/metabolism ; Plasmodium falciparum/genetics ; Plasmodium falciparum/metabolism ; RNA, Transfer, Amino Acyl/genetics ; RNA, Transfer, Amino Acyl/metabolism ; Ribosomes/metabolism
    Chemical Substances Codon, Terminator ; Peptide Termination Factors ; RNA, Transfer, Amino Acyl ; tRNA, peptidyl-
    Language English
    Publishing date 2016-06
    Publishing country England
    Document type Journal Article
    ZDB-ID 619315-8
    ISSN 1365-2958 ; 0950-382X
    ISSN (online) 1365-2958
    ISSN 0950-382X
    DOI 10.1111/mmi.13369
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Dehydroascorbate-derivatized chitosan particles for targeting antimalarial agents to infected erythrocytes.

    Shafi, Hasham / Reddy, D V Siva / Khan, Tabassum / Ranjan, Rajeev / Srivastava, Ashish / Vaishya, Suniti / Sharma, Tanuj / Siddiqui, Mohammad Imran / Habib, Saman / Misra, Amit

    International journal of pharmaceutics

    2017  Volume 524, Issue 1-2, Page(s) 205–214

    Abstract: The mammalian glucose transporter GLUT-1 and Plasmodium falciparum hexose transporter PfHT1 are overexpressed on human RBC infected with the parasite (iRBC), presumably for enhanced glucose uptake. Dehydroascorbic acid (DHA) competes out glucose in GLUT- ... ...

    Abstract The mammalian glucose transporter GLUT-1 and Plasmodium falciparum hexose transporter PfHT1 are overexpressed on human RBC infected with the parasite (iRBC), presumably for enhanced glucose uptake. Dehydroascorbic acid (DHA) competes out glucose in GLUT-1 binding. We prepared particles containing chloroquine phosphate using novel derivatives of chitosan (CSN). CSN was either pre-derivatized with DHA (PRE) or particles made of CSN were derivatized by surface-grafting DHA (POST). The optimized formulations were analyzed for size (170-200nm) drug content (about 40%) entrapment efficiency (50-57%), in vitro drug release (80% in 72h, Higuchi's model), hemolysis on exposure to whole blood or RBC at 5% hematocrit, cytotoxicity towards cultured HEK 293T (kidney) and HepG2 (hepatic) cells, targeting iRBC and in vitro efficacy against P. falciparum. PRE particles were superior to POST CSN particles in terms of uptake and extent of preferential targeting to iRBCs than RBCs. Unlike starch particles reported earlier, dextrose did not competitively inhibit uptake of DHA-derivatized CSN particles. Both formulations significantly induced parasite inhibition at 1nM while free drug showed comparable activity at 100nM. Both PRE and POST particles were superior to free drug in efficacy. Targeting with high efficiency promises dose reduction and possibility of overcoming efflux-based drug resistance.
    Language English
    Publishing date 2017-05-30
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 428962-6
    ISSN 1873-3476 ; 0378-5173
    ISSN (online) 1873-3476
    ISSN 0378-5173
    DOI 10.1016/j.ijpharm.2017.03.088
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: The effect of fusidic acid on Plasmodium falciparum elongation factor G (EF-G).

    Gupta, Ankit / Mir, Snober S / Saqib, Uzma / Biswas, Subir / Vaishya, Suniti / Srivastava, Kumkum / Siddiqi, Mohammad Imran / Habib, Saman

    Molecular and biochemical parasitology

    2013  Volume 192, Issue 1-2, Page(s) 39–48

    Abstract: Inhibition of growth of the malaria parasite Plasmodium falciparum by known translation-inhibitory antibiotics has generated interest in understanding their action on the translation apparatus of the two genome containing organelles of the malaria ... ...

    Abstract Inhibition of growth of the malaria parasite Plasmodium falciparum by known translation-inhibitory antibiotics has generated interest in understanding their action on the translation apparatus of the two genome containing organelles of the malaria parasite: the mitochondrion and the relic plastid (apicoplast). We report GTPase activity of recombinant EF-G proteins that are targeted to the organelles and further use these to test the effect of the EF-G inhibitor fusidic acid (FA) on the factor-ribosome interface. Our results monitoring locking of EF-G·GDP onto surrogate Escherichia coli ribosomes as well as multi-turnover GTP hydrolysis by the factor indicate that FA has a greater effect on apicoplast EF-G compared to the mitochondrial counterpart. Deletion of a three amino acid (GVG) sequence in the switch I loop that is conserved in proteins of the mitochondrial EF-G1 family and the Plasmodium mitochondrial factor, but is absent in apicoplast EF-G, demonstrated that this motif contributes to differential inhibition of the two EF-Gs by FA. Additionally, the drug thiostrepton, that is known to target the apicoplast and proteasome, enhanced retention of only mitochondrial EF-G on ribosomes providing support for the reported effect of the drug on parasite mitochondrial translation.
    MeSH term(s) Amino Acid Sequence ; Binding Sites ; Fusidic Acid/chemistry ; Fusidic Acid/pharmacology ; Guanosine Triphosphate/chemistry ; Guanosine Triphosphate/metabolism ; Hydrolysis ; Mitochondria/metabolism ; Models, Molecular ; Molecular Conformation ; Molecular Sequence Data ; Mutagenesis, Insertional ; Peptide Elongation Factor G/antagonists & inhibitors ; Peptide Elongation Factor G/chemistry ; Peptide Elongation Factor G/genetics ; Peptide Elongation Factor G/metabolism ; Plasmodium falciparum/drug effects ; Plasmodium falciparum/physiology ; Protein Binding ; Protein Biosynthesis/drug effects ; Protein Conformation ; Sequence Alignment
    Chemical Substances Peptide Elongation Factor G ; Fusidic Acid (59XE10C19C) ; Guanosine Triphosphate (86-01-1)
    Language English
    Publishing date 2013-11
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 756166-0
    ISSN 1872-9428 ; 0166-6851
    ISSN (online) 1872-9428
    ISSN 0166-6851
    DOI 10.1016/j.molbiopara.2013.10.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: The effect of fusidic acid on Plasmodium falciparum elongation factor G (EF-G)

    Gupta, Ankit / Mir, Snober S / Saqib, Uzma / Biswas, Subir / Vaishya, Suniti / Srivastava, Kumkum / Siddiqi, Mohammad Imran / Habib, Saman

    Molecular and biochemical parasitology. 2013 , v. 192, no. 1-2

    2013  

    Abstract: Inhibition of growth of the malaria parasite Plasmodium falciparum by known translation-inhibitory antibiotics has generated interest in understanding their action on the translation apparatus of the two genome containing organelles of the malaria ... ...

    Abstract Inhibition of growth of the malaria parasite Plasmodium falciparum by known translation-inhibitory antibiotics has generated interest in understanding their action on the translation apparatus of the two genome containing organelles of the malaria parasite: the mitochondrion and the relic plastid (apicoplast). We report GTPase activity of recombinant EF-G proteins that are targeted to the organelles and further use these to test the effect of the EF-G inhibitor fusidic acid (FA) on the factor–ribosome interface. Our results monitoring locking of EF-G·GDP onto surrogate Escherichia coli ribosomes as well as multi-turnover GTP hydrolysis by the factor indicate that FA has a greater effect on apicoplast EF-G compared to the mitochondrial counterpart. Deletion of a three amino acid (GVG) sequence in the switch I loop that is conserved in proteins of the mitochondrial EF-G1 family and the Plasmodium mitochondrial factor, but is absent in apicoplast EF-G, demonstrated that this motif contributes to differential inhibition of the two EF-Gs by FA. Additionally, the drug thiostrepton, that is known to target the apicoplast and proteasome, enhanced retention of only mitochondrial EF-G on ribosomes providing support for the reported effect of the drug on parasite mitochondrial translation.
    Keywords Escherichia coli ; Plasmodium falciparum ; amino acids ; drugs ; genome ; growth retardation ; guanosine triphosphate ; guanosinetriphosphatase ; hydrolysis ; malaria ; monitoring ; parasites ; parasitology ; proteasome endopeptidase complex ; proteins ; ribosomes ; thiostrepton ; translation (genetics)
    Language English
    Dates of publication 2013-11
    Size p. 39-48.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 756166-0
    ISSN 1872-9428 ; 0166-6851
    ISSN (online) 1872-9428
    ISSN 0166-6851
    DOI 10.1016/j.molbiopara.2013.10.003
    Database NAL-Catalogue (AGRICOLA)

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  8. Article: effect of fusidic acid on Plasmodium falciparum elongation factor G (EF-G)

    Gupta, Ankit / Mir, Snober S. / Saqib, Uzma / Biswas, Subir / Vaishya, Suniti / Srivastava, Kumkum / Siddiqi, Mohammad Imran / Habib, Saman

    Molecular and biochemical parasitology

    Volume v. 192,, Issue no. 1

    Abstract: Inhibition of growth of the malaria parasite Plasmodium falciparum by known translation-inhibitory antibiotics has generated interest in understanding their action on the translation apparatus of the two genome containing organelles of the malaria ... ...

    Abstract Inhibition of growth of the malaria parasite Plasmodium falciparum by known translation-inhibitory antibiotics has generated interest in understanding their action on the translation apparatus of the two genome containing organelles of the malaria parasite: the mitochondrion and the relic plastid (apicoplast). We report GTPase activity of recombinant EF-G proteins that are targeted to the organelles and further use these to test the effect of the EF-G inhibitor fusidic acid (FA) on the factor–ribosome interface. Our results monitoring locking of EF-G·GDP onto surrogate Escherichia coli ribosomes as well as multi-turnover GTP hydrolysis by the factor indicate that FA has a greater effect on apicoplast EF-G compared to the mitochondrial counterpart. Deletion of a three amino acid (GVG) sequence in the switch I loop that is conserved in proteins of the mitochondrial EF-G1 family and the Plasmodium mitochondrial factor, but is absent in apicoplast EF-G, demonstrated that this motif contributes to differential inhibition of the two EF-Gs by FA. Additionally, the drug thiostrepton, that is known to target the apicoplast and proteasome, enhanced retention of only mitochondrial EF-G on ribosomes providing support for the reported effect of the drug on parasite mitochondrial translation.
    Keywords monitoring ; parasites ; drugs ; parasitology ; hydrolysis ; guanosine triphosphate ; Plasmodium falciparum ; genome ; growth retardation ; ribosomes ; translation (genetics) ; proteasome endopeptidase complex ; amino acids ; malaria ; Escherichia coli ; guanosinetriphosphatase ; thiostrepton ; proteins
    Language English
    Document type Article
    ISSN 0166-6851
    Database AGRIS - International Information System for the Agricultural Sciences and Technology

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