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1
Structure, Function and Regulation of the Hsp90 Machinery
Structure, Function and Regulation of the Hsp90 Machinery
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Structure, Function and Regulation of the Hsp90 Machinery

Biomedical Journal, 2013-05, Vol.36 (3), p.106-117 [Peer Reviewed Journal]

COPYRIGHT 2013 Medknow Publications and Media Pvt. Ltd. ;Copyright Medknow Publications & Media Pvt Ltd May-Jun 2013 ;ISSN: 2319-4170 ;EISSN: 2320-2890 ;DOI: 10.4103/2319-4170.113230 ;PMID: 23806880

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2
Some of Domain Matrix Lamda Defined By φ-function
Some of Domain Matrix Lamda Defined By φ-function
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Some of Domain Matrix Lamda Defined By φ-function

Journal of physics. Conference series, 2018-12, Vol.1116 (2), p.22038 [Peer Reviewed Journal]

Published under licence by IOP Publishing Ltd ;2018. This work is published under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;ISSN: 1742-6588 ;EISSN: 1742-6596 ;DOI: 10.1088/1742-6596/1116/2/022038

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3
Closed range of ∂ ¯ on unbounded domains in ℂ n
Closed range of ∂ ¯ on unbounded domains in ℂ n
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Closed range of ∂ ¯ on unbounded domains in ℂ n

Journal d'analyse mathématique (Jerusalem), 2019-01, Vol.138 (1), p.185-208 [Peer Reviewed Journal]

Copyright Springer Nature B.V. 2019 ;ISSN: 0021-7670 ;EISSN: 1565-8538 ;DOI: 10.1007/s11854-019-0025-7

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4
SAMHD1 Functions and Human Diseases
SAMHD1 Functions and Human Diseases
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SAMHD1 Functions and Human Diseases

Viruses, 2020-03, Vol.12 (4), p.382 [Peer Reviewed Journal]

COPYRIGHT 2020 MDPI AG ;2020. This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2020 by the authors. 2020 ;ISSN: 1999-4915 ;EISSN: 1999-4915 ;DOI: 10.3390/v12040382 ;PMID: 32244340

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5
Preface
Preface
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Preface

Journal of physics. Conference series, 2019-09, Vol.1297 (1) [Peer Reviewed Journal]

2019. This work is published under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;ISSN: 1742-6588 ;EISSN: 1742-6596 ;DOI: 10.1088/1742-6596/1297/1/011001

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6
Tumour DDR1 promotes collagen fibre alignment to instigate immune exclusion
Tumour DDR1 promotes collagen fibre alignment to instigate immune exclusion
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Tumour DDR1 promotes collagen fibre alignment to instigate immune exclusion

Nature (London), 2021-11, Vol.599 (7886), p.673-678 [Peer Reviewed Journal]

2021. The Author(s), under exclusive licence to Springer Nature Limited. ;COPYRIGHT 2021 Nature Publishing Group ;Copyright Nature Publishing Group Nov 25, 2021 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/s41586-021-04057-2 ;PMID: 34732895

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7
Versatile and multivalent nanobodies efficiently neutralize SARS-CoV-2
Versatile and multivalent nanobodies efficiently neutralize SARS-CoV-2
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Versatile and multivalent nanobodies efficiently neutralize SARS-CoV-2

Science, 2020-12, Vol.370 (6523), p.1479-1484 [Peer Reviewed Journal]

Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. ;2020. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works ;Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works 2020 American Association for the Advancement of Science ;ISSN: 0036-8075 ;EISSN: 1095-9203 ;DOI: 10.1126/science.abe4747 ;PMID: 33154108

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8
The MRE11-RAD50-NBS1 Complex Conducts the Orchestration of Damage Signaling and Outcomes to Stress in DNA Replication and Repair
The MRE11-RAD50-NBS1 Complex Conducts the Orchestration of Damage Signaling and Outcomes to Stress in DNA Replication and Repair
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The MRE11-RAD50-NBS1 Complex Conducts the Orchestration of Damage Signaling and Outcomes to Stress in DNA Replication and Repair

Annual review of biochemistry, 2018-06, Vol.87 (1), p.263-294 [Peer Reviewed Journal]

Copyright Annual Reviews, Inc. 2018 ;ISSN: 0066-4154 ;EISSN: 1545-4509 ;DOI: 10.1146/annurev-biochem-062917-012415 ;PMID: 29709199

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9
Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain
Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain
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Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain

Nature communications, 2022-03, Vol.13 (1), p.1214-1214, Article 1214 [Peer Reviewed Journal]

2022. The Author(s). ;The Author(s) 2022. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;The Author(s) 2022 ;ISSN: 2041-1723 ;EISSN: 2041-1723 ;DOI: 10.1038/s41467-022-28882-9 ;PMID: 35241675

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10
Functional interplay between protein domains in a supramodular structure involving the postsynaptic density protein PSD-95
Functional interplay between protein domains in a supramodular structure involving the postsynaptic density protein PSD-95
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Functional interplay between protein domains in a supramodular structure involving the postsynaptic density protein PSD-95

The Journal of biological chemistry, 2020-02, Vol.295 (7), p.1992-2000 [Peer Reviewed Journal]

2020 © 2020 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2020 Laursen et al. ;2020 Laursen et al. 2020 Laursen et al. ;ISSN: 0021-9258 ;ISSN: 1083-351X ;EISSN: 1083-351X ;DOI: 10.1074/jbc.RA119.011050 ;PMID: 31831623

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11
Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein
Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein
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Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein

Antiviral research, 2018-01, Vol.149, p.58 [Peer Reviewed Journal]

Copyright © 2017 Elsevier B.V. All rights reserved. ;EISSN: 1872-9096 ;DOI: 10.1016/j.antiviral.2017.11.001 ;PMID: 29128390

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12
Protein docking using case-based reasoning
Protein docking using case-based reasoning
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Protein docking using case-based reasoning

Proteins, structure, function, and bioinformatics, 2013-12, Vol.81 (12), p.2150-2158 [Peer Reviewed Journal]

Copyright © 2013 Wiley Periodicals, Inc. ;This article is protected by copyright. All rights reserved. ;Distributed under a Creative Commons Attribution 4.0 International License ;ISSN: 0887-3585 ;EISSN: 1097-0134 ;DOI: 10.1002/prot.24433 ;PMID: 24123156

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13
NAD + cleavage activity by animal and plant TIR domains in cell death pathways
NAD + cleavage activity by animal and plant TIR domains in cell death pathways
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NAD + cleavage activity by animal and plant TIR domains in cell death pathways

Science (American Association for the Advancement of Science), 2019-08, Vol.365 (6455), p.793-799 [Peer Reviewed Journal]

Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. ;Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works ;ISSN: 0036-8075 ;EISSN: 1095-9203 ;DOI: 10.1126/science.aax1911 ;PMID: 31439792

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14
Chemical inhibitors targeting histone methylation readers
Chemical inhibitors targeting histone methylation readers
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Chemical inhibitors targeting histone methylation readers

Pharmacology & therapeutics (Oxford), 2024-04, Vol.256, p.108614 [Peer Reviewed Journal]

Copyright © 2024 Elsevier Inc. All rights reserved. ;EISSN: 1879-016X ;DOI: 10.1016/j.pharmthera.2024.108614 ;PMID: 38401773

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15
MetaDome: Pathogenicity analysis of genetic variants through aggregation of homologous human protein domains
MetaDome: Pathogenicity analysis of genetic variants through aggregation of homologous human protein domains
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MetaDome: Pathogenicity analysis of genetic variants through aggregation of homologous human protein domains

Human mutation, 2019-08, Vol.40 (8), p.1030-1038, Article humu.23798 [Peer Reviewed Journal]

2019 The Authors. Published by Wiley Periodicals, Inc. ;2019 The Authors. Human Mutation Published by Wiley Periodicals, Inc. ;2019 Wiley Periodicals, Inc. ;ISSN: 1059-7794 ;EISSN: 1098-1004 ;DOI: 10.1002/humu.23798 ;PMID: 31116477

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16
A Cyclin-Binding Motif in Human SAMHD1 Is Required for Its HIV-1 Restriction, dNTPase Activity, Tetramer Formation, and Efficient Phosphorylation
A Cyclin-Binding Motif in Human SAMHD1 Is Required for Its HIV-1 Restriction, dNTPase Activity, Tetramer Formation, and Efficient Phosphorylation
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A Cyclin-Binding Motif in Human SAMHD1 Is Required for Its HIV-1 Restriction, dNTPase Activity, Tetramer Formation, and Efficient Phosphorylation

Journal of virology, 2018-03, Vol.92 (6) [Peer Reviewed Journal]

Copyright © 2018 American Society for Microbiology. ;Copyright © 2018 American Society for Microbiology. 2018 American Society for Microbiology ;ISSN: 0022-538X ;EISSN: 1098-5514 ;DOI: 10.1128/JVI.01787-17 ;PMID: 29321329

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17
The SAM domain of mouse SAMHD1 is critical for its activation and regulation
The SAM domain of mouse SAMHD1 is critical for its activation and regulation
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The SAM domain of mouse SAMHD1 is critical for its activation and regulation

Nature communications, 2018-01, Vol.9 (1), p.411-9, Article 411 [Peer Reviewed Journal]

2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;The Author(s) 2018 ;ISSN: 2041-1723 ;EISSN: 2041-1723 ;DOI: 10.1038/s41467-017-02783-8 ;PMID: 29379009

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18
Functional degradation: A mechanism of NLRP1 inflammasome activation by diverse pathogen enzymes
Functional degradation: A mechanism of NLRP1 inflammasome activation by diverse pathogen enzymes
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Functional degradation: A mechanism of NLRP1 inflammasome activation by diverse pathogen enzymes

Science (American Association for the Advancement of Science), 2019-04, Vol.364 (6435) [Peer Reviewed Journal]

Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. ;Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works ;ISSN: 0036-8075 ;EISSN: 1095-9203 ;DOI: 10.1126/science.aau1330 ;PMID: 30872533

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19
A structural prospective for collagen receptors such as DDR and their binding of the collagen fibril
A structural prospective for collagen receptors such as DDR and their binding of the collagen fibril
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A structural prospective for collagen receptors such as DDR and their binding of the collagen fibril

Biochimica et biophysica acta. Molecular cell research, 2019-11, Vol.1866 (11), p.118478 [Peer Reviewed Journal]

Copyright © 2019 Elsevier B.V. All rights reserved. ;EISSN: 1879-2596 ;DOI: 10.1016/j.bbamcr.2019.04.008 ;PMID: 31004686

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20
Searching for single domain magnetite in the "pseudo-single-domain" sedimentary haystack: Implications of biogenic magnetite preservation for sediment magnetism and relative paleointensity determinations
Searching for single domain magnetite in the "pseudo-single-domain" sedimentary haystack: Implications of biogenic magnetite preservation for sediment magnetism and relative paleointensity determinations
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Searching for single domain magnetite in the "pseudo-single-domain" sedimentary haystack: Implications of biogenic magnetite preservation for sediment magnetism and relative paleointensity determinations

Journal of Geophysical Research: Solid Earth, 2012-08, Vol.117 (B8), p.n/a [Peer Reviewed Journal]

Published in 2012 by the American Geophysical Union ;2015 INIST-CNRS ;ISSN: 0148-0227 ;ISSN: 2169-9313 ;EISSN: 2156-2202 ;EISSN: 2169-9356 ;DOI: 10.1029/2012JB009412

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