Example of Steroids format
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Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format
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Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format Example of Steroids format
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open access Open Access ISSN: 0039128X e-ISSN: 18785867

Steroids — Template for authors

Publisher: Elsevier
Categories Rank Trend in last 3 yrs
Organic Chemistry #84 of 185 down down by 35 ranks
Pharmacology #146 of 297 down down by 46 ranks
Biochemistry #245 of 415 down down by 96 ranks
Clinical Biochemistry #69 of 113 down down by 27 ranks
Endocrinology #74 of 117 down down by 22 ranks
Molecular Biology #264 of 382 down down by 88 ranks
journal-quality-icon Journal quality:
Good
calendar-icon Last 4 years overview: 567 Published Papers | 2115 Citations
indexed-in-icon Indexed in: Scopus
last-updated-icon Last updated: 02/07/2020
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Top papers
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FAQ

Journal Performance & Insights

  • Impact Factor
  • CiteRatio
  • SJR
  • SNIP

Impact factor determines the importance of a journal by taking a measure of frequency with which the average article in a journal has been cited in a particular year.

1.948

9% from 2018

Impact factor for Steroids from 2016 - 2019
Year Value
2019 1.948
2018 2.136
2017 2.523
2016 2.282
graph view Graph view
table view Table view

insights Insights

  • Impact factor of this journal has decreased by 9% in last year.
  • This journal’s impact factor is in the top 10 percentile category.

CiteRatio is a measure of average citations received per peer-reviewed paper published in the journal.

3.7

3% from 2019

CiteRatio for Steroids from 2016 - 2020
Year Value
2020 3.7
2019 3.8
2018 4.9
2017 4.9
2016 4.8
graph view Graph view
table view Table view

insights Insights

  • CiteRatio of this journal has decreased by 3% in last years.
  • This journal’s CiteRatio is in the top 10 percentile category.

SCImago Journal Rank (SJR) measures weighted citations received by the journal. Citation weighting depends on the categories and prestige of the citing journal.

0.469

16% from 2019

SJR for Steroids from 2016 - 2020
Year Value
2020 0.469
2019 0.557
2018 0.641
2017 0.904
2016 0.957
graph view Graph view
table view Table view

insights Insights

  • SJR of this journal has decreased by 16% in last years.
  • This journal’s SJR is in the top 10 percentile category.

Source Normalized Impact per Paper (SNIP) measures actual citations received relative to citations expected for the journal's category.

0.907

5% from 2019

SNIP for Steroids from 2016 - 2020
Year Value
2020 0.907
2019 0.866
2018 0.906
2017 0.992
2016 1.052
graph view Graph view
table view Table view

insights Insights

  • SNIP of this journal has increased by 5% in last years.
  • This journal’s SNIP is in the top 10 percentile category.

Related Journals

open access Open Access ISSN: 21922195 e-ISSN: 21922209

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CiteRatio: 4.3 | SJR: 0.633 | SNIP: 1.433
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De Gruyter

CiteRatio: 6.5 | SJR: 1.246 | SNIP: 0.854
open access Open Access ISSN: 9394451 e-ISSN: 14382199

Springer

CiteRatio: 6.0 | SJR: 0.894 | SNIP: 1.005
open access Open Access ISSN: 10967192 e-ISSN: 10967206

Elsevier

CiteRatio: 7.0 | SJR: 1.329 | SNIP: 1.627

Steroids

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Elsevier

Steroids

Steroids is an international journal devoted to original research on all aspects of steroids. Its focus is on both experimental and theoretical studies in chemistry and physiochemistry, biosynthesis, metabolism, molecular biology, physiology, pharmacology, analytical technique...... Read More

Chemistry

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Last updated on
01 Jul 2020
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ISSN
0039-128X
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Impact Factor
High - 1.144
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Open Access
Yes
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Sherpa RoMEO Archiving Policy
Green faq
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Plagiarism Check
Available via Turnitin
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Endnote Style
Download Available
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Bibliography Name
elsarticle-num
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Citation Type
Numbered
[25]
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Bibliography Example
G. E. Blonder, M. Tinkham, T. M. Klapwijk, Transition from metallic to tunneling regimes in superconducting microconstrictions: Excess current, charge imbalance, and supercurrent conversion, Phys. Rev. B 25 (7) (1982) 4515–4532. URL 10.1103/PhysRevB.25.4515

Top papers written in this journal

Journal Article DOI: 10.1016/0039-128X(75)90077-X
The determination of five steroids in avian plasma by radioimmunoassay and competitive protein-binding
John C. Wingfield1, Donald S. Farner1
01 Sep 1975 - Steroids

Abstract:

A method has been developed for the simultaneous determination of testosterone, 5α-dihydrotestosterone and corticosterone, or of estrone, estradiol-17β and corticosterone, after separation on a Celite: propylene glycol:ethylene glycol column (6:1.5:1.5 w/v/v). The lower quarter of the column was packed with a Celite:water mix... A method has been developed for the simultaneous determination of testosterone, 5α-dihydrotestosterone and corticosterone, or of estrone, estradiol-17β and corticosterone, after separation on a Celite: propylene glycol:ethylene glycol column (6:1.5:1.5 w/v/v). The lower quarter of the column was packed with a Celite:water mixture (3:1 w/v) as a stationary phase (glycol) ‘trap’. This effectively prevented leaching of the glycols into the eluate as the concentration of ethyl acetate in the mobile phase was increased to elute the more polar steroids. In addition, a second system utilizing a Celite:ethylene glycol column (2:1 w/v) for the separation of estrone and estradiol-17β is described. Testosterone, 5α-dihydrotestosterone, estrone and estradiol-17β were measured by radioimmunoassay and corticosterone by a competitive protein-binding technique. Reliability criteria are presented showing that the assay systems used are accurate and reproducible. Plasma-steroid levels of eight avian species are also presented and compared with those found by other investigators. read more read less

Topics:

Ethylene glycol (54%)54% related to the paper, Estrone (52%)52% related to the paper
620 Citations
Journal Article DOI: 10.1016/S0039-128X(96)00242-5
The estradiol pharmacophore: Ligand structure-estrogen receptor binding affinity relationships and a model for the receptor binding site
Gregory M. Anstead1, Kathryn E. Carlson2, John A. Katzenellenbogen2
01 Mar 1997 - Steroids

Abstract:

The accumulated knowledge on the binding of estradiol (E2) and its analogs and the results of affinity-labeling studies have been reviewed and are used herein to derive a binding site model for the estrogen receptor (ER). Estradiol is nonpolar and hydrophobic, except at its molecular termini. Most of its skeletal flexibility ... The accumulated knowledge on the binding of estradiol (E2) and its analogs and the results of affinity-labeling studies have been reviewed and are used herein to derive a binding site model for the estrogen receptor (ER). Estradiol is nonpolar and hydrophobic, except at its molecular termini. Most of its skeletal flexibility resides in the B-ring, and it probably binds in a low-energy conformation. The phenolic OH group in the A-ring contributes about 1.9 kcal/mol to the binding free energy and probably acts primarily as a hydrogen bond donor. The 17 beta-hydroxyl group in the D-ring contributes approximately 0.6 kcal/mol to the binding and probably acts as a hydrogen bond acceptor, either directly or via a water molecule. There also seems to be a degree of flexibility in the region of the receptor that encompasses the D-ring. The aromatic ring contributes about 1.5 kcal/mol, probably through weak polar interactions with receptor residues that contact the beta-face of the steroid. The receptor seems to surround the ligand, so that all four rings contribute significantly to binding. Small hydrophobic substituents enhance binding affinity at positions 4, 12 beta, 14, and 16 alpha; whereas, larger hydrophobic substituents are tolerated at positions 7 alpha, 11 beta, and 17 alpha. In general, the ER is intolerant of polar substituents. Based on E2 analogs bearing affinity-labeling groups, cysteine residues might be present in the binding site in the area of C-4, C-17 alpha, and C-17 beta, and a lysine residue might be located near C-16. Models that represent the limits of deformability of the ligand binding site, the position of preformed pockets, and space occupied by the receptor are presented. The various elements in this model for the binding of steroidal estrogens by the estrogen receptor are consistent with evidence emerging from the crystal structures of related nuclear hormone receptor ligand complexes. read more read less

Topics:

Estrogen receptor binding (69%)69% related to the paper, Ligand (biochemistry) (63%)63% related to the paper, Ligand efficiency (58%)58% related to the paper, Binding site (56%)56% related to the paper, Cooperative binding (56%)56% related to the paper
597 Citations
open accessOpen access Journal Article DOI: 10.1016/J.STEROIDS.2007.02.003
Neurotrophic and neuroprotective actions of estrogen: Basic mechanisms and clinical implications
01 May 2007 - Steroids

Abstract:

Estrogen is an important hormone signal that regulates multiple tissues and functions in the body. This review focuses on the neurotrophic and neuroprotective actions of estrogen in the brain, with particular emphasis on estrogen actions in the hippocampus, cerebral cortex and striatum. Sex differences in the risk, onset and ... Estrogen is an important hormone signal that regulates multiple tissues and functions in the body. This review focuses on the neurotrophic and neuroprotective actions of estrogen in the brain, with particular emphasis on estrogen actions in the hippocampus, cerebral cortex and striatum. Sex differences in the risk, onset and severity of neurodegenerative disease such as Alzheimer's disease, Parkinson's disease and stroke are well known, and the potential role of estrogen as a neuroprotective factor is discussed in this context. The review assimilates a complex literature that spans research in humans, non-human primates and rodent animal models and attempts to contrast and compare the findings across species where possible. Current controversies regarding the Women's Health Initiative (WHI) study, its ramifications, concerns and the new studies needed to address these concerns are also addressed. Signaling mechanisms underlying estrogen-induced neuroprotection and synaptic plasticity are reviewed, including the important concepts of genomic versus nongenomic mechanisms, types of estrogen receptor involved and their subcellular targeting, and implicated downstream signaling pathways and mediators. Finally, a multicellular mode of estrogen action in the regulation of neuronal survival and neurotrophism is discussed, as are potential future directions for the field. read more read less

Topics:

Estrogen receptor (56%)56% related to the paper, Estrogen (53%)53% related to the paper, Neuroprotection (52%)52% related to the paper
487 Citations
Journal Article DOI: 10.1016/S0039-128X(99)00107-5
Estrogen receptor interaction with co-activators and co-repressors.
Carolyn M. Klinge1
01 May 2000 - Steroids

Topics:

Estrogen receptor beta (61%)61% related to the paper, Estrogen receptor alpha (59%)59% related to the paper, Estrogen-related receptor gamma (55%)55% related to the paper, Estrogen-related receptor alpha (54%)54% related to the paper, Estrogen receptor (54%)54% related to the paper
473 Citations
Journal Article DOI: 10.1016/S0039-128X(02)00110-1
Estrogen receptor phosphorylation
Deborah A. Lannigan1
01 Jan 2003 - Steroids

Abstract:

Estrogen receptor alpha (ERalpha) is phosphorylated on multiple amino acid residues. For example, in response to estradiol binding, human ERalpha is predominately phosphorylated on Ser-118 and to a lesser extent on Ser-104 and Ser-106. In response to activation of the mitogen-activated protein kinase pathway, phosphorylation ... Estrogen receptor alpha (ERalpha) is phosphorylated on multiple amino acid residues. For example, in response to estradiol binding, human ERalpha is predominately phosphorylated on Ser-118 and to a lesser extent on Ser-104 and Ser-106. In response to activation of the mitogen-activated protein kinase pathway, phosphorylation occurs on Ser-118 and Ser-167. These serine residues are all located within the activation function 1 region of the N-terminal domain of ERalpha. In contrast, activation of protein kinase A increases the phosphorylation of Ser-236, which is located in the DNA-binding domain. The in vivo phosphorylation status of Tyr-537, located in the ligand-binding domain, remains controversial. In this review, I present evidence that these phosphorylations occur, and identify the kinases thought to be responsible. Additionally, the functional importance of ERalpha phosphorylation is discussed. read more read less

Topics:

Protein phosphorylation (63%)63% related to the paper, Phosphorylation cascade (61%)61% related to the paper, Phosphorylation (58%)58% related to the paper, Protein kinase A (57%)57% related to the paper, Estrogen receptor alpha (56%)56% related to the paper
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452 Citations
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SciSpace is a very innovative solution to the formatting problem and existing providers, such as Mendeley or Word did not really evolve in recent years.

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With SciSpace, you do not need a word template for Steroids.

It automatically formats your research paper to Elsevier formatting guidelines and citation style.

You can download a submission ready research paper in pdf, LaTeX and docx formats.

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Time taken to format a paper and Compliance with guidelines

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Steroids format uses elsarticle-num citation style.

Automatically format and order your citations and bibliography in a click.

SciSpace allows imports from all reference managers like Mendeley, Zotero, Endnote, Google Scholar etc.

Frequently asked questions

Absolutely not! With our tool, you can freely write without having to focus on LaTeX. You can write your entire paper as per the Steroids guidelines and autoformat it.

Yes. The template is fully compliant as per the guidelines of this journal. Our experts at SciSpace ensure that. Also, if there's any update in the journal format guidelines, we take care of it and include that in our algorithm.

Sure. We support all the top citation styles like APA style, MLA style, Vancouver style, Harvard style, Chicago style, etc. For example, in case of this journal, when you write your paper and hit autoformat, it will automatically update your article as per the Steroids citation style.

You can avail our Free Trial for 7 days. I'm sure you'll find our features very helpful. Plus, it's quite inexpensive.

Yup. You can choose the right template, copy-paste the contents from the word doc and click on auto-format. You'll have a publish-ready paper that you can download at the end.

A matter of seconds. Besides that, our intuitive editor saves a load of your time in writing and formating your manuscript.

One little Google search can get you the Word template for any journal. However, why do you need a Word template when you can write your entire manuscript on SciSpace, autoformat it as per Steroids's guidelines and download the same in Word, PDF and LaTeX formats? Try us out!.

Absolutely! You can do it using our intuitive editor. It's very easy. If you need help, you can always contact our support team.

SciSpace is an online tool for now. We'll soon release a desktop version. You can also request (or upvote) any feature that you think might be helpful for you and the research community in the feature request section once you sign-up with us.

Sure. You can request any template and we'll have it up and running within a matter of 3 working days. You can find the request box in the Journal Gallery on the right sidebar under the heading, "Couldn't find the format you were looking for?".

After you have written and autoformatted your paper, you can download it in multiple formats, viz., PDF, Docx and LaTeX.

To be honest, the answer is NO. The impact factor is one of the many elements that determine the quality of a journal. Few of those factors the review board, rejection rates, frequency of inclusion in indexes, Eigenfactor, etc. You must assess all the factors and then take the final call.

SHERPA/RoMEO Database

We have extracted this data from Sherpa Romeo to help our researchers understand the access level of this journal. The following table indicates the level of access a journal has as per Sherpa Romeo Archiving Policy.

RoMEO Colour Archiving policy
Green Can archive pre-print and post-print or publisher's version/PDF
Blue Can archive post-print (ie final draft post-refereeing) or publisher's version/PDF
Yellow Can archive pre-print (ie pre-refereeing)
White Archiving not formally supported
FYI:
  1. Pre-prints as being the version of the paper before peer review and
  2. Post-prints as being the version of the paper after peer-review, with revisions having been made.

The 5 most common citation types in order of usage are:.

S. No. Citation Style Type
1. Author Year
2. Numbered
3. Numbered (Superscripted)
4. Author Year (Cited Pages)
5. Footnote

Our journal submission experts are skilled in submitting papers to various international journals.

After uploading your paper on SciSpace, you would see a button to request a journal submission service for Steroids.

Each submission service is completed within 4 - 5 working days.

Yes. SciSpace provides this functionality.

After signing up, you would need to import your existing references from Word or .bib file.

SciSpace would allow download of your references in Steroids Endnote style, according to elsevier guidelines.

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