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<Article>
<Journal>
				<PublisherName>Shiraz University Press</PublisherName>
				<JournalTitle>Molecular Biology Research Communications</JournalTitle>
				<Issn>2322-181X</Issn>
				<Volume>3</Volume>
				<Issue>4</Issue>
				<PubDate PubStatus="epublish">
					<Year>2014</Year>
					<Month>12</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>Identification and characterization of major histocompatibility complex class IIB alleles from three species of European ranid frogs</ArticleTitle>
<VernacularTitle></VernacularTitle>
			<FirstPage>215</FirstPage>
			<LastPage>222</LastPage>
			<ELocationID EIdType="pii">2486</ELocationID>
			
<ELocationID EIdType="doi">10.22099/mbrc.2014.2486</ELocationID>
			
			<Language>EN</Language>
<AuthorList>
<Author>
					<FirstName>Béla</FirstName>
					<LastName>A. Marosi</LastName>
<Affiliation>Department of Parasitology, University of Agricultural Science and Veterinary Medicine, Mănăștur Street nr. 3-5, RO-400372 Cluj-Napoca, Romania</Affiliation>

</Author>
<Author>
					<FirstName>Karen</FirstName>
					<LastName>M. Kiemnec-Tyburczy</LastName>
<Affiliation>Department of Biological Sciences, Humboldt State University 95521 USA</Affiliation>

</Author>
<Author>
					<FirstName>Ioan</FirstName>
					<LastName>V. Ghira</LastName>
<Affiliation>Faculty of Biology and Geology, Babes-Bolyai-University Cluj-Napoca, Clinicilor street 5-7, RO-400006 Cluj-Napoca, Romania</Affiliation>

</Author>
<Author>
					<FirstName>Tibor</FirstName>
					<LastName>Sos</LastName>
<Affiliation>Association for Bird and Nature Protection &amp;ldquo;Milvus Group&amp;rdquo;, Targu Mures, 22 Crinului Street, RO-540343</Affiliation>

</Author>
<Author>
					<FirstName>Octavian</FirstName>
					<LastName>Popescu</LastName>
<Affiliation>Molecular Biology Center, Interdisciplinary Research Institute on Bio-Nano-Sciences, Babes-Bolyai University Cluj-Napoca, 42 Treboniu Laurian Street, RO-400271 Cluj-Napoca, Romania</Affiliation>

</Author>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
			<History>
				<PubDate PubStatus="received">
					<Year>2014</Year>
					<Month>07</Month>
					<Day>15</Day>
				</PubDate>
			</History>
		<Abstract>Immune genes of the major histocompatibility complex (MHC) are among the most polymorphic genes in the vertebrate genome. Due to their polymorphic nature, they are often used to assess the adaptive genetic variability of natural populations. This study describes the first molecular characterization of 13 partial MHC class IIB sequences from three European ranid frogs.  The utility of previously published primers was expanded by using them to successfully amplify eight exon 2 alleles from &lt;em&gt;Rana arvalis&lt;/em&gt;.&lt;em&gt; &lt;/em&gt;We also designed a novel primer set that successfully amplified exon 2 from &lt;em&gt;Pelophylax kurtmuelleri&lt;/em&gt;. &lt;em&gt;Pelophylax lessonae&lt;/em&gt; was also designed as part of this study. Results indicate the presence of one or two class IIB loci in these three species. In &lt;em&gt;R. arvalis&lt;/em&gt;, significant evidence of positive selection acting on MHC antigen binding sites was found. Many European ranid populations are experiencing disease-related declines; the newly developed primers can, therefore, be used for further population analyses of native frogs.</Abstract>
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<ArchiveCopySource DocType="pdf">https://mbrc.shirazu.ac.ir/article_2486_8506b1334d9f2c95d43d0d9204ee6d62.pdf</ArchiveCopySource>
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<Article>
<Journal>
				<PublisherName>Shiraz University Press</PublisherName>
				<JournalTitle>Molecular Biology Research Communications</JournalTitle>
				<Issn>2322-181X</Issn>
				<Volume>3</Volume>
				<Issue>4</Issue>
				<PubDate PubStatus="epublish">
					<Year>2014</Year>
					<Month>12</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>Association of CAT C-262T and SOD1 A251G single nucleotide polymorphisms susceptible to gastric cancer</ArticleTitle>
<VernacularTitle></VernacularTitle>
			<FirstPage>223</FirstPage>
			<LastPage>229</LastPage>
			<ELocationID EIdType="pii">2490</ELocationID>
			
<ELocationID EIdType="doi">10.22099/mbrc.2014.2490</ELocationID>
			
			<Language>EN</Language>
<AuthorList>
<Author>
					<FirstName>Shiva</FirstName>
					<LastName>Ebrahimpour</LastName>
<Affiliation>Shiraz University</Affiliation>

</Author>
<Author>
					<FirstName>Iraj</FirstName>
					<LastName>Saadat</LastName>
<Affiliation>Department of Biology, College of Sciences, Shiraz University</Affiliation>

</Author>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
			<History>
				<PubDate PubStatus="received">
					<Year>2014</Year>
					<Month>10</Month>
					<Day>15</Day>
				</PubDate>
			</History>
		<Abstract>Oxidative stress is known to be one of the major factors involved in the development and progression of cancer. Oxidative stress can occur due to an imbalance between concentrations of reactive oxygen species and antioxidant capacities. Catalase (CAT; OMIM 115500) and superoxide dismutase 1 (SOD1; OMIM 147450) play important roles in the primary defense against oxidative stress. In the present study, we investigated possible associations between polymorphisms of &lt;em&gt;CAT &lt;/em&gt;C-262T (rs1001179) and &lt;em&gt;SOD1&lt;/em&gt; A251G (rs2070424) with susceptibility to gastric cancer. This case-control study included 160 gastric cancer patients and 241 age and gender frequency-matched healthy controls. Genotyping was done using PCR-RFLP based method. There were no significant differences in T allele frequencies in patients as compared to the controls in the &lt;em&gt;CAT&lt;/em&gt; C-262T polymorphism (OR=0.80, 95% CI: 0.52- 1.23, P=0.304). Subjects with AG (OR=0.47, 95% CI: 0.24-0.91, P=0.026) or AG+GG (OR=0.45, 95% CI: 0.23-0.88, P=0.021) genotypes of the rs2070424 polymorphism were at lower risks of developing gastric cancer in comparison with the AA genotype. Our findings showed that there was no significant association between &lt;em&gt;CAT&lt;/em&gt; C-262T polymorphism and gastric cancer susceptibility. However, we found that the G allele of the &lt;em&gt;SOD1&lt;/em&gt; A251G polymorphism has protective effects against the risk of gastric cancer.</Abstract>
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			<Param Name="value">Gastric cancer</Param>
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			<Object Type="keyword">
			<Param Name="value">Genetic polymorphism</Param>
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			<Param Name="value">Oxidative stress</Param>
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			<Param Name="value">SOD1</Param>
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<ArchiveCopySource DocType="pdf">https://mbrc.shirazu.ac.ir/article_2490_4278d151cee906f62d914711aed3caed.pdf</ArchiveCopySource>
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<Article>
<Journal>
				<PublisherName>Shiraz University Press</PublisherName>
				<JournalTitle>Molecular Biology Research Communications</JournalTitle>
				<Issn>2322-181X</Issn>
				<Volume>3</Volume>
				<Issue>4</Issue>
				<PubDate PubStatus="epublish">
					<Year>2014</Year>
					<Month>12</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>Molecular characterization of Myxobolus cuttacki (Myxozoa, Myxosporea, Bivalvulida) infecting gill lamellae of minor carp Labeo bata (Ham.)</ArticleTitle>
<VernacularTitle></VernacularTitle>
			<FirstPage>231</FirstPage>
			<LastPage>239</LastPage>
			<ELocationID EIdType="pii">2493</ELocationID>
			
<ELocationID EIdType="doi">10.22099/mbrc.2014.2493</ELocationID>
			
			<Language>EN</Language>
<AuthorList>
<Author>
					<FirstName>Sandya Chinna</FirstName>
					<LastName>Rajesh</LastName>
<Affiliation>Department of Aquatic Animal Health, Faculty of Fishery Sciences, West Bengal University of Animal and Fishery Sciences, Kolkata</Affiliation>

</Author>
<Author>
					<FirstName>Sayani</FirstName>
					<LastName>Banerjee</LastName>
<Affiliation>Department of Aquatic Animal Health, Faculty of Fishery Sciences, WBUAFS, Kolkata</Affiliation>

</Author>
<Author>
					<FirstName>Avijit</FirstName>
					<LastName>Patra</LastName>
<Affiliation>Department of Aquatic Animal Health, Faculty of Fishery Sciences, WBUAFS, Kolkata</Affiliation>

</Author>
<Author>
					<FirstName>Gadadhar</FirstName>
					<LastName>Dash</LastName>
<Affiliation>Department of Aquatic Animal Health, Faculty of Fishery Sciences, WBUAFS, Kolkata</Affiliation>

</Author>
<Author>
					<FirstName>Thangapalam</FirstName>
					<LastName>Abraham</LastName>
<Affiliation>Department of Aquatic Animal Health, Faculty of Fishery Sciences, West Bengal University of Animal and Fishery Sciences, Chakgaria, Kolkata - 700 094, West Bengal, India</Affiliation>

</Author>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
			<History>
				<PubDate PubStatus="received">
					<Year>2014</Year>
					<Month>09</Month>
					<Day>21</Day>
				</PubDate>
			</History>
		<Abstract>As new pathogenic strains are emerging and threatening aquaculture development, myxosporeans (Myxozoa) are receiving much attention in recent years. Myxosporean taxonomy is traditionally based on morphology of the myxospore stage. Molecular data on Indian myxosporeans are rare. In this report, the 18S rRNA gene sequence of Myxobolus cuttacki infecting gill lamellae of minor carp &lt;em&gt;Labeo bata&lt;/em&gt; (Ham.) and its phylogenetic relationship with other myxobolids are described for the first time. The plasmodia of &lt;em&gt;M. cuttacki&lt;/em&gt; were 0.5-0.9 mm in size and whitish with a round to oval shape. The mean mature spore size was 16.10×7.05 μm. The 18S rRNA nucleotide sequence with 1703 bp of &lt;em&gt;M. cuttacki&lt;/em&gt; (accession number KF465682) clustered phylogenetically with other &lt;em&gt;Myxobolus&lt;/em&gt; spp. infecting cyprinid gills with 78-90% homogeneity. The gill lamellae infecting &lt;em&gt;M. catmrigalae&lt;/em&gt; (KC933944) and &lt;em&gt;M. orissae&lt;/em&gt; (KF448527) of Indian major carp &lt;em&gt;Cirrhinus mrigala&lt;/em&gt; from India, exhibited 86% and 81% homogeneity with &lt;em&gt;M. cuttacki&lt;/em&gt;, respectively. The infection rate was low to moderate on the gills which can have a negative impact on respiratory and physiological functions and subsequently on fish production.  </Abstract>
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			<Object Type="keyword">
			<Param Name="value">Myxobolus cuttacki</Param>
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			<Param Name="value">18S rRNA</Param>
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			<Object Type="keyword">
			<Param Name="value">Phylogenetic relationship</Param>
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<ArchiveCopySource DocType="pdf">https://mbrc.shirazu.ac.ir/article_2493_984c1cc375f528f24f37c3c7a03628cd.pdf</ArchiveCopySource>
</Article>

<Article>
<Journal>
				<PublisherName>Shiraz University Press</PublisherName>
				<JournalTitle>Molecular Biology Research Communications</JournalTitle>
				<Issn>2322-181X</Issn>
				<Volume>3</Volume>
				<Issue>4</Issue>
				<PubDate PubStatus="epublish">
					<Year>2014</Year>
					<Month>12</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>Differential expression of BnSRK2D gene in two Brassica napus cultivars under water deficit stress</ArticleTitle>
<VernacularTitle></VernacularTitle>
			<FirstPage>241</FirstPage>
			<LastPage>251</LastPage>
			<ELocationID EIdType="pii">2494</ELocationID>
			
<ELocationID EIdType="doi">10.22099/mbrc.2014.2494</ELocationID>
			
			<Language>EN</Language>
<AuthorList>
<Author>
					<FirstName>Bahlanes</FirstName>
					<LastName>Bakhtari</LastName>
<Affiliation>Department of Crop Production and Plant Breeding, College of Agriculture, Shiraz University, Shiraz, Iran</Affiliation>

</Author>
<Author>
					<FirstName>Hooman</FirstName>
					<LastName>Razi</LastName>
<Affiliation>Department of Crop Production and Plant Breeding, College of Agriculture, Shiraz University</Affiliation>

</Author>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
			<History>
				<PubDate PubStatus="received">
					<Year>2014</Year>
					<Month>10</Month>
					<Day>07</Day>
				</PubDate>
			</History>
		<Abstract>The sucrose non-fermenting 1-related protein kinase 2 (SnRK2) family members are plant unique serine/threonine kinases which play a key role in cellular signaling in response to abiotic stresses. The three SnRK2 members including SRK2D, SRK2I and SRK2E are known to phosphorylate major abscisic acid (ABA) responsive transcription factors, ABF2 and ABF4, involved in an ABA-dependent stress signaling pathway in Arabidopsis. This study aimed to clone and sequence an ortholog of the Arabidopsis &lt;em&gt;SRK2D&lt;/em&gt; gene from &lt;em&gt;Brassica napus&lt;/em&gt;, designated as BnSRK2D. An 833bp cDNA fragment of &lt;em&gt;BnSRK2D&lt;/em&gt;, which shared high amino acid sequence identity with its Arabidopsis counterpart, was obtained suggesting a possible conserved function for these genes. The expression pattern of &lt;em&gt;BnSRK2D&lt;/em&gt; and its potential target gene &lt;em&gt;B. napus&lt;/em&gt; ABF2 (&lt;em&gt;BnABF2&lt;/em&gt;) were then analyzed in the two cultivars with contrasting reaction to water deficit stress. Semi-quantitative reverse transcription polymerase chain reaction (RT-PCR) showed that &lt;em&gt;BnSRK2D&lt;/em&gt; and &lt;em&gt;BnABF2&lt;/em&gt; were water-deficit stress responsive genes with similar expression profiles. The accumulation of the &lt;em&gt;BnSRK2D&lt;/em&gt; and &lt;em&gt;BnABF2&lt;/em&gt; transcripts in the two cultivars was linked with their level of drought tolerance, as the drought tolerant cultivar had significantly higher expression levels of both genes under normal and water deficit stress conditions. These findings suggest that &lt;em&gt;BnSRK2D&lt;/em&gt; and &lt;em&gt;BnABF2&lt;/em&gt; genes may be involved in conferring drought tolerance in &lt;em&gt;B. napus&lt;/em&gt;.</Abstract>
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			<Param Name="value">Rapeseed</Param>
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			<Object Type="keyword">
			<Param Name="value">SnRK2</Param>
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			<Object Type="keyword">
			<Param Name="value">BnABF2</Param>
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			<Param Name="value">Drought tolerance</Param>
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			<Param Name="value">Transcript accumulation</Param>
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<ArchiveCopySource DocType="pdf">https://mbrc.shirazu.ac.ir/article_2494_9ec56ede547cef850b2f64c31b10e72c.pdf</ArchiveCopySource>
</Article>

<Article>
<Journal>
				<PublisherName>Shiraz University Press</PublisherName>
				<JournalTitle>Molecular Biology Research Communications</JournalTitle>
				<Issn>2322-181X</Issn>
				<Volume>3</Volume>
				<Issue>4</Issue>
				<PubDate PubStatus="epublish">
					<Year>2014</Year>
					<Month>12</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>Resistance mechanism of human immunodeficiency virus type-1 protease to inhibitors: A molecular dynamic approach</ArticleTitle>
<VernacularTitle></VernacularTitle>
			<FirstPage>253</FirstPage>
			<LastPage>267</LastPage>
			<ELocationID EIdType="pii">2510</ELocationID>
			
<ELocationID EIdType="doi">10.22099/mbrc.2014.2510</ELocationID>
			
			<Language>EN</Language>
<AuthorList>
<Author>
					<FirstName>Mohammad Reza</FirstName>
					<LastName>Dayer</LastName>
<Affiliation>Department of Biology, Faculty of Science, Shahid Chamran University, Ahvaz, Iran</Affiliation>

</Author>
<Author>
					<FirstName>Mohammad Saaid</FirstName>
					<LastName>Dayer</LastName>
<Affiliation>Department of Parasitology and Medical Entomology, Tarbiat Modares University, Tehran</Affiliation>

</Author>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
			<History>
				<PubDate PubStatus="received">
					<Year>2014</Year>
					<Month>09</Month>
					<Day>21</Day>
				</PubDate>
			</History>
		<Abstract>Human immunodeficiency virus type 1 (HIV-1) protease inhibitors comprise an important class of drugs used in HIV treatments. However, mutations of protease genes accelerated by low fidelity of reverse transcriptase yield drug resistant mutants of reduced affinities for the inhibitors. This problem is considered to be a serious barrier against HIV treatment for the foreseeable future. In this study, molecular dynamic simulation method was used to examine the combinational and additive effects of all known mutations involved in drug resistance against FDA approved inhibitors. Results showed that drug resistant mutations are not randomly distributed along the protease sequence; instead, they are localized on flexible or hot points of the protein chain.  Substitution of more hydrophobic residues in flexible points of protease chains tends to increase the folding, lower the flexibility and decrease the active site area of the protease. The reduced affinities of HIV-1 protease for inhibitors seemed to be due to substantial decrease in the size of the active site and flap mobility. A correlation was found between the binding energy of inhibitors and their affinities for each mutant suggesting the distortion of the active site geometry in drug resistance by preventing effective fitting of inhibitors into the enzymes&#039; active site. To overcome the problem of drug resistance of HIV-1 protease, designing inhibitors of variable functional groups and configurations is proposed.</Abstract>
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			<Param Name="value">HIV-1 Protease</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">Inhibitors</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">AIDS Treatment</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">Drug Resistance</Param>
			</Object>
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<ArchiveCopySource DocType="pdf">https://mbrc.shirazu.ac.ir/article_2510_0b8642cdf2649d00b6db556491f4e238.pdf</ArchiveCopySource>
</Article>

<Article>
<Journal>
				<PublisherName>Shiraz University Press</PublisherName>
				<JournalTitle>Molecular Biology Research Communications</JournalTitle>
				<Issn>2322-181X</Issn>
				<Volume>3</Volume>
				<Issue>4</Issue>
				<PubDate PubStatus="epublish">
					<Year>2014</Year>
					<Month>12</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>Effect of endurance training and cinnamon supplementation on post-exercise oxidative responses in rats</ArticleTitle>
<VernacularTitle></VernacularTitle>
			<FirstPage>269</FirstPage>
			<LastPage>281</LastPage>
			<ELocationID EIdType="pii">2723</ELocationID>
			
<ELocationID EIdType="doi">10.22099/mbrc.2014.2723</ELocationID>
			
			<Language>EN</Language>
<AuthorList>
<Author>
					<FirstName>Gholamreza</FirstName>
					<LastName>Dehghan</LastName>
<Affiliation>Department of Biology, Faculty of Natural Science, University of Tabriz, Tabriz, Iran</Affiliation>

</Author>
<Author>
					<FirstName>Mehrnoosh</FirstName>
					<LastName>Shaghaghi</LastName>
<Affiliation>Department of Biology, Faculty of Basic Science,  Payamenoor University, Tehran, Iran.</Affiliation>

</Author>
<Author>
					<FirstName>Afshar</FirstName>
					<LastName>Jafari</LastName>
<Affiliation>Department of Sports Physiology, Faculty of Physical Education and Sports Sciences, University of Tabriz, Tabriz, Iran</Affiliation>

</Author>
<Author>
					<FirstName>Mustafa</FirstName>
					<LastName>Mohammadi</LastName>
<Affiliation>Department of Physiology, Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran</Affiliation>

</Author>
<Author>
					<FirstName>Reza</FirstName>
					<LastName>Badalzadeh</LastName>
<Affiliation>Department of Physiology, Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran</Affiliation>

</Author>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
			<History>
				<PubDate PubStatus="received">
					<Year>2014</Year>
					<Month>01</Month>
					<Day>02</Day>
				</PubDate>
			</History>
		<Abstract>Despite the preventative and therapeutic effects of regular exercise, exhaustive exercise may be harmful to health. The present study aimed to determine the protective effect of endurance training and cinnamon bark extract (CBE) supplementation on oxidative responses induced by an exhaustive exercise schedule in rats. The rats were randomly divided into the following five groups of 6; control sedentary (Con/Sed), control exercised (Con/Ex), trained exercised (Tr/Ex), supplemented exercised (Sup/Ex), and trained, supplemented and exercised (Tr/Sup/Ex). Animals in exercise groups ran on a rodent treadmill for an 8-week endurance training program. At the end of the experiment, blood samples were collected and (MDA) and total thiol (TT) levels were measured in plasma. Glutathione peroxidase (GPX), superoxide dismutase (SOD), and catalase (CAT) activities were determined in soleus muscles. Results showed significant increases in SOD activity and malondealdehyde (MDA) levels in the soleus muscles and serum of exercised rats fed with the normal diet. The exhaustive exercise also induced a decrease in serum total thiol level and GPX activity. Elevated levels of total thiol and total antioxidant capacity (TAC) and reduced serum MDA levels were found in the Sup/Ex and Tr/Sup/Ex groups. CAT and GPX activities increased by CBE treatment in trained rats. Regular training increased CAT and GPX activities in the Tr/Sup/Ex group. CAT, GPX and SOD activities were not affected by the CBE treatment in untrained rats. Results suggest that additional use of regular training and CBE supplementation increase TAC and protect healthy male rats against oxidative damage induced by exhaustive exercise. </Abstract>
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			<Param Name="value">Oxidative stress</Param>
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			<Param Name="value">exhaustive exercise</Param>
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			<Param Name="value">lipid peroxidation</Param>
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<ArchiveCopySource DocType="pdf">https://mbrc.shirazu.ac.ir/article_2723_9bbcc8a46719a1989542faaecdeb4d1f.pdf</ArchiveCopySource>
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