Pub Date : 2024-02-13DOI: 10.1080/0889311x.2024.2311172
Oksana Danylyuk
This review focuses on the pathway-dependent crystallization of the host–guest complexes based on the macrocyclic host molecules in aqueous media. The high degree of structural diversity from the s...
{"title":"Host–guest complexes in the crystal land: a plethora of crystal forms and crystallization peculiarities","authors":"Oksana Danylyuk","doi":"10.1080/0889311x.2024.2311172","DOIUrl":"https://doi.org/10.1080/0889311x.2024.2311172","url":null,"abstract":"This review focuses on the pathway-dependent crystallization of the host–guest complexes based on the macrocyclic host molecules in aqueous media. The high degree of structural diversity from the s...","PeriodicalId":54385,"journal":{"name":"Crystallography Reviews","volume":"5 1","pages":""},"PeriodicalIF":3.0,"publicationDate":"2024-02-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139769560","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2023-11-22DOI: 10.1080/0889311x.2023.2282799
Petra Bombicz
the ‘Structural Biology of SARS-CoV-2 Exori-bonuclease/N7 Methyltransferase (nsp14), 2 (cid:2) O methyltransferase (nsp16)
发表于《晶体学评论》(Vol. 29, No. 3, 2023)
{"title":"Reviews on the structural and non-structural proteins of SARS-CoV-2, and anharmonic description of atomic vibrations","authors":"Petra Bombicz","doi":"10.1080/0889311x.2023.2282799","DOIUrl":"https://doi.org/10.1080/0889311x.2023.2282799","url":null,"abstract":"the ‘Structural Biology of SARS-CoV-2 Exori-bonuclease/N7 Methyltransferase (nsp14), 2 (cid:2) O methyltransferase (nsp16)","PeriodicalId":54385,"journal":{"name":"Crystallography Reviews","volume":"5 4","pages":""},"PeriodicalIF":3.0,"publicationDate":"2023-11-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138511970","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2023-11-05DOI: 10.1080/0889311x.2023.2266400
S. N. Volkov, D. O. Charkin, V. A. Firsova, S. M. Aksenov, R. S. Bubnova
All thermal vibrations of atoms are in fact anharmonic – this is the underlying reason for the manifestation of many physical properties of solids, primarily its thermal expansion. By now, over thr...
{"title":"Gram–Charlier approach for anharmonic atomic displacements in inorganic solids: A review","authors":"S. N. Volkov, D. O. Charkin, V. A. Firsova, S. M. Aksenov, R. S. Bubnova","doi":"10.1080/0889311x.2023.2266400","DOIUrl":"https://doi.org/10.1080/0889311x.2023.2266400","url":null,"abstract":"All thermal vibrations of atoms are in fact anharmonic – this is the underlying reason for the manifestation of many physical properties of solids, primarily its thermal expansion. By now, over thr...","PeriodicalId":54385,"journal":{"name":"Crystallography Reviews","volume":"3 4","pages":""},"PeriodicalIF":3.0,"publicationDate":"2023-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138511977","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2023-11-05DOI: 10.1080/0889311x.2023.2253735
Luise Kandler, Oliver Kippes, Maximilian Edich, Sabrina Stäb, Gianluca Santoni, Andrea Thorn
The structural proteins located on the SARS-CoV-2 envelope, namely the spike, membrane and envelope protein, play important roles during the entire viral infection cycle. For example, the interacti...
{"title":"SARS-CoV-2 envelope protein and its relationship to the membrane protein","authors":"Luise Kandler, Oliver Kippes, Maximilian Edich, Sabrina Stäb, Gianluca Santoni, Andrea Thorn","doi":"10.1080/0889311x.2023.2253735","DOIUrl":"https://doi.org/10.1080/0889311x.2023.2253735","url":null,"abstract":"The structural proteins located on the SARS-CoV-2 envelope, namely the spike, membrane and envelope protein, play important roles during the entire viral infection cycle. For example, the interacti...","PeriodicalId":54385,"journal":{"name":"Crystallography Reviews","volume":"85 3","pages":""},"PeriodicalIF":3.0,"publicationDate":"2023-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138511972","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2023-10-28DOI: 10.1080/0889311x.2023.2268534
Cameron Fyfe, Lea C. von Soosten, Gianluca Santoni, Andrea Thorn
{"title":"Structural biology of SARS-CoV-2 exoribonuclease/N7–methyltransferase (nsp14), 2′–O–methyltransferase (nsp16) and their enhancing protein (nsp10)","authors":"Cameron Fyfe, Lea C. von Soosten, Gianluca Santoni, Andrea Thorn","doi":"10.1080/0889311x.2023.2268534","DOIUrl":"https://doi.org/10.1080/0889311x.2023.2268534","url":null,"abstract":"","PeriodicalId":54385,"journal":{"name":"Crystallography Reviews","volume":"279 3","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-10-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136233691","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2023-04-03DOI: 10.1080/0889311X.2023.2248841
P. Bombicz
Proteins perform incredibly diverse and highly selective functions. It is the consequence of their finely tuned three-dimensional structure. The ‘lock-and-key’ model used for more than a century refers to the classical structure-function paradigm. However, as Professor Giuseppe Zanotti of theUniversity of Padua, Italy reviews for usmany protein functions do not require a unique structure. The carriers of such structure-independent functions are the intrinsically disordered regions among ordered domains of proteins (IDRs), or the fully, intrinsically, disordered proteins (IDPs). IDRs and IDPs frequently occur in nature in all proteomes of organisms. The abundance of disorder, the lack of a fixed quaternary protein structure increases proportionally with the complexity of the organism. The presence of significantly disordered regions is estimated around 33% in the eukaryotic proteins and 35% in the human proteome. And in his final note, Giuseppe Zanotti states
{"title":"Structural biology and drug design: conformational stability, flexibility and disordering; the SARS-CoV-1/SARS-CoV-2 main protease; first two Springer/IUCr Briefs","authors":"P. Bombicz","doi":"10.1080/0889311X.2023.2248841","DOIUrl":"https://doi.org/10.1080/0889311X.2023.2248841","url":null,"abstract":"Proteins perform incredibly diverse and highly selective functions. It is the consequence of their finely tuned three-dimensional structure. The ‘lock-and-key’ model used for more than a century refers to the classical structure-function paradigm. However, as Professor Giuseppe Zanotti of theUniversity of Padua, Italy reviews for usmany protein functions do not require a unique structure. The carriers of such structure-independent functions are the intrinsically disordered regions among ordered domains of proteins (IDRs), or the fully, intrinsically, disordered proteins (IDPs). IDRs and IDPs frequently occur in nature in all proteomes of organisms. The abundance of disorder, the lack of a fixed quaternary protein structure increases proportionally with the complexity of the organism. The presence of significantly disordered regions is estimated around 33% in the eukaryotic proteins and 35% in the human proteome. And in his final note, Giuseppe Zanotti states","PeriodicalId":54385,"journal":{"name":"Crystallography Reviews","volume":"29 1","pages":"45 - 47"},"PeriodicalIF":3.0,"publicationDate":"2023-04-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46414323","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2023-04-03DOI: 10.1080/0889311X.2023.2222275
Yunyun Gao, J. Kaub, G. Santoni, N. Pearce, A. Thorn
The SARS-CoV-1/SARS-CoV-2 main protease cleaves the nascent viral polyproteins into biologically functional molecules, which are essential for viral reproduction inside the host cell. With more than 500 crystal structures available, it is one of the most heavily researched coronavirus proteins and a popular drug target. This review focuses on putting the function and structure of the main protease into a historical perspective, highlighting the structure-based design of inhibitors of the main protease and discussing potential future research directions.
{"title":"Structural biology of SARS-CoV-1/SARS-CoV-2 main protease","authors":"Yunyun Gao, J. Kaub, G. Santoni, N. Pearce, A. Thorn","doi":"10.1080/0889311X.2023.2222275","DOIUrl":"https://doi.org/10.1080/0889311X.2023.2222275","url":null,"abstract":"The SARS-CoV-1/SARS-CoV-2 main protease cleaves the nascent viral polyproteins into biologically functional molecules, which are essential for viral reproduction inside the host cell. With more than 500 crystal structures available, it is one of the most heavily researched coronavirus proteins and a popular drug target. This review focuses on putting the function and structure of the main protease into a historical perspective, highlighting the structure-based design of inhibitors of the main protease and discussing potential future research directions.","PeriodicalId":54385,"journal":{"name":"Crystallography Reviews","volume":"29 1","pages":"76 - 101"},"PeriodicalIF":3.0,"publicationDate":"2023-04-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42642843","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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