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Article: Nutrition in ICU Patients

Mehta, Yatin / Joshi, Anshu

Journal of Cardiac Critical Care TSS

2022 Volume 06, Issue 01, Page(s) 5–6

Language	English
Publishing date	2022-01-01
Publisher	Thieme Medical and Scientific Publishers Pvt. Ltd.
Publishing place	Stuttgart ; New York
Document type	Article
ISSN	2456-9224
ISSN (online)	2456-9224
DOI	10.1055/s-0041-1739526
Database	Thieme publisher's database

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Article: Dysglycemia in ICU Patients

Joshi, Anshu / Mehta, Yatin

Journal of Cardiac Critical Care TSS

2022 Volume 06, Issue 01, Page(s) 40–42

Abstract: Dysglycemia has emerged as a very common challenge in critically ill patients, especially with regard to current coronavirus disease 2019 pandemic. Prediabetes, poorly controlled diabetes, pharmaceutical intervention in intensive care unit (ICU) with ... ...

Abstract	Dysglycemia has emerged as a very common challenge in critically ill patients, especially with regard to current coronavirus disease 2019 pandemic. Prediabetes, poorly controlled diabetes, pharmaceutical intervention in intensive care unit (ICU) with glucocorticoids, catecholamines and other medicines, and stress response all contribute to dysglycemia in critically ill patients. Early identification and management are the key to prevent further complications. Patient prognosis in terms of clinical outcome, length of ICU stay, and in-hospital morbidity/mortality are adversely affected by patient's dysglycemic status. Apart from hyperglycemia, the other three important pillars of dysglycemia are discussed in this article. Synopsis of early intervention have been captured from India-specific practice guidelines. Important landmark trials have also been captured in this article to provide a clarity on certain aspects of managing dysglycemia in ICUs. Hence, this review article is an attempt to bring forth the salient aspects in diagnosing and managing dysglycemia in critical care settings.
Keywords	intensive care unit ; glycemic variability ; blood glucose
Language	English
Publishing date	2022-01-01
Publisher	Thieme Medical and Scientific Publishers Pvt. Ltd.
Publishing place	Stuttgart ; New York
Document type	Article
ISSN	2456-9224
ISSN (online)	2456-9224
DOI	10.1055/s-0042-1750116
Database	Thieme publisher's database

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Article: Common Controversies in Critical Care Nutrition: Review of Latest Evidences

Joshi, Anshu / Mehta, Yatin

Journal of Cardiac Critical Care TSS

2019 Volume 3, Issue 02, Page(s) 85–88

Abstract: Context: Critical care nutrition favorably influences patient prognosis and remains an essential component of overall patient care. Various guidelines and literature discuss the modalities, benefits, and other finer details of nutrition in intensive ... ...

Abstract	Context: Critical care nutrition favorably influences patient prognosis and remains an essential component of overall patient care. Various guidelines and literature discuss the modalities, benefits, and other finer details of nutrition in intensive care units. Critical care nutrition is still an emerging modality and hence, ambiguity/subjectivity exists in various aspects. Clear recommendations are not there, especially when it comes to diverse topics such as nutrition screening/assessment, underfeeding patients, types of nutrition formulae, monitoring nutrition adequacy, and tolerance and likewise. This article is an attempt to address couple of these concerns and review the latest evidences/guidelines in context of nutrition screening/assessment and monitoring tolerance by measuring gastric residual volumes (GRVs). Evidence Acquisition: Various literature including existing guidelines, original articles, and review articles published till September 2019 and discussing the specifics of nutrition screening/assessment and monitoring tolerance by measuring gastric residuals were searched on popular scientific databases such as PubMed, Scholar Google, and Embase and reviewed for contextual relevance. Results: Majority of the recommendations/evidences in this regard are either inconsistent or incomplete. Most of the tools that are recommended for nutrition screening/assessment of critical care patients are not validated for this population. Majority of literature is unanimous on not recommending biochemical parameters to be used for this purpose. Recommendations for the acceptable values of GRVs are consistent but subjectivity exits on the frequency of measurement, timing of measurement in relation to meals, and other variables. Conclusion: Till the time, nutrition screening/assessment tools for critical care patients are validated in large multicentric settings, it would be prudent to adhere to the recommendations of existing guidelines. Similarly, GRV practices and cutoff values can be followed from relevant guidelines.
Keywords	enteral nutrition (EN) ; gastric residual volumes (GRVs) ; intensive care unit (ICU)
Language	English
Publishing date	2019-12-01
Publisher	Thieme Medical and Scientific Publishers Private Ltd.
Publishing place	Stuttgart ; New York
Document type	Article
ISSN	2456-9224
ISSN (online)	2456-9224
DOI	10.1055/s-0039-3402344
Database	Thieme publisher's database

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Article ; Online: Crystal Structure of FOXC2 in Complex with DNA Target.

Li, Shichang / Pradhan, Lagnajeet / Ashur, Shayan / Joshi, Anshu / Nam, Hyun-Joo

ACS omega

2019 Volume 4, Issue 6, Page(s) 10906–10914

Abstract: Forkhead transcription factor C2 (FOXC2) is a transcription factor regulating vascular and lymphatic development, and its mutations are linked to lymphedema-distichiasis syndrome. FOXC2 is also a crucial regulator of the epithelial-mesenchymal transition ...

Abstract	Forkhead transcription factor C2 (FOXC2) is a transcription factor regulating vascular and lymphatic development, and its mutations are linked to lymphedema-distichiasis syndrome. FOXC2 is also a crucial regulator of the epithelial-mesenchymal transition processes essential for tumor metastasis. Here, we report the crystal structure of the FOXC2-DNA-binding domain in complex with its cognate DNA. The crystal structure provides the basis of DNA sequence recognition by FOXC2 for the T/CAAAC motif. Helix 3 makes the majority of the DNA-protein interactions and confers the DNA sequence specificity. The computational energy calculation results also validate the structural observations. The FOXC2 and DNA complex structure provides a detailed picture of protein and DNA interactions, which allows us to predict its DNA recognition specificity and impaired functions in mutants identified in human patients.
Language	English
Publishing date	2019-06-24
Publishing country	United States
Document type	Journal Article
ISSN	2470-1343
ISSN (online)	2470-1343
DOI	10.1021/acsomega.9b00756
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Obvious to try and non-obviousness post KSR

Dhulap, Sivakami / Joshi, Anshu / Kulkarni, M. G

International journal of intellectual property management : IJIPM Vol. 8, No. 3/4 , p. 190-206

origins and implications

2015 Volume 8, Issue 3, Page(s) 190–206

Author's details	Sivakami Dhulap, Anshu Joshi and M.G. Kulkarni (Council of Scientific and Industrial Research-Unit for Research and Development of Information Products, Pune, Maharashtra, India)
Keywords	non-obviosuness ; patentability criteria ; pharmaceutical inventions ; post KSR ; obvious to try
Language	English
Publisher	Inderscience Enterprises
Publishing place	Genève [u.a.]
Document type	Article
ZDB-ID	2451202-3
ISSN	1478-9647
Database	ECONomics Information System

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Article ; Online: Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement.

McCallum, Matthew / Czudnochowski, Nadine / Rosen, Laura E / Zepeda, Samantha K / Bowen, John E / Walls, Alexandra C / Hauser, Kevin / Joshi, Anshu / Stewart, Cameron / Dillen, Josh R / Powell, Abigail E / Croll, Tristan I / Nix, Jay / Virgin, Herbert W / Corti, Davide / Snell, Gyorgy / Veesler, David

Science (New York, N.Y.)

2022 Volume 375, Issue 6583, Page(s) 864–868

Abstract: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant of concern evades antibody-mediated immunity that comes from vaccination or infection with earlier variants due to accumulation of numerous spike mutations. To understand ... ...

Abstract	The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant of concern evades antibody-mediated immunity that comes from vaccination or infection with earlier variants due to accumulation of numerous spike mutations. To understand the Omicron antigenic shift, we determined cryo-electron microscopy and x-ray crystal structures of the spike protein and the receptor-binding domain bound to the broadly neutralizing sarbecovirus monoclonal antibody (mAb) S309 (the parent mAb of sotrovimab) and to the human ACE2 receptor. We provide a blueprint for understanding the marked reduction of binding of other therapeutic mAbs that leads to dampened neutralizing activity. Remodeling of interactions between the Omicron receptor-binding domain and human ACE2 likely explains the enhanced affinity for the host receptor relative to the ancestral virus.
MeSH term(s)	Amino Acid Substitution ; Angiotensin-Converting Enzyme 2/chemistry ; Angiotensin-Converting Enzyme 2/metabolism ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/metabolism ; Antibodies, Viral/chemistry ; Antibodies, Viral/immunology ; Antibodies, Viral/metabolism ; Antigenic Drift and Shift ; Broadly Neutralizing Antibodies/chemistry ; Broadly Neutralizing Antibodies/immunology ; Broadly Neutralizing Antibodies/metabolism ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Humans ; Immune Evasion ; Models, Molecular ; Mutation ; Protein Binding ; Protein Conformation ; Protein Domains/genetics ; Protein Interaction Domains and Motifs/genetics ; Receptors, Coronavirus/chemistry ; Receptors, Coronavirus/metabolism ; SARS-CoV-2/chemistry ; SARS-CoV-2/genetics ; SARS-CoV-2/immunology ; SARS-CoV-2/physiology ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/immunology ; Spike Glycoprotein, Coronavirus/metabolism
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Viral ; Broadly Neutralizing Antibodies ; Receptors, Coronavirus ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Language	English
Publishing date	2022-01-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.abn8652
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: SARS-CoV-2 breakthrough infections elicit potent, broad, and durable neutralizing antibody responses.

Walls, Alexandra C / Sprouse, Kaitlin R / Bowen, John E / Joshi, Anshu / Franko, Nicholas / Navarro, Mary Jane / Stewart, Cameron / Cameroni, Elisabetta / McCallum, Matthew / Goecker, Erin A / Degli-Angeli, Emily J / Logue, Jenni / Greninger, Alex / Corti, Davide / Chu, Helen Y / Veesler, David

Cell

2022 Volume 185, Issue 5, Page(s) 872–880.e3

Abstract: Although infections among vaccinated individuals lead to milder COVID-19 symptoms relative to those in unvaccinated subjects, the specificity and durability of antibody responses elicited by breakthrough cases remain unknown. Here, we demonstrate that ... ...

Abstract	Although infections among vaccinated individuals lead to milder COVID-19 symptoms relative to those in unvaccinated subjects, the specificity and durability of antibody responses elicited by breakthrough cases remain unknown. Here, we demonstrate that breakthrough infections induce serum-binding and -neutralizing antibody responses that are markedly more potent, durable, and resilient to spike mutations observed in variants than those in subjects who received only 2 doses of vaccine. However, we show that breakthrough cases, subjects who were vaccinated after infection, and individuals vaccinated three times have serum-neutralizing activity of comparable magnitude and breadth, indicating that an increased number of exposures to SARS-CoV-2 antigen(s) enhance the quality of antibody responses. Neutralization of SARS-CoV was moderate, however, underscoring the importance of developing vaccines eliciting broad sarbecovirus immunity for pandemic preparedness.
Language	English
Publishing date	2022-01-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2022.01.011
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 1167: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Structure, receptor recognition, and antigenicity of the human coronavirus CCoV-HuPn-2018 spike glycoprotein.

Tortorici, M Alejandra / Walls, Alexandra C / Joshi, Anshu / Park, Young-Jun / Eguia, Rachel T / Miranda, Marcos C / Kepl, Elizabeth / Dosey, Annie / Stevens-Ayers, Terry / Boeckh, Michael J / Telenti, Amalio / Lanzavecchia, Antonio / King, Neil P / Corti, Davide / Bloom, Jesse D / Veesler, David

Cell

2022 Volume 185, Issue 13, Page(s) 2279–2291.e17

Abstract: The isolation of CCoV-HuPn-2018 from a child respiratory swab indicates that more coronaviruses are spilling over to humans than previously appreciated. We determined the structures of the CCoV-HuPn-2018 spike glycoprotein trimer in two distinct ... ...

Abstract	The isolation of CCoV-HuPn-2018 from a child respiratory swab indicates that more coronaviruses are spilling over to humans than previously appreciated. We determined the structures of the CCoV-HuPn-2018 spike glycoprotein trimer in two distinct conformational states and showed that its domain 0 recognizes sialosides. We identified that the CCoV-HuPn-2018 spike binds canine, feline, and porcine aminopeptidase N (APN) orthologs, which serve as entry receptors, and determined the structure of the receptor-binding B domain in complex with canine APN. The introduction of an oligosaccharide at position N739 of human APN renders cells susceptible to CCoV-HuPn-2018 spike-mediated entry, suggesting that single-nucleotide polymorphisms might account for viral detection in some individuals. Human polyclonal plasma antibodies elicited by HCoV-229E infection and a porcine coronavirus monoclonal antibody inhibit CCoV-HuPn-2018 spike-mediated entry, underscoring the cross-neutralizing activity among ɑ-coronaviruses. These data pave the way for vaccine and therapeutic development targeting this zoonotic pathogen representing the eighth human-infecting coronavirus.
MeSH term(s)	Animals ; CD13 Antigens/chemistry ; CD13 Antigens/metabolism ; Cats ; Cell Line ; Coronavirus/metabolism ; Coronavirus 229E, Human/metabolism ; Coronavirus Infections ; Dogs ; Humans ; Receptors, Virus/metabolism ; Spike Glycoprotein, Coronavirus/metabolism ; Swine
Chemical Substances	Receptors, Virus ; Spike Glycoprotein, Coronavirus ; CD13 Antigens (EC 3.4.11.2)
Language	English
Publishing date	2022-05-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2022.05.019
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: SARS-CoV-2 breakthrough infections elicit potent, broad, and durable neutralizing antibody responses

Walls, Alexandra C. / Sprouse, Kaitlin R. / Bowen, John E. / Joshi, Anshu / Franko, Nicholas / Navarro, Mary Jane / Stewart, Cameron / Cameroni, Elisabetta / McCallum, Matthew / Goecker, Erin A. / Degli-Angeli, Emily J. / Logue, Jenni / Greninger, Alex / Corti, Davide / Chu, Helen Y. / Veesler, David

Cell. 2022 Mar. 03, v. 185, no. 5

2022

Abstract	Although infections among vaccinated individuals lead to milder COVID-19 symptoms relative to those in unvaccinated subjects, the specificity and durability of antibody responses elicited by breakthrough cases remain unknown. Here, we demonstrate that breakthrough infections induce serum-binding and -neutralizing antibody responses that are markedly more potent, durable, and resilient to spike mutations observed in variants than those in subjects who received only 2 doses of vaccine. However, we show that breakthrough cases, subjects who were vaccinated after infection, and individuals vaccinated three times have serum-neutralizing activity of comparable magnitude and breadth, indicating that an increased number of exposures to SARS-CoV-2 antigen(s) enhance the quality of antibody responses. Neutralization of SARS-CoV was moderate, however, underscoring the importance of developing vaccines eliciting broad sarbecovirus immunity for pandemic preparedness.
Keywords	COVID-19 infection ; Severe acute respiratory syndrome coronavirus 2 ; antigens ; durability ; neutralization ; pandemic ; vaccines
Language	English
Dates of publication	2022-0303
Size	p. 872-880.e3.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2022.01.011
Database	NAL-Catalogue (AGRICOLA)

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Article: Structure, receptor recognition and antigenicity of the human coronavirus CCoV-HuPn-2018 spike glycoprotein

Tortorici, M. Alejandra / Walls, Alexandra C. / Joshi, Anshu / Park, Young-Jun / Eguia, Rachel T. / Miranda, Marcos C. / Kepl, Elizabeth / Dosey, Annie / Stevens-Ayers, Terry / Boeckh, Michael J. / Telenti, Amalio / Lanzavecchia, Antonio / King, Neil P. / Corti, Davide / Bloom, Jesse D. / Veesler, David

Cell. 2022 May 23,

2022

Abstract: The isolation of CCoV-HuPn-2018 from a child respiratory swab indicates that more coronaviruses are spilling over to humans than previously appreciated. We determined structures of the CCoV-HuPn-2018 spike glycoprotein trimer in two distinct ... ...

Abstract	The isolation of CCoV-HuPn-2018 from a child respiratory swab indicates that more coronaviruses are spilling over to humans than previously appreciated. We determined structures of the CCoV-HuPn-2018 spike glycoprotein trimer in two distinct conformational states and show that its domain 0 recognizes sialosides. We identified that the CCoV-HuPn-2018 spike binds canine, feline and porcine aminopeptidase N (APN) orthologs, which serve as entry receptors, and determined the structure of the receptor-binding B domain in complex with canine APN. Introduction of an oligosaccharide at position N739 of human APN renders cells susceptible to CCoV-HuPn-2018 spike-mediated entry, suggesting that single nucleotide polymorphisms might account for viral detection in some individuals. Human polyclonal plasma antibodies elicited by HCoV-229E infection and a porcine coronavirus monoclonal antibody inhibit CCoV-HuPn-2018 spike-mediated entry, underscoring cross-neutralizing activity among ɑ-coronaviruses. These data pave the way for vaccine and therapeutic development targeting this zoonotic pathogen representing the 8ᵗʰ human-infecting coronavirus.
Keywords	Orthocoronavirinae ; cats ; children ; dogs ; glycoproteins ; humans ; membrane alanyl aminopeptidase ; monoclonal antibodies ; oligosaccharides ; pathogens ; swine ; therapeutics ; vaccines
Language	English
Dates of publication	2022-0523
Publishing place	Elsevier Inc.
Document type	Article
Note	Pre-press version
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2022.05.019
Database	NAL-Catalogue (AGRICOLA)

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