cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.5517/ccdc.csd.cc282fph
title: CCDC 2087716: Experimental Crystal Structure Determination

description: Related Article: Daniel J. Blair, Sriyankari Chitti, Melanie Trobe, David M. Kostyra, Hannah M. S. Haley, Richard L. Hansen, Steve G. Ballmer, Toby J. Woods, Wesley Wang, Vikram Mubayi, Michael J. Schmidt, Robert W. Pipal, Greg. F. Morehouse, Andrea M. E. Palazzolo Ray, Danielle L. Gray, Adrian L. Gill, Martin D. Burke|2022|Nature (London)|604|92|doi:10.1038/s41586-022-04491-w
DOI: 10.5517/ccdc.csd.cc28bwfy
title: CCDC 2095830: Experimental Crystal Structure Determination

description: Related Article: Constance Lecourt, Yan Suffren, Erwann Jeanneau, Dominique Luneau, Cédric Desroches|2022|Cryst.Growth Des.|22|2279|doi:10.1021/acs.cgd.1c01348
DOI: 10.5517/ccdc.csd.cc28y36k
title: CCDC 2113338: Experimental Crystal Structure Determination

description: Related Article: Ryusei Oketani, Hiroki Takahashi, Simon Clevers, Akira Oyamada, Ichiro Hisaki, Gérard Coquerel, Kazuaki Yamanaka, Hirohito Tsue|2022|Cryst.Growth Des.|22|2230|doi:10.1021/acs.cgd.1c01330
DOI: 10.5517/ccdc.csd.cc28y35j
title: CCDC 2113337: Experimental Crystal Structure Determination

description: Related Article: Ryusei Oketani, Hiroki Takahashi, Simon Clevers, Akira Oyamada, Ichiro Hisaki, Gérard Coquerel, Kazuaki Yamanaka, Hirohito Tsue|2022|Cryst.Growth Des.|22|2230|doi:10.1021/acs.cgd.1c01330
DOI: 10.5517/ccdc.csd.cc28y37l
title: CCDC 2113339: Experimental Crystal Structure Determination

description: Related Article: Ryusei Oketani, Hiroki Takahashi, Simon Clevers, Akira Oyamada, Ichiro Hisaki, Gérard Coquerel, Kazuaki Yamanaka, Hirohito Tsue|2022|Cryst.Growth Des.|22|2230|doi:10.1021/acs.cgd.1c01330
DOI: 10.5517/ccdc.csd.cc28y34h
title: CCDC 2113336: Experimental Crystal Structure Determination

description: Related Article: Ryusei Oketani, Hiroki Takahashi, Simon Clevers, Akira Oyamada, Ichiro Hisaki, Gérard Coquerel, Kazuaki Yamanaka, Hirohito Tsue|2022|Cryst.Growth Des.|22|2230|doi:10.1021/acs.cgd.1c01330
DOI: 10.5517/ccdc.csd.cc295k79
title: CCDC 2120500: Experimental Crystal Structure Determination

description: Related Article: Daniel J. Blair, Sriyankari Chitti, Melanie Trobe, David M. Kostyra, Hannah M. S. Haley, Richard L. Hansen, Steve G. Ballmer, Toby J. Woods, Wesley Wang, Vikram Mubayi, Michael J. Schmidt, Robert W. Pipal, Greg. F. Morehouse, Andrea M. E. Palazzolo Ray, Danielle L. Gray, Adrian L. Gill, Martin D. Burke|2022|Nature (London)|604|92|doi:10.1038/s41586-022-04491-w
DOI: 10.48370/ofd/nkxecx
title: Plagionotus bartholomei (Motschulsky, 1859), C-868

description: Coleoptera collection
DOI: 10.48370/ofd/k2trul
title: Xylotrechus capricornis (Gebler, 1830), C-869

description: Coleoptera collection
DOI: 10.48370/ofd/dkyxxq
title: Xylotrechus sieversi (Ganglbauer, 1890), C-870

description: Coleoptera collection
DOI: 10.34740/kaggle/dsv/3491522
title: Dalle-2
DOI: 10.6084/m9.figshare.19446938.v7
title: Dataset of energetic value estimates for BaYaka food items/ Base de données des estimations de la valeur énergétique des produits alimentaires BaYaka

description: We present a database that systematically estimates the energetic value of wild and domesticated food resources collected and consumed by Congolese BaYaka foragers. This dataset is unique in that it accounts for everyday practices of food processing and consumption. Reported values of inedible portions, moisture content, and estimated energetic values (kcal/g) were extracted from field research and the published food chemistry and nutrition literature. These data are central to understanding how nutritional needs are met in rainforest environments and will allow for current and future tracking of diet composition in this environment and in similar ecologies.<br>Nous présentons un ensemble de données qui estime systématiquement la valeur énergétique des ressources alimentaires sauvages et domestiques collectées et consommées par les fourrageurs congolais BaYaka. Cet ensemble de données est unique dans la mesure où il tient compte des pratiques quotidiennes de transformation et de consommation des aliments. Les valeurs rapportées des portions non comestibles, la teneur en humidité et les valeurs énergétiques estimées (kcal/g) ont été extraites des recherches sur le terrain et de la littérature publiée sur la chimie alimentaire et la nutrition. Ces données sont essentielles pour comprendre comment les besoins nutritionnels sont satisfaits dans les environnements de forêt tropicale et permettront de suivre la composition du régime alimentaire dans cet environnement et dans des écologies similaires.<br>
DOI: 10.6084/m9.figshare.19446938.v8
title: Dataset of energetic value estimates for BaYaka food items/ Base de données des estimations de la valeur énergétique des produits alimentaires BaYaka

description: We present a database that systematically estimates the energetic value of wild and domesticated food resources collected and consumed by Congolese BaYaka foragers. This dataset is unique in that it accounts for everyday practices of food processing and consumption. Reported values of inedible portions, moisture content, and estimated energetic values (kcal/g) were extracted from field research and the published food chemistry and nutrition literature. These data are central to understanding how nutritional needs are met in rainforest environments and will allow for current and future tracking of diet composition in this environment and in similar ecologies.<br>Nous présentons un ensemble de données qui estime systématiquement la valeur énergétique des ressources alimentaires sauvages et domestiques collectées et consommées par les fourrageurs congolais BaYaka. Cet ensemble de données est unique dans la mesure où il tient compte des pratiques quotidiennes de transformation et de consommation des aliments. Les valeurs rapportées des portions non comestibles, la teneur en humidité et les valeurs énergétiques estimées (kcal/g) ont été extraites des recherches sur le terrain et de la littérature publiée sur la chimie alimentaire et la nutrition. Ces données sont essentielles pour comprendre comment les besoins nutritionnels sont satisfaits dans les environnements de forêt tropicale et permettront de suivre la composition du régime alimentaire dans cet environnement et dans des écologies similaires.<br>
DOI: 10.6084/m9.figshare.19614604
title: AlphaFold2 model of Syn-ChlG from The terminal enzymes of (bacterio)chlorophyll biosynthesis

description: (Bacterio)chlorophylls are modified tetrapyrroles that are used by phototrophic organisms to harvest solar energy, powering the metabolic processes that sustain most of the life on Earth. Biosynthesis of these pigments involves enzymatic modification of the side chains and oxidation state of a porphyrin precursor, modifications that differ by species and alter the absorption properties of the pigments. (Bacterio)chlorophylls are coordinated by proteins that form macromolecular assemblies to absorb light and transfer excitation energy to a special pair of redox-active (bacterio)chlorophyll molecules in the photosynthetic reaction centre. Assembly of these pigment–protein complexes is aided by an isoprenoid moiety esterified to the (bacterio)chlorin macrocycle, which anchors and stabilizes the pigments within their protein scaffolds. The reduction of the isoprenoid ‘tail’ and its addition to the macrocycle are the final stages in (bacterio)chlorophyll biosynthesis and are catalysed by two enzymes, geranylgeranyl reductase and (bacterio)chlorophyll synthase. These enzymes work in conjunction with photosynthetic complex assembly factors and the membrane biogenesis machinery to synchronize delivery of the pigments to the proteins that coordinate them. In this review, we summarize current understanding of the catalytic mechanism, substrate recognition and regulation of these crucial enzymes and their involvement in thylakoid biogenesis and photosystem repair in oxygenic phototrophs.
DOI: 10.6084/m9.figshare.19614604.v1
title: AlphaFold2 model of Syn-ChlG from The terminal enzymes of (bacterio)chlorophyll biosynthesis

description: (Bacterio)chlorophylls are modified tetrapyrroles that are used by phototrophic organisms to harvest solar energy, powering the metabolic processes that sustain most of the life on Earth. Biosynthesis of these pigments involves enzymatic modification of the side chains and oxidation state of a porphyrin precursor, modifications that differ by species and alter the absorption properties of the pigments. (Bacterio)chlorophylls are coordinated by proteins that form macromolecular assemblies to absorb light and transfer excitation energy to a special pair of redox-active (bacterio)chlorophyll molecules in the photosynthetic reaction centre. Assembly of these pigment–protein complexes is aided by an isoprenoid moiety esterified to the (bacterio)chlorin macrocycle, which anchors and stabilizes the pigments within their protein scaffolds. The reduction of the isoprenoid ‘tail’ and its addition to the macrocycle are the final stages in (bacterio)chlorophyll biosynthesis and are catalysed by two enzymes, geranylgeranyl reductase and (bacterio)chlorophyll synthase. These enzymes work in conjunction with photosynthetic complex assembly factors and the membrane biogenesis machinery to synchronize delivery of the pigments to the proteins that coordinate them. In this review, we summarize current understanding of the catalytic mechanism, substrate recognition and regulation of these crucial enzymes and their involvement in thylakoid biogenesis and photosystem repair in oxygenic phototrophs.
DOI: 10.6084/m9.figshare.19614607
title: AlphaFold2 model of At-ChlG from The terminal enzymes of (bacterio)chlorophyll biosynthesis

description: (Bacterio)chlorophylls are modified tetrapyrroles that are used by phototrophic organisms to harvest solar energy, powering the metabolic processes that sustain most of the life on Earth. Biosynthesis of these pigments involves enzymatic modification of the side chains and oxidation state of a porphyrin precursor, modifications that differ by species and alter the absorption properties of the pigments. (Bacterio)chlorophylls are coordinated by proteins that form macromolecular assemblies to absorb light and transfer excitation energy to a special pair of redox-active (bacterio)chlorophyll molecules in the photosynthetic reaction centre. Assembly of these pigment–protein complexes is aided by an isoprenoid moiety esterified to the (bacterio)chlorin macrocycle, which anchors and stabilizes the pigments within their protein scaffolds. The reduction of the isoprenoid ‘tail’ and its addition to the macrocycle are the final stages in (bacterio)chlorophyll biosynthesis and are catalysed by two enzymes, geranylgeranyl reductase and (bacterio)chlorophyll synthase. These enzymes work in conjunction with photosynthetic complex assembly factors and the membrane biogenesis machinery to synchronize delivery of the pigments to the proteins that coordinate them. In this review, we summarize current understanding of the catalytic mechanism, substrate recognition and regulation of these crucial enzymes and their involvement in thylakoid biogenesis and photosystem repair in oxygenic phototrophs.
DOI: 10.6084/m9.figshare.19614607.v1
title: AlphaFold2 model of At-ChlG from The terminal enzymes of (bacterio)chlorophyll biosynthesis

description: (Bacterio)chlorophylls are modified tetrapyrroles that are used by phototrophic organisms to harvest solar energy, powering the metabolic processes that sustain most of the life on Earth. Biosynthesis of these pigments involves enzymatic modification of the side chains and oxidation state of a porphyrin precursor, modifications that differ by species and alter the absorption properties of the pigments. (Bacterio)chlorophylls are coordinated by proteins that form macromolecular assemblies to absorb light and transfer excitation energy to a special pair of redox-active (bacterio)chlorophyll molecules in the photosynthetic reaction centre. Assembly of these pigment–protein complexes is aided by an isoprenoid moiety esterified to the (bacterio)chlorin macrocycle, which anchors and stabilizes the pigments within their protein scaffolds. The reduction of the isoprenoid ‘tail’ and its addition to the macrocycle are the final stages in (bacterio)chlorophyll biosynthesis and are catalysed by two enzymes, geranylgeranyl reductase and (bacterio)chlorophyll synthase. These enzymes work in conjunction with photosynthetic complex assembly factors and the membrane biogenesis machinery to synchronize delivery of the pigments to the proteins that coordinate them. In this review, we summarize current understanding of the catalytic mechanism, substrate recognition and regulation of these crucial enzymes and their involvement in thylakoid biogenesis and photosystem repair in oxygenic phototrophs.
DOI: 10.6084/m9.figshare.19614610.v1
title: AlphaFold2 model of Rba-BchG from The terminal enzymes of (bacterio)chlorophyll biosynthesis

description: (Bacterio)chlorophylls are modified tetrapyrroles that are used by phototrophic organisms to harvest solar energy, powering the metabolic processes that sustain most of the life on Earth. Biosynthesis of these pigments involves enzymatic modification of the side chains and oxidation state of a porphyrin precursor, modifications that differ by species and alter the absorption properties of the pigments. (Bacterio)chlorophylls are coordinated by proteins that form macromolecular assemblies to absorb light and transfer excitation energy to a special pair of redox-active (bacterio)chlorophyll molecules in the photosynthetic reaction centre. Assembly of these pigment–protein complexes is aided by an isoprenoid moiety esterified to the (bacterio)chlorin macrocycle, which anchors and stabilizes the pigments within their protein scaffolds. The reduction of the isoprenoid ‘tail’ and its addition to the macrocycle are the final stages in (bacterio)chlorophyll biosynthesis and are catalysed by two enzymes, geranylgeranyl reductase and (bacterio)chlorophyll synthase. These enzymes work in conjunction with photosynthetic complex assembly factors and the membrane biogenesis machinery to synchronize delivery of the pigments to the proteins that coordinate them. In this review, we summarize current understanding of the catalytic mechanism, substrate recognition and regulation of these crucial enzymes and their involvement in thylakoid biogenesis and photosystem repair in oxygenic phototrophs.
DOI: 10.6084/m9.figshare.19614610
title: AlphaFold2 model of Rba-BchG from The terminal enzymes of (bacterio)chlorophyll biosynthesis

description: (Bacterio)chlorophylls are modified tetrapyrroles that are used by phototrophic organisms to harvest solar energy, powering the metabolic processes that sustain most of the life on Earth. Biosynthesis of these pigments involves enzymatic modification of the side chains and oxidation state of a porphyrin precursor, modifications that differ by species and alter the absorption properties of the pigments. (Bacterio)chlorophylls are coordinated by proteins that form macromolecular assemblies to absorb light and transfer excitation energy to a special pair of redox-active (bacterio)chlorophyll molecules in the photosynthetic reaction centre. Assembly of these pigment–protein complexes is aided by an isoprenoid moiety esterified to the (bacterio)chlorin macrocycle, which anchors and stabilizes the pigments within their protein scaffolds. The reduction of the isoprenoid ‘tail’ and its addition to the macrocycle are the final stages in (bacterio)chlorophyll biosynthesis and are catalysed by two enzymes, geranylgeranyl reductase and (bacterio)chlorophyll synthase. These enzymes work in conjunction with photosynthetic complex assembly factors and the membrane biogenesis machinery to synchronize delivery of the pigments to the proteins that coordinate them. In this review, we summarize current understanding of the catalytic mechanism, substrate recognition and regulation of these crucial enzymes and their involvement in thylakoid biogenesis and photosystem repair in oxygenic phototrophs.
DOI: 10.48370/ofd/avec8b
title: Xylotrechus ilamensis ssp. campadelli (Sama, 1992), C-871

description: Coleoptera collection
DOI: 10.48370/ofd/funszn
title: Amyloxenasma allantosporum (Oberw.) Hjortstam Ryvarden, 2514

description: Fungarium Macromycetes
DOI: 10.48370/ofd/9adywx
title: Xylotrechus ilamensis ssp. campadelli (Sama, 1992), C-872

description: Coleoptera collection
DOI: 10.48370/ofd/hmu631
title: Athelopsis glaucina (Bourdot Galzin) Oberw. ex Parmasto, 1437

description: Fungarium Macromycetes
DOI: 10.48370/ofd/xihlt1/jocwg3
title: Xylotrechus cuneipennis.JPG

description: :unav
DOI: 10.48370/ofd/xihlt1
title: Xylotrechus cuneipennis (Kraatz, 1879), C-873

description: Coleoptera collection
DOI: 10.21227/ag6z-ck74
title: Transducer Design for Clamp-on Guided Wave Flow Measurement in Thin-walled Pipes

description: Clamp-on ultrasonic transit time difference flow meters provide opportunities for metering where it is impractical or undesirable to cut into an existing pipeline to install an alternative flow meter. Up until now, it has been difficult to perform this type of measurement on thin-walled metal pipes, due to the difficulty of interpreting the guided wave modes in the combined pipe wall and internal fluid system, but a new method has been reported recently that utilises these guided wave modes for flow measurement. Through computational modelling, and construction and testing of different transducers, the design considerations for clamp-on transducers are highlighted and their impact on guided wave flow rate measurement is evaluated. The design features considered include a curved contact face to provide focusing of the ultrasound within the pipe and a scattering surface to reduce internal reflections. It is found that additional unwanted ultrasonic modes can be minimised by ultrasonic transducer wedge design features such as profiling the curvature of the transducer to conform to the pipe wall or creating a scattering edge to minimise internal wedge reflections. It is also observed that minimising these unwanted modes does not offer any advantage for the transit time difference measurement used in calculating flow.
DOI: 10.48370/ofd/q8kjch/hwz2qx
title: MIRPAS_coll_130686_VulpesVulpes_1978_scan.jpg

description: :unav
DOI: 10.48370/ofd/q8kjch
title: Vulpes vulpes - 130686, Zoological collection of the Mammal Research Institute, PAS

description: Vulpes vulpes (Red fox) from Zoological collection of the Mammal Research Institute PAS. Collected 1978-12-03, in: Tofiłowce, Poland.
DOI: 10.48370/ofd/jpouzz/823uwh
title: MIRPAS_coll_164828_VulpesVulpes_1996_scan.jpg

description: :unav
DOI: 10.48370/ofd/6hodeu
title: Xylotrechus adspersus (Gebler, 1830), C-874

description: Coleoptera collection
DOI: 10.48370/ofd/jpouzz
title: Vulpes vulpes - 164828, Zoological collection of the Mammal Research Institute, PAS

description: Vulpes vulpes (Red fox) from Zoological collection of the Mammal Research Institute PAS. Collected 1996-12-10, in: Ladzka Forest, Poland.
DOI: 10.48370/ofd/8d3eoj/5w4tyw
title: MIRPAS_coll_164829_VulpesVulpes_1996_scan.jpg

description: :unav
DOI: 10.48370/ofd/8d3eoj
title: Vulpes vulpes - 164829, Zoological collection of the Mammal Research Institute, PAS

description: Vulpes vulpes (Red fox) from Zoological collection of the Mammal Research Institute PAS. Collected 1996-12-10, in: Ladzka Forest, Poland.
DOI: 10.48370/ofd/6ifxbr
title: Athelopsis lacerata (Litsch.) J.Erikss. Ryvarden, 4372

description: Fungarium Macromycetes
DOI: 10.48370/ofd/0mlziw/euuy1j
title: MRIPAS_coll_36376_VespertilioMurinus_1964_scan.jpg

description: :unav
DOI: 10.48370/ofd/0mlziw/2fucwc
title: MRIPAS_coll_36376_VespertilioMurinus_1964_F_scan_ct.swf

description: :unav
DOI: 10.48370/ofd/0mlziw
title: Vespertilio murinus - 36376, Zoological collection of the Mammal Research Institute, PAS

description: Vespertilio murinus (Parti-coloured Bat) from Zoological collection of the Mammal Research Institute PAS. Collected 1964-07-23, in: Topiło, Poland. Material type: head
DOI: 10.48370/ofd/uebq73/vniz66
title: MRIPAS_coll_36379_VespertilioMurinus_1964_scan.jpg

description: :unav
DOI: 10.48370/ofd/uebq73/bhiev0
title: MRIPAS_coll_36379_VespertilioMurinus_1964_F_scan_ct.swf

description: :unav
DOI: 10.48370/ofd/uebq73
title: Vespertilio murinus - 36379, Zoological collection of the Mammal Research Institute, PAS

description: Vespertilio murinus (Parti-coloured Bat) from Zoological collection of the Mammal Research Institute PAS. Collected 1964-07-23, in: Topiło, Poland. Material type: head
DOI: 10.48370/ofd/gc64an/z8yrns
title: MRIPAS_coll_36380_VespertilioMurinus_1964_scan.jpg

description: :unav
DOI: 10.48370/ofd/gc64an
title: Vespertilio murinus - 36380, Zoological collection of the Mammal Research Institute, PAS

description: Vespertilio murinus (Parti-coloured Bat) from Zoological collection of the Mammal Research Institute PAS. Collected 1964-07-23, in: Topiło, Poland.
DOI: 10.48370/ofd/qpziuc/wue9qj
title: MRIPAS_coll_119104_VerspertilioMurinus_1976_scan.jpg

description: :unav
DOI: 10.48370/ofd/qpziuc/s8ror5
title: MRIPAS_coll_119104_VespertilioMurinus_1976_M_scan_ct.swf

description: :unav
DOI: 10.48370/ofd/qpziuc
title: Vespertilio murinus - 119104, Zoological collection of the Mammal Research Institute, PAS

description: Vespertilio murinus (Parti-coloured Bat) from Zoological collection of the Mammal Research Institute PAS. Collected 1976-07-13, in: Białowieża, Poland. Material type: head
DOI: 10.48370/ofd/z8jzyg
title: Xylotrechus adspersus (Gebler, 1830), C-875

description: Coleoptera collection
DOI: 10.48370/ofd/1fy0f2/cbaros
title: MRIPAS_coll_59867_exp_11000_SciurusVulgaris_1966_scan.jpg

description: :unav
DOI: 10.48370/ofd/1fy0f2
title: Sciurus vulgaris - 59867, Zoological collection of the Mammal Research Institute, PAS

description: Sciurus vulgaris (Red squirrel) from Zoological collection of the Mammal Research Institute PAS. Collected 1966-08-12, in: Białowieża Forest, Poland.
DOI: 10.48370/ofd/2klqcu/wpsw0a
title: MRIPAS_coll_61015_exp_15092_SciurusVulgaris_1966_scan.jpg

description: :unav
DOI: 10.48370/ofd/2klqcu
title: Sciurus vulgaris - 61015, Zoological collection of the Mammal Research Institute, PAS

description: Sciurus vulgaris (Red squirrel) from Zoological collection of the Mammal Research Institute PAS. Collected 1966-08-16, in: Trzebieszki, Poland.
DOI: 10.48370/ofd/0fuwfs/ozflhm
title: MRIPAS_coll_102701_exp_34856_SciurusVulgaris_1971_scan.jpg

description: :unav
DOI: 10.48370/ofd/0fuwfs
title: Sciurus vulgaris - 102701, Zoological collection of the Mammal Research Institute, PAS

description: Sciurus vulgaris (Red squirrel) from Zoological collection of the Mammal Research Institute PAS. Collected 1971-08-21, in: Kosobudy, Poland.
DOI: 10.48370/ofd/qfwiyl/hcibtv
title: MRIPAS_coll_124195_SciurusVulgaris_1977_scan.jpg

description: :unav
DOI: 10.48370/ofd/qfwiyl
title: Sciurus vulgaris - 124195, Zoological collection of the Mammal Research Institute, PAS

description: Sciurus vulgaris (Red squirrel) from Zoological collection of the Mammal Research Institute PAS. Collected 1977-04-18 in: Białowieża Forest, Poland.
DOI: 10.48370/ofd/sj4voj/jsyhyt
title: MIRPAS_coll_88596_exp_27300_LutraLutra_1937_scan.jpg

description: :unav
DOI: 10.48370/ofd/sj4voj
title: Lutra lutra - 88596, Zoological collection of the Mammal Research Institute, PAS

description: Lutra lutra (Eurasian otter) from Zoological collection of the Mammal Research Institute PAS. Collected 1937, in: Jesionka, Poland.
DOI: 10.48370/ofd/1xujca/ept8dk
title: MIRPAS_coll_135864_exp_53485_LutraLutra_1980_scan.jpg

description: :unav
DOI: 10.48370/ofd/cozud4
title: Xylotrechus hircus (Gebler, 1825), C-876

description: Coleoptera collection
DOI: 10.48370/ofd/1xujca
title: Lutra lutra - 135864, Zoological collection of the Mammal Research Institute, PAS

description: Lutra lutra (Eurasian otter) from Zoological collection of the Mammal Research Institute PAS. Collected 1980-01-18, in: Biebrza National Park, Olszowa Droga, Poland.