Progesterone (P4) metabolism in dairy cattle can be manipulated by alterations in dry matter intake and diet composition. Our objectives were to determine the effects of grazing allowance and fat supplementation on P4 metabolism in lactating dairy cows. Forty mid- to late-lactation Holstein-Friesian dairy cows were used in a completely randomized block design, with a 2 × 2 factorial arrangement of treatments. Cows were assigned to receive 1 of 2 pasture allowances (ad libitum allowance [AL], 9.5 kg dry matter per day, or restricted allowance [R] 7 kg dry matter per day) and 1 of 2 fat supplementation treatments (750 g per day saturated fat [F] or no fat supplement [NF]). All cows received an additional 4 kg per day of concentrate. Grass dry matter intake (GDMI) was measured 5 wk after the initiation of dietary treatment. Cows were treated with prostaglandin F2α (PGF2α) to eliminate the endogenous source of P4, and two intravaginal progesterone-releasing devices (CIDR) were inserted into each ...

This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols using NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme binds bile acid with high affinity, and shows minimal 3-alpha-hydroxysteroid dehydrogenase activity. This gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14. Three transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Dec 2011 ...

Hydroxybutyrate (GHB) is an endogenous metabolite synthesized in the brain. There is strong evidence to suggest that GHB has an important role as a neurotransmitter or neuromodulator.. The human aldo-keto reductase AKR7A2 has been proposed previously to catalyze the NADPH-dependent reduction of succinic semialdehyde (SSA) to GHB in human brain. In this study we have used RNA interference to evaluate the role of AKR7A2 in GHB biosynthesis in human neuroblastoma SH-SY5Y cells. Quantitative reverse transcription-PCR analysis and immunoblotting revealed that short interfering RNA molecules directed against AKR7A2 led to a significant reduction in both AKR7A2 transcript and protein levels 72 h post-transfection. We have shown that reduced expression of AKR7A2 results in a 90% decrease in SSA reductase activity of cell extracts. Furthermore, we have shown using gas chromatography-mass spectrometry that a decrease in the level of AKR7A2 was paralleled with a significant reduction in intracellular GHB ...

trans-1,2-dihydrobenzene-1,2-diol dehydrogenase: rat liver cytosol enzyme also catalyzes 3alpha-hydroxysteroid dehydrogenase activity (EC 1.1.1.50); GenBank AH009074 (rat); RefSeq NM_001818 (human)

AKR1C3 - AKR1C3 (untagged)-Human aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II) (AKR1C3) available for purchase from OriGene - Your Gene Company.

Aldo-keto Reductase 1B10/AKR1B10 Proteins available through Novus Biologicals. Browse our Aldo-keto Reductase 1B10/AKR1B10 Protein catalog backed by our Guarantee+.

Aldo-keto Reductase 1C4/AKR1C4 Lysates available through Novus Biologicals. Browse our Aldo-keto Reductase 1C4/AKR1C4 Lysate catalog backed by our Guarantee+.

Weinstein, Y, 20alpha-hydroxysteroid Dehydrogenase. A t lymphocyte-associated enzyme. (1977). Subject Strain Bibliography 1977. 930 ...

From NCBI Gene:. This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols using NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme binds bile acid with high affinity, and shows minimal 3-alpha-hydroxysteroid dehydrogenase activity. This gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14. Three transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Dec 2011]. From UniProt: ...

AKR1A1 - AKR1A1 (Myc-DDK-tagged)-Human aldo-keto reductase family 1, member A1 (aldehyde reductase) (AKR1A1), transcript variant 1 available for purchase from OriGene - Your Gene Company.

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TY - JOUR. T1 - Identification of a renal-specific oxido-reductase in newborn diabetic mice. AU - Yang, Qiwei. AU - Dixit, Bharat. AU - Wada, Jun. AU - Tian, Yufeng. AU - Wallner, Elisabeth I.. AU - Srivastva, Satish K.. AU - Kanwar, Yashpal S.. PY - 2000/8/29. Y1 - 2000/8/29. N2 - Aldose reductase (ALR2), a NADPH-dependent aldo-keto reductase (AKR), is widely distributed in mammalian tissues and has been implicated in complications of diabetes, including diabetic nephropathy. To identify a renal-specific reductase belonging to the AKR family, representational difference analyses of cDNA from diabetic mouse kidney were performed. A full-length cDNA with an ORF of 855 nt and yielding a ≃ 1.5-kb mRNA transcript was isolated from a mouse kidney library. Human and rat homologues also were isolated, and they had ≃ 91% and ≃ 97% amino acid identity with mouse protein. In vitro translation of the cDNA yielded a protein product of ≃ 33 kDa. Northern and Western blot analyses, using the cDNA and ...

1J96: Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolution.

1MRQ: Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids.

3cv7: Structure of aldehyde reductase in ternary complex with coenzyme and the potent 20alpha-hydroxysteroid dehydrogenase inhibitor 3,5-dichlorosalicylic acid: implications for inhibitor binding and selectivity.

Mouse polyclonal antibody raised against a full-length human AKR1CL2 protein. AKR1CL2 (AAH02862.1, 1 a.a. ~ 307 a.a) full-length human protein. (H00083592-B01P) - Products - Abnova

TY - JOUR. T1 - Erratum to Expression of rat aldehyde reductase AKR7A1: influence of age and sex and tissue-specific inducibility [Biochemical Pharmacology V.62 (2001) 1511-1519]. AU - Grant, Anne W.. AU - Staffas, Louise. AU - Mankowitz, Louise. AU - Kelly, Vincent P.. AU - Manson, Margaret M.. AU - DePierre, Joseph W.. AU - Hayes, John D.. AU - Ellis, E.M.. N1 - This is an erratum to Strathprint ID http://strathprints.strath.ac.uk/23620/. PY - 2002/7/15. Y1 - 2002/7/15. N2 - This is an erratum to Expression of rat aldehyde reductase AKR7A1: influence of age and sex and tissue-specific inducibility published in Biochemical Pharmacology vol 62 (2001) pages 1511-1519.. AB - This is an erratum to Expression of rat aldehyde reductase AKR7A1: influence of age and sex and tissue-specific inducibility published in Biochemical Pharmacology vol 62 (2001) pages 1511-1519.. KW - aldehyde reductase. KW - developmental regulation. KW - fetal expression. KW - sex-specific expression. KW - growth ...

PubMed journal article: Probing the substrate binding site of Candida tenuis xylose reductase (AKR2B5) with site-directed mutagenesis. Download Prime PubMed App to iPhone, iPad, or Android

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Aldo-keto reductases (AKRs) are a class of NADPH-dependent oxidoreductases that have been linked to metabolism of the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN). Although widely used, cardiotoxicity continues to be a serious side effect that may be linked to metabolites or reactive intermediates generated in their metabolism. In this study we examine the little known effects of nonsynonymous single nucleotide polymorphisms of human AKR1A1 on the metabolism of these drugs to their alcohol metabolites. Expressed and purified from bacteria using affinity chromatography, the AKR1A1 protein with a single histidine (6x-His) tag exhibited the greatest activity using two test substrates: p-nitrobenzaldehyde (5.09 ± 0.16 μmol/min/mg of purified protein) and dl-glyceraldehyde (1.24 ± 0.17 μmol/min/mg). These activities are in agreement with published literature values of nontagged human AKR1A1. The 6x-His-tagged AKR1A1 wild type and allelic variants, E55D and N52S, were subsequently ...

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Complete information for HSDL1 gene (Protein Coding), Hydroxysteroid Dehydrogenase Like 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium

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TY - JOUR. T1 - Structural and functional aspects of placental lactogens (PLs) and ovarian 20α-hydroxysteroid dehydrogenase (20α-HSD) in the rat. AU - Shiota, K.. AU - Hirosawa, M.. AU - Hattori, N.. AU - Itonori, S.. AU - Miura, R.. AU - Noda, K.. AU - Takahashi, M.. AU - Ogawa, T.. PY - 1994. Y1 - 1994. N2 - The placenta plays an essential role in fetal growth and the maintenance of pregnancy. Successful development and maturation of the embryo is totally dependent on placental function. The main endocrine participation of the placenta is attributed to placental lactogens (PLs). Progesterone is essential for pregnancy in all mammals and is secreted by the ovary and placenta, depending on the animal species. In the rat, the main source of progesterone throughout pregnancy is the ovary, and 20α-hydroxysteroid dehydrogenase (20α-HSD) is a key enzyme for ovarian progesterone secretion. The primary action of prolactin (PRL) in the maintenance of ovarian progesterone secretion is suppression of ...

20α-Hydroxysteroid dehydrogenase (20α-HSD), which metabolizes progesterone to an inactive steroid in the corpus luteum of mice and rats but not of humans, is thought to play a crucial role in shortening the oestrous cycles in these rodent species. We determined the nucleotide sequence of the 5′-flanking region of the mouse 20α-HSD gene, and examined its promoter activity using a rat luteinized granulosa cell culture. A reporter assay, using reporter constructs of various lengths of the 5′-flanking region, revealed that the region between −83 and 60 bp upstream of the transcription start site was essential for transcriptional activity. Furthermore, mutational analysis demonstrated that a putative Sp1 site in this region was critical to the expression of the reporter gene. Electrophoretic mobility-shift assays showed that the interaction of proteins in a nuclear extract from rat luteinized granulosa cells with this region was inhibited by a competitor having the wild-type Sp1 sequence in ...

Also acts on other 17beta-hydroxysteroids and on the 3alpha-hydroxy group of pregnanes and bile acids. Different from EC 1.1.1.50 3alpha-hydroxysteroid dehydrogenase (Si-specific) or EC 1.1.1.213 3alpha-hydroxysteroid dehydrogenase (Re-specific ...

TY - JOUR. T1 - Ascorbic acid reverses the prolonged anesthetic action of pentobarbital in Akr1a-knockout mice. AU - Ito, Junitsu. AU - Otsuki, Noriyuki. AU - Zhang, Xuhong. AU - Konno, Tasuku. AU - Kurahashi, Toshihiro. AU - Takahashi, Motoko. AU - Yamato, Mayumi. AU - Matsuoka, Yuta. AU - Yamada, Ken-Ichi. AU - Miyata, Satoshi. AU - Fujii, Junichi. PY - 2014/1/24. Y1 - 2014/1/24. N2 - Aims Aldehyde reductase (AKR1A), a member of the aldo-keto reductase superfamily, is highly expressed in the liver and is involved in both the detoxification of carbonyl compounds and ascorbic acid biosynthesis. By comparison with wild-type mice, Akr1a-knockout (Akr1a-/-) mice and human Akrla-transgenic (Akr1atg/+) mice experience different anesthetic actions from pentobarbital - prolonged in Akr1a-knockout (Akr1a -/-) mice and shortened in human Akrla-transgenic (Akr1a tg/+) mice. Main methods We investigated this alteration in the anesthetic efficacy of pentobarbital in Akr1a genetically modified mice. Key ...

Androgens and estrogens increase the number of cell division and the opportunity for random genetic errors and are thus involved in carcinogenesis of hormone related cancers. [...]

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17β-Hydroxysteroid dehydrogenases (HSD17Bs) comprise a large family of 15 members that are mainly involved in sex hormone metabolism. Some HSD17Bs enzymes also play key roles in cholesterol and fatty acid metabolism. Recent study showed that hydroxysteroid 17β-dehydrogenase 13 (HSD17B13), an enzyme …

The impact of quercetin on the mRNA expression of hepatic enzymes involved in drug metabolism was evaluated with a DNA microarray and real-time PCR. Male Sprague-Dawley rats were fed an experimental d

Complete information for AKR1C4 gene (Protein Coding), Aldo-Keto Reductase Family 1 Member C4, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium

TY - JOUR. T1 - Preparation of highly purified 3α- and 3β-hydroxysteroid dehydrogenases from Pseudomonas sp. AU - Shikita, Mikio. AU - Talalay, Paul. PY - 1979/5. Y1 - 1979/5. N2 - A method is described for preparing highly purified 3α- and 3β-hydroxysteroid dehydrogenases (EC 1.1.1.50 and EC 1.1.1.145, respectively), essentially uncontaminated with one another, from extracts of a steroid-induced Pseudomonas species. These enzymes are suitable for the microanalysis of 3α-hydroxy-, 3β-hydroxy-, and 3-ketosteroids.. AB - A method is described for preparing highly purified 3α- and 3β-hydroxysteroid dehydrogenases (EC 1.1.1.50 and EC 1.1.1.145, respectively), essentially uncontaminated with one another, from extracts of a steroid-induced Pseudomonas species. These enzymes are suitable for the microanalysis of 3α-hydroxy-, 3β-hydroxy-, and 3-ketosteroids.. UR - http://www.scopus.com/inward/record.url?scp=0018474352&partnerID=8YFLogxK. UR - ...

The enzyme 11β-hydroxysteroid dehydrogenase type 2 (11β-HSD2) is selectively expressed in aldosterone target tissues, conferring aldosterone selectivity for the mineralocorticoid receptor. A diminished activity causes salt-sensitive hypertension. The mechanism of the variable and distinct 11β-hydroxysteroid dehydrogenase type 2 gene (HSD11B2) expression in the cortical collecting duct is poorly understood. Here, we analyzed for the first time whether the 11β-HSD2 expression is modulated by microRNAs (miRNAs). In silico analysis revealed 53 and 27 miRNAs with potential binding sites on human or rat HSD11B2 3′-untranslated region. A reporter assay demonstrated 3′-untranslated region-dependent regulation of human and rodent HSD11B2. miRNAs were profiled from cortical collecting ducts and proximal convoluted tubules. Bioinformatic analyses showed a distinct clustering for cortical collecting ducts and proximal convoluted tubules with 53 of 375 miRNAs, where 13 were predicted to bind to the ...

Title: Effect of Free and in Poly(η-caprolactone) Nanoparticles Incorporated New Type 1 17β -Hydroxysteroid Dehydrogenase Inhibitors on Cancer Cells. VOLUME: 6 ISSUE: 1. Author(s):Petra Kocbek, Karmen Teskac, Petra Brozic, Tea Lanisnik Rizner, Stanislav Gobec and Julijana Kristl. Affiliation:Askerceva 7, 1000 Ljubljana, Slovenia.. Keywords:Nanoparticles, enzyme inhibitors, T-47D cells, cellular uptake, drug delivery, breast cancer. Abstract: Development and progression of breast cancer can be caused by increased estradiol activity, which stimulates cell proliferation. Inhibitors of type 1 17β-hydroxysteroid dehydrogenase (17β-HSD) enzyme inhibit estradiol biosynthesis and therefore have potential anticancer activity. In this study two new trans-cinnamic acid esters were established as inhibitors of the human recombinant type 1 17β-HSD enzyme. Studied compounds are poorly water soluble and have low stability in aqueous medium. Free inhibitors were tested on T-47D cells, which express ...

Regulation of 3β‐Hydroxysteroid Dehydrogenase Activity by Human Chorionic Gonadotropin, Androgens, and Antiandrogens in Cultured Testicular ...

Abstract Interference with the pregnancy-maintaining influence of progesterone is the basis of most methods for termination of unwanted pregnancy in dogs. The currently available methods are based on induction of luteolysis or blocking of the progesterone receptor. Inhibition of progesterone synthesis using a competitive inhibitor of 3 -hydroxysteroid dehydrogenase (3 ... read more -HSD) could be another strategy to terminate unwanted pregnancies. In this study we investigated the effects of the 3 -HSD inhibitor trilostane on corpus luteum function in non-pregnant bitches. Trilostane was administered orally for seven consecutive days in either the pituitary-independent part of the luteal phase (PIP, start of treatment on D11 after ovulation, n 6) or the pituitary-dependent part (PDP, start of treatment on D31 after ovulation, n 6), in an oral dose of about 4.5 mg/kg bw, twice daily. Results were compared with those obtained in control bitches (n 6). ACTH stimulation tests were performed to ...

Status of 17β-hydroxysteroid dehydrogenase type 2 (17βHSD2) immunoreactivity was significantly higher in invasive lobular carcinoma (ILC) than in invasive duc

The primary source of oestrogen in premenopausal women is the ovary but, after menopause, oestrogen biosynthesis in peripheral tissue is the exclusive site of formation. An enzyme group that affects the availability of active oestrogens is the 17β-hydroxysteroid dehydrogenase (17HSD) family. In breast cancer, 17HSD type 1 and type 2 have been mostly investigated and seem to be the principal 17HSD enzymes involved thus far. The question whether 17HSD type 1 or type 2 is of greatest importance in breast tumour development is still not clear. The aim of this study was to investigate how the loss of 17HSD type 2 expression, using siRNA in the non-tumour breast epithelial cells HMEC (human mammal epithelial cells) and MCF10A, and gain of 17HSD type 2 expression, using transient transfection in the breast cancer derived cell lines MCF7 and T47D, affect oestradiol conversion and proliferation rate measured as S-phase fraction. We further investigated how this was related to the endogenous expression ...

Accepted name: 17β-estradiol 17-dehydrogenase. Reaction: 17β-estradiol + NAD(P)+ = estrone + NAD(P)H + H+. Other name(s): 20α-hydroxysteroid dehydrogenase; 17β,20α-hydroxysteroid dehydrogenase; 17β-estradiol dehydrogenase; estradiol dehydrogenase; estrogen 17-oxidoreductase; 17β-HSD; HSD17B7. Systematic name: 17β-estradiol:NAD(P)+ 17-oxidoreductase. Comments: The enzyme oxidizes or reduces the hydroxy/keto group on C17 of estrogens and androgens in mammals and regulates the biological potency of these steroids. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.270, 3β-hydroxysteroid 3-dehydrogenase [3]. The enzyme also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds, oxidizing the (S)-20-group, but unlike EC 1.1.1.149, 20α-hydroxysteroid dehydrogenase, it is Si-specific with respect to NAD(P)+.. Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9028-61-9. References:. 1. Kautsky, M.P. and Hagerman, D.D. 17β-Estradiol ...

Accepted name: 17β-estradiol 17-dehydrogenase. Reaction: 17β-estradiol + NAD(P)+ = estrone + NAD(P)H + H+. Other name(s): 20α-hydroxysteroid dehydrogenase; 17β,20α-hydroxysteroid dehydrogenase; 17β-estradiol dehydrogenase; estradiol dehydrogenase; estrogen 17-oxidoreductase; 17β-HSD; HSD17B7. Systematic name: 17β-estradiol:NAD(P)+ 17-oxidoreductase. Comments: The enzyme oxidizes or reduces the hydroxy/keto group on C17 of estrogens and androgens in mammals and regulates the biological potency of these steroids. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.270, 3β-hydroxysteroid 3-dehydrogenase [3]. The enzyme also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds, oxidizing the (S)-20-group, but unlike EC 1.1.1.149, 20α-hydroxysteroid dehydrogenase, it is Si-specific with respect to NAD(P)+.. Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9028-61-9. References:. 1. Kautsky, M.P. and Hagerman, D.D. 17β-Estradiol ...

Aldo-keto reductase family 1 member C1 also known as 20α-hydroxysteroid dehydrogenase, 3α-hydroxysteroid dehydrogenase, and dihydrodiol dehydrogenase 1/2 is an enzyme that in humans is encoded by the AKR1C1 gene.[1][2] This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme catalyzes the reduction of progesterone to the inactive form 20-alpha-hydroxy-progesterone. This gene shares high sequence identity with three other gene members, and is clustered with those three genes at chromosome 10p15-p14.[2] ...

Circulating levels of the steroid hormone, progesterone (P), increase during development of the primate corpus luteum (CL) and then decline during luteal regres...

Inderbinen SG, Zogg M, Kley M, Smieško M, Odermatt A Endocrine Disruption and Steroid Hormone Action Toxicology and Applied Pharmacology, 1 Feb 2021 ...

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Macdonald, I.A., Mahony, D.E., Jellett, J.F. and Meier, C.E. (1977). NAD-dependent 3α- and 12α-hydroxysteroid dehydrogenase activities from Eubacterium lentum ATCC no. 25559. Biochim. Biophys. Acta 489: 466-476. PMID 201289. ...

The enzyme 20α-hydroxysteroid dehydrogenase (20α-HSD) catalyzes the conversion of progesterone to its inactive form, 20α-hydroxyprogesterone. This enzyme has been shown to play a critical role in the regulation of luteal function in experimental animals. In this study, we cloned and expressed the gene encoding elk deer 20α-HSD from reproductive placental ...

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