Example of Cell Stress and Chaperones format
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Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format Example of Cell Stress and Chaperones format
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open access Open Access

Cell Stress and Chaperones — Template for authors

Publisher: Springer
Categories Rank Trend in last 3 yrs
Biochemistry #162 of 415 down down by 8 ranks
Cell Biology #134 of 279 up up by 5 ranks
journal-quality-icon Journal quality:
Good
calendar-icon Last 4 years overview: 381 Published Papers | 2060 Citations
indexed-in-icon Indexed in: Scopus
last-updated-icon Last updated: 09/07/2020
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Related Journals

open access Open Access

American Chemical Society

Quality:  
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CiteRatio: 6.5
SJR: 1.158
SNIP: 1.002
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American Association for the Advancement of Science

Quality:  
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SJR: 3.659
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open access Open Access

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Quality:  
High
CiteRatio: 6.8
SJR: 1.329
SNIP: 1.08
open access Open Access

Springer

Quality:  
High
CiteRatio: 5.7
SJR: 1.158
SNIP: 1.069

Journal Performance & Insights

Impact Factor

CiteRatio

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.

A measure of average citations received per peer-reviewed paper published in the journal.

2.892

0% from 2018

Impact factor for Cell Stress and Chaperones from 2016 - 2019
Year Value
2019 2.892
2018 2.903
2017 2.571
2016 2.411
graph view Graph view
table view Table view

5.4

4% from 2019

CiteRatio for Cell Stress and Chaperones from 2016 - 2020
Year Value
2020 5.4
2019 5.2
2018 4.8
2017 4.8
2016 4.5
graph view Graph view
table view Table view

insights Insights

  • Impact factor of this journal has decreased by 0% in last year.
  • This journal’s impact factor is in the top 10 percentile category.

insights Insights

  • CiteRatio of this journal has increased by 4% in last years.
  • This journal’s CiteRatio is in the top 10 percentile category.

SCImago Journal Rank (SJR)

Source Normalized Impact per Paper (SNIP)

Measures weighted citations received by the journal. Citation weighting depends on the categories and prestige of the citing journal.

Measures actual citations received relative to citations expected for the journal's category.

0.994

17% from 2019

SJR for Cell Stress and Chaperones from 2016 - 2020
Year Value
2020 0.994
2019 0.852
2018 1.077
2017 0.987
2016 0.995
graph view Graph view
table view Table view

0.971

1% from 2019

SNIP for Cell Stress and Chaperones from 2016 - 2020
Year Value
2020 0.971
2019 0.957
2018 0.91
2017 0.883
2016 0.781
graph view Graph view
table view Table view

insights Insights

  • SJR of this journal has increased by 17% in last years.
  • This journal’s SJR is in the top 10 percentile category.

insights Insights

  • SNIP of this journal has increased by 1% in last years.
  • This journal’s SNIP is in the top 10 percentile category.
Cell Stress and Chaperones

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Springer

Cell Stress and Chaperones

Approved by publishing and review experts on SciSpace, this template is built as per for Cell Stress and Chaperones formatting guidelines as mentioned in Springer author instructions. The current version was created on and has been used by 953 authors to write and format their manuscripts to this journal.

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Last updated on
08 Jul 2020
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ISSN
1466-1268
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Open Access
Hybrid
i
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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Citation Type
Author Year
(Blonder et al, 1982)
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Bibliography Example
Beenakker CWJ (2006) Specular andreev reflection in graphene. Phys Rev Lett 97(6):067,007, URL 10.1103/PhysRevLett.97.067007

Top papers written in this journal

open accessOpen access Journal Article DOI: 10.1379/CSC-99R.1
Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications
Daniel R. Ciocca1, Stuart K. Calderwood2, Stuart K. Calderwood3
01 Jan 2005 - Cell Stress & Chaperones

Abstract:

Heat shock proteins (Hsps) are overexpressed in a wide range of human cancers and are implicated in tumor cell proliferation, differentiation, invasion, metastasis, death, and recognition by the immune system. We review the current status of the role of Hsp expression in cancer with special emphasis on the clinical setting. A... Heat shock proteins (Hsps) are overexpressed in a wide range of human cancers and are implicated in tumor cell proliferation, differentiation, invasion, metastasis, death, and recognition by the immune system. We review the current status of the role of Hsp expression in cancer with special emphasis on the clinical setting. Although Hsp levels are not informative at the diagnostic level, they are useful biomarkers for carcinogenesis in some tissues and signal the degree of differentiation and the aggressiveness of some cancers. In addition, the circulating levels of Hsp and anti-Hsp antibodies in cancer patients may be useful in tumor diagnosis. Furthermore, several Hsp are implicated with the prognosis of specific cancers, most notably Hsp27, whose expression is associated with poor prognosis in gastric, liver, and prostate carcinoma, and osteosarcomas, and Hsp70, which is correlated with poor prognosis in breast, endometrial, uterine cervical, and bladder carcinomas. Increased Hsp expression may also predict the response to some anticancer treatments. For example, Hsp27 and Hsp70 are implicated in resistance to chemotherapy in breast cancer, Hsp27 predicts a poor response to chemotherapy in leukemia patients, whereas Hsp70 expression predicts a better response to chemotherapy in osteosarcomas. Implication of Hsp in tumor progression and response to therapy has led to its successful targeting in therapy by 2 main strategies, including: (1) pharmacological modification of Hsp expression or molecular chaperone activity and (2) use of Hsps in anticancer vaccines, exploiting their ability to act as immunological adjuvants. In conclusion, the present times are of importance for the field of Hsps in cancer, with great contributions to both basic and clinical cancer research. read more read less

Topics:

Cancer (59%)59% related to the paper, Metastasis (56%)56% related to the paper, Tumor progression (54%)54% related to the paper, Breast cancer (53%)53% related to the paper, Heat shock protein (53%)53% related to the paper
View PDF
1,307 Citations
open accessOpen access Journal Article DOI: 10.1007/S12192-008-0068-7
Guidelines for the nomenclature of the human heat shock proteins
01 Jan 2009 - Cell Stress & Chaperones

Abstract:

The expanding number of members in the various human heat shock protein (HSP) families and the inconsistencies in their nomenclature have often led to confusion. Here, we propose new guidelines for the nomenclature of the human HSP families, HSPH (HSP110), HSPC (HSP90), HSPA (HSP70), DNAJ (HSP40), and HSPB (small HSP) as well... The expanding number of members in the various human heat shock protein (HSP) families and the inconsistencies in their nomenclature have often led to confusion. Here, we propose new guidelines for the nomenclature of the human HSP families, HSPH (HSP110), HSPC (HSP90), HSPA (HSP70), DNAJ (HSP40), and HSPB (small HSP) as well as for the human chaperonin families HSPD/E (HSP60/HSP10) and CCT (TRiC). The nomenclature is based largely on the more consistent nomenclature assigned by the HUGO Gene Nomenclature Committee and used in the National Center of Biotechnology Information Entrez Gene database for the heat shock genes. In addition to this nomenclature, we provide a list of the human Entrez Gene IDs and the corresponding Entrez Gene IDs for the mouse orthologs. read more read less

Topics:

Gene nomenclature (70%)70% related to the paper, Entrez Gene (58%)58% related to the paper
View PDF
1,104 Citations
open accessOpen access Journal Article DOI: 10.1379/1466-1268(2001)006<0177:AATHST>2.0.CO;2
Arabidopsis and the heat stress transcription factor world: how many heat stress transcription factors do we need?
Lutz Nover1, Kapil Bharti1, Pascal Döring1, Shravan Kumar Mishra1, Arnab Ganguli1, Klaus-Dieter Scharf1
01 Jul 2001 - Cell Stress & Chaperones

Abstract:

Sequencing of the Arabidopsis genome revealed a unique complexity of the plant heat stress transcription factor (Hsf) family. By structural characteristics and phylogenetic comparison, the 21 representatives are assigned to 3 classes and 14 groups. Particularly striking is the finding of a new class of Hsfs (AtHsfC1) closely ... Sequencing of the Arabidopsis genome revealed a unique complexity of the plant heat stress transcription factor (Hsf) family. By structural characteristics and phylogenetic comparison, the 21 representatives are assigned to 3 classes and 14 groups. Particularly striking is the finding of a new class of Hsfs (AtHsfC1) closely related to Hsf1 from rice and to Hsfs identified from frequently found expressed sequence tags of tomato, potato, barley, and soybean. Evidently, this new type of Hsf is well expressed in different plant tissues. Besides the DNA binding and oligomerization domains (HR-A/B region), we identified other functional modules of Arabidopsis Hsfs by sequence comparison with the well-characterized tomato Hsfs. These are putative motifs for nuclear import and export and transcriptional activation (AHA motifs). There is intriguing flexibility of size and sequence in certain parts of the otherwise strongly conserved N-terminal half of these Hsfs. We have speculated about possible exon-intron borders in this region in the ancient precursor gene of plant Hsfs, similar to the exon-intron structure of the present mammalian Hsf-encoding genes. read more read less

Topics:

Arabidopsis (53%)53% related to the paper
672 Citations
open accessOpen access Journal Article DOI: 10.1379/1466-1268(1996)001<0109:IOMACC>2.3.CO;2
Influence of molecular and chemical chaperones on protein folding
Welch Wj1, Brown Cr
01 Jun 1996 - Cell Stress & Chaperones

Abstract:

Protein folding inside the cell involves the Participation of accessory components known as molecular chaperones. In addition to their active participation in the folding process, molecular chaperones serve as a type of ‘quality control system’, recognizing, retaining and targeting misfolded proteins for their eventual degrad... Protein folding inside the cell involves the Participation of accessory components known as molecular chaperones. In addition to their active participation in the folding process, molecular chaperones serve as a type of ‘quality control system’, recognizing, retaining and targeting misfolded proteins for their eventual degradation. It is now known that a number of human diseases arise as a consequence of specific point mutations or deletions within genes encoding essential proteins. In many cases these mutations/deletions are not so sever as to totally destroy the biological activity of the particular gene product. Rather, the mutations often result in only subtle folding abnormalities which lead to the newly synthesized protein being retained at the endoplasmic reticulum by the actions of the cellylar quality control system. In this short review article we discuss our recent studies showing that the protein folding defect associated with the most common mutation in patients with cystic fibriosis can be overcome by a novel strategy. As shown in the paper by Brown et al in this issue (Brown et al 1996), a number of different low molecular weight compounds, all known to stabilize proteins in their native conformation, are effective in rescuing the processing defect of the mutant cystic fibrosis transmembrane conductance regulator protein. We then discuss how these same compounds, which we now call chemical chaperones, also may prove to be effective in correcting a number of other protein folding abnormalities which constitute the underlying basis of a large number of different human diseases. read more read less

Topics:

Co-chaperone (71%)71% related to the paper, Chaperone (protein) (64%)64% related to the paper, Protein folding (60%)60% related to the paper, Chemical chaperone (59%)59% related to the paper
519 Citations
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Frequently asked questions

1. Can I write Cell Stress and Chaperones in LaTeX?

Absolutely not! Our tool has been designed to help you focus on writing. You can write your entire paper as per the Cell Stress and Chaperones guidelines and auto format it.

2. Do you follow the Cell Stress and Chaperones guidelines?

Yes, the template is compliant with the Cell Stress and Chaperones guidelines. Our experts at SciSpace ensure that. If there are any changes to the journal's guidelines, we'll change our algorithm accordingly.

3. Can I cite my article in multiple styles in Cell Stress and Chaperones?

Of course! We support all the top citation styles, such as APA style, MLA style, Vancouver style, Harvard style, and Chicago style. For example, when you write your paper and hit autoformat, our system will automatically update your article as per the Cell Stress and Chaperones citation style.

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Sign up for our free trial, and you'll be able to use all our features for seven days. You'll see how helpful they are and how inexpensive they are compared to other options, Especially for Cell Stress and Chaperones.

5. Can I use a manuscript in Cell Stress and Chaperones that I have written in MS Word?

Yes. You can choose the right template, copy-paste the contents from the word document, and click on auto-format. Once you're done, you'll have a publish-ready paper Cell Stress and Chaperones that you can download at the end.

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7. Where can I find the template for the Cell Stress and Chaperones?

It is possible to find the Word template for any journal on Google. However, why use a template when you can write your entire manuscript on SciSpace , auto format it as per Cell Stress and Chaperones's guidelines and download the same in Word, PDF and LaTeX formats? Give us a try!.

8. Can I reformat my paper to fit the Cell Stress and Chaperones's guidelines?

Of course! You can do this using our intuitive editor. It's very easy. If you need help, our support team is always ready to assist you.

9. Cell Stress and Chaperones an online tool or is there a desktop version?

SciSpace's Cell Stress and Chaperones is currently available as an online tool. We're developing a desktop version, too. You can request (or upvote) any features that you think would be helpful for you and other researchers in the "feature request" section of your account once you've signed up with us.

10. I cannot find my template in your gallery. Can you create it for me like Cell Stress and Chaperones?

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11. What is the output that I would get after using Cell Stress and Chaperones?

After writing your paper autoformatting in Cell Stress and Chaperones, you can download it in multiple formats, viz., PDF, Docx, and LaTeX.

12. Is Cell Stress and Chaperones's impact factor high enough that I should try publishing my article there?

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 these factors include review board, rejection rates, frequency of inclusion in indexes, and Eigenfactor. You need to assess all these factors before you make your final call.

13. What is Sherpa RoMEO Archiving Policy for Cell Stress and Chaperones?

SHERPA/RoMEO Database

We extracted this data from Sherpa Romeo to help researchers understand the access level of this journal in accordance with the Sherpa Romeo Archiving Policy for Cell Stress and Chaperones. The table below indicates the level of access a journal has as per Sherpa Romeo's 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.

14. What are the most common citation types In Cell Stress and Chaperones?

The 5 most common citation types in order of usage for Cell Stress and Chaperones are:.

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

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16. Can I download Cell Stress and Chaperones in Endnote format?

Yes, SciSpace provides this functionality. After signing up, you would need to import your existing references from Word or Bib file to SciSpace. Then SciSpace would allow you to download your references in Cell Stress and Chaperones Endnote style according to Elsevier guidelines.

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