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List of results

• SUIT-031  + ([[File:1PM;2D;3S;4Rot;5U;-.png|400px]])
• SUIT-004  + ([[File:1PM;2D;3U;4S;5Rot.png|450px]])
• SUIT-029 O2 mt D066  + ([[File:1PM;2T;2D;2c;3Omy;4U;5G;6S;6U;7Rot;8Ama.png|350px]])
• SUIT-019 O2 pfi D045  + ([[File:1PalM;2D;2c;3Oct;4P;5G;6U;7S;8Rot;9Ama.png|400px]])
• SUIT-019  + ([[File:1PalM;2D;3Oct;4P;5G;6U;7S;8Rot-.png|450px]])
• SUIT-009 O2 mt D015  + ([[File:1S;2D;2c;3P;4Rot;5Ama.png|400px|SUIT9]])
• SUIT-009  + ([[File:1S;2D;3P;4Rot-.png|400px|SUIT9]])
• SUIT-009 AmR mt D021  + ([[File:1S;2D;3P;4Rot;5Ama.png|400px|SUIT-009]])
• SUIT-026 O2 mt D063  + ([[File:1S;2Rot;3D;3c;4Ama.png|400px]])
• SUIT-026  + ([[File:1S;2Rot;3D;4Ama.png|350px]])
• SUIT-006 O2 mt D022  + ([[File:1SRot;2D;2c;3(Omy);4U;5Ama.png|400px]])
• SUIT-006  + ([[File:1X;2D;2c;3Omy;4U-.png|450px]])
• SUIT-003 O2 ce D009  + ([[File:1ce;2ceOmy;3ceU-.jpg|450px]])
• SUIT-003 Ce1;ce2U-  + ([[File:1ce;2ceU-.jpg|150px]])
• SUIT-003 Ce1;ce3U-  + ([[File:1ce;3ceU-.jpg|150px]])
• SUIT-032 NADH mt D078  + ([[File:1mt;1PGM;2D;3Anox;4Myx;5Reox.png|300px]])
• Oxoglutarate  + ([[File:2-Oxoglutaric_acid.jpg|left|100px|2 … [[File:2-Oxoglutaric_acid.jpg|left|100px|2-Oxoglutaric acid]]</br>'''2-Oxoglutaric acid''' or alpha-ketoglutaric acid, C₅H₆O₅, occurs under physiological conditions as the anion '''2-Oxoglutarate^2-, Og'''. 2-Oxoglutarate (alpha-ketoglutarate) is formed from isocitrate as a product of [[isocitrate dehydrogenase]] (IDH) in the [[TCA cycle]], and is a substrate of [[oxoglutarate dehydrogenase]] (OgDH). The 2-oxoglutarate carrier exchanges malate^2- for 2-oxoglutarate^2- as part of the [[malate-aspartate shuttle]]. In the cytosol, oxoglutarate+aspartate are transaminated to form oxaloacetate+glutamate. Cytosolic malate dehydrogenase converts oxaloacetate+NADH to malate.transaminated to form oxaloacetate+glutamate. Cytosolic malate dehydrogenase converts oxaloacetate+NADH to malate.)
• Mitochondria-Targeted Drug Development  + ([[File:21640 - Mitochondria Targeted Thera … [[File:21640 - Mitochondria Targeted Therapeutics logo NEW.jpg|200px|left|Mitochondria-Targeted Drug Development]]</br>The '''Mitochondria-Targeted Drug Development Summit''' was first established in 2021, as an online conference. Due to its success and unmatched focus, the 2^nd edition returns to Boston this March 2022. </br>This is the only industry-led meeting that unites key stakeholders under a mutual and ambitious objective of '''accelerating the discovery and development of novel drugs that target mitochondrial functions''' for chronic, primary mitochondrial diseases, muscular dystrophy, metabolic disorders, and neurodegenerative diseases.</br>Join our speakers from '''GenSight Biologics, Abliva, Reneo Pharma, Mito BioPharma, Mitokinin''' and more with exciting networking opportunities, panel discussions and dedicated roundtables.tunities, panel discussions and dedicated roundtables.)
• Screwdriver allen wrench  + ([[File:24330-02.jpg|right|180px]]'''Screwdriver allen wrench''', a standard component of the [[O2k-FluoRespirometer]] and [[O2k-sV-Module]].)
• MultiSensor-Connector  + ([[File:30420-24 MultiSensorConnector.JPG|right|180px]] '''MultiSensor-Connector''': for separate reference electrode and [[ISE]]; only for O2k-Series B and Series C with MultiSensor electronic upgrading before 2011.)
• MultiSensor-Preamplifier 1/100  + ([[File:30430--24 NO-Attachment.JPG|right|180px]] '''MultiSensor-Preamplifier 1/100''': Required only for O2k-Series A-C, for application of NO (or other amperometric) sensors (single chamber mode of application).)
• TIP2k-Needle Safety Support with cable guide  + ([[File:31330-01 3.jpg|right|280px]] '''TIP2k-Needle Safety Support with cable guide''': for safe storage of TIP2k-needles and MultiSensor Modules cables when not required during the experiment.)
• Storage box sV  + ([[File:32001-01.jpg|right|180px]]'''Storage box sV''' empty, for storage of [[O2k-sV-Module]] components.)
• O2k-Chamber Holder sV  + ([[File:32100-01.jpg|right|180px]]'''O2k-Chamber Holder sV''' (black POM) for PVDF or PEEK stoppers (0.5-mL [[O2k-chamber]]), with [[O-ring\Viton\16x2 mm]] and [[V-ring\30-35-4.5 mm]].)
• POS-Holder sV  + ([[File:32300-01.jpg|right|180px]] '''POS-H … [[File:32300-01.jpg|right|180px]]</br>'''POS-Holder sV''', made from black POM, to be screwed into the copper block of the [[O2k-Main Unit]], guiding the [[OroboPOS|POS]] to the [[O2k-Chamber sV]], and keeping the SmartPOS/OroboPOS-Connector in a fixed position for sealing the O2k-Chamber sV with the [[POS-Seal Tip]]. In addition, the POS-Holder sV fixes the O2k-Chamber sV in an accurate rotational position by pressing against the angular cut of the glass chamber.inst the angular cut of the glass chamber.)
• O2k-Chamber sV  + ([[File:33100-01.jpg|right|180px]]'''O2k-Chamber sV''': 12 mm inner diameter, Duran® glass polished, with standard operation volume ''V'' of 0.5 mL.)
• Stirrer-Bar sV\white PVDF\11.5x6.2 mm  + ([[File:33210-01.jpg|right|180px]]'''Stirre … [[File:33210-01.jpg|right|180px]]'''Stirrer-Bar sV\white [[PVDF]]\11.5x6.2 mm''', operated in the 0.5-mL [[O2k-Chamber sV]] at constant stirring speed (standard is 750 rpm, or 12.5 Hz), to provide optimum mixing of the sample in the aqueous medium and ensure a stable signal of the polarographic oxygen sensor ([[OroboPOS]]) placed in a position of maximum current of the medium.position of maximum current of the medium.)
• Stopper sV\black PEEK\conical Shaft\central Port  + ([[File:34000-01.jpg|right|180px]]'''Stoppe … [[File:34000-01.jpg|right|180px]]'''Stopper sV\black PEEK\conical Shaft\central Port''': with conical shaft (with PTFE, graphite, carbon fiber) and one central capillary (1.0 mm diameter; 48.9 mm length), [[Volume-Calibration Ring sV]] (A or B) for volume adjustment 0.5 mL; 2 mounted O-rings ([[O-ring sV\Viton\9.5x1 mm]]).[[O-ring sV\Viton\9.5x1 mm]]).)
• O-ring sV\Viton\9.5x1 mm  + ([[File:34310-02.jpg|right|180px]]'''O-ring sV\[[Viton]]\9.5x1 mm''', for [[Stopper sV\black PEEK\conical Shaft\central Port | PEEK Stopper sV]], 2 are mounted on each PEEK Stopper sV, box of 8 as spares.)
• Asia Society for Mitochondrial Research and Medicine  + ([[File:ASMRM LOGO.JPG|200px|left]]The '''Asia Society for Mitochondrial Research and Medicine''' (ASMRM) was founded in 2003 to share the latest knowledge on mitochondrial research.)
• Acetyl-CoA  + ([[File:Acetyl coenzyme A 700.png|left|200p … [[File:Acetyl coenzyme A 700.png|left|200px|acetyl-CoA]]'''Acetyl-CoA''', C₂₃H₃₈N₇O₁₇P₃S, is a central piece in metabolism involved in several biological processes, but its main role is to deliver the acetyl group into the [[TCA cycle]] for its oxidation. It can be synthesized in different pathways: (i) in glycolysis from [[pyruvate]], by pyruvate dehydrogenase, which also forms NADH; (ii) from fatty acids β-oxidation, which releases one acetyl-CoA each round; (iii) in the catabolism of some amino acids such as leucine, lysine, phenylalanine, tyrosine and tryptophan.</br><br>In the mitochondrial matrix, acetyl-CoA is condensed with [[oxaloacetate]] to form [[citrate]] through the action of [[citrate synthase]] in the [[tricarboxylic acid cycle]]. Acetyl-CoA cannot cross the mitochondrial inner membrane but citrate can be transported out of the mitochondria. In the cytosol, citrate can be converted to acetyl-CoA and be used in the synthesis of fatty acid, cholesterol, ketone bodies, acetylcholine, and other processes. and be used in the synthesis of fatty acid, cholesterol, ketone bodies, acetylcholine, and other processes.)
• Aconitase  + ([[File:Aconitase.jpg|right|500px|aconitase … [[File:Aconitase.jpg|right|500px|aconitase]]'''Aconitase''' is a [[TCA cycle]] enzyme that catalyzes the reversible isomerization of [[citrate]] to [[isocitrate]]. Also, an isoform is also present in the cytosol acting as a trans-regulatory factor that controls iron homeostasis at a post-transcriptional level.<br>tasis at a post-transcriptional level.<br>)
• Cardiovascular Exercise Research Group  + ([[File:CERG.gif|200px|left|CERG]] The '''C … [[File:CERG.gif|200px|left|CERG]]</br>The '''Cardiovascular Exercise Research Group''' (CERG) was established in January 2008 and their research focuses on identifying the key cellular and molecular mechanisms underlying the beneficial effects of physical exercise on the heart, arteries and skeletal muscle in the context of disease prevention and management through experimental, clinical and epidemiological studies. </br>Since 2003 this research group organizes the biennial seminar [http://www.ntnu.edu/cerg/seminar-2013 "Exercise in Medicine"] in Trondheim, Norway.ercise in Medicine"] in Trondheim, Norway.)
• Complex II ambiguities  + ([[File:CII-ambiguities Graphical abstract. … [[File:CII-ambiguities Graphical abstract.png|300px|left|link=Gnaiger 2023 MitoFit CII]]The current narrative that the reduced coenzymes NADH and FADH2 feed electrons from the tricarboxylic acid (TCA) cycle into the mitochondrial electron transfer system can create ambiguities around respiratory Complex CII. Succinate dehydrogenase or CII reduces FAD to FADH2 in the canonical forward TCA cycle. However, some graphical representations of the membrane-bound electron transfer system (ETS) depict CII as the site of oxidation of FADH2. This leads to the false believe that FADH2 generated by electron transferring flavoprotein (CETF) in fatty acid oxidation and mitochondrial glycerophosphate dehydrogenase (CGpDH) feeds electrons into the ETS through CII. In reality, NADH and succinate produced in the TCA cycle are the substrates of Complexes CI and CII, respectively, and the reduced flavin groups FMNH2 and FADH2 are downstream products of CI and CII, respectively, carrying electrons from CI and CII into the Q-junction. Similarly, CETF and CGpDH feed electrons into the Q-junction but not through CII. The ambiguities surrounding Complex II in the literature call for quality control, to secure scientific standards in current communications on bioenergetics and support adequate clinical applications.nd support adequate clinical applications.)
• Complex II  + ([[File:CII.png |right|200px|link=Gnaiger 2 … [[File:CII.png |right|200px|link=Gnaiger 2023 MitoFit CII]]</br>'''Complex II''' or '''succinate:quinone oxidoreductase (SQR)''' is the only membrane-bound enzyme in the [[TCA cycle]] and is part of the [[electron transfer pathway]]. The reversible oxidoreduction of succinate and fumarate is catalyzed in a soluble domain and coupled to the reversible oxidoreduction of quinol and quinone in the mitochondrial inner membrane. CII consists in most species of four subunits. The flavoprotein [[succinate dehydrogenase]] is the largest polypeptide of CII, located on the matrix face of the mt-inner membrane. Succinate:quinone oxidoreductases (SQRs, SDHABCD) favour oxidation of succinate and reduction of quinone in the canonical forward direction of the TCA cycle and electron transfer into the [[Q-junction]]. In contrast, quinol:fumarate reductases (QFRs, fumarate reductases, FRDABCD) tend to operate in the reverse direction reducing fumarate and oxidizing quinol.on reducing fumarate and oxidizing quinol.)
• SUIT-007 O2 ce-pce D030  + ([[File:Ce1;1Dig;1G;2D;2c;3M;4U;5Ama.png|400px]])
• SUIT-027 O2 ce-pce D065  + ([[File:Ce1;1Dig;1M;2D;3M;4P;5G;6Ama.png|500px]])
• SUIT-006 O2 ce-pce D029  + ([[File:Ce1;1Dig;1PM;2D;2c;3Omy;4U;5Ama.png|600px]])
• SUIT-031 O2 ce-pce D079  + ([[File:Ce1;1Dig;1PM;2D;2c;3S;4Rot;5U;6Ama.png|400px]])
• SUIT-024  + ([[File:Ce1;1Dig;1PM;2T;2D;3Omy-.png|410px]])
• SUIT-024 O2 ce-pce D056  + ([[File:Ce1;1Dig;1PM;2T;2D;3Omy;4Ama.png|410px]])
• SUIT-031 Q ce-pce D074  + ([[File:Ce1;1Dig;1Q2;1PM;2D;3S;4Rot;5U;6Anox;7Ama.png|400px]])
• SUIT-009 O2 ce-pce D016  + ([[File:Ce1;1Dig;1S;2D;2c;3P;4Rot;5Ama.png|520px|SUIT-009]])
• SUIT-009 AmR ce-pce D019  + ([[File:Ce1;1Dig;1S;2D;3P;4Rot;5Ama.png|520px|SUIT9]])
• SUIT-026 AmR ce-pce D087  + ([[File:Ce1;1Dig;1S;2Rot;3D;4Ama.png|600px]])
• SUIT-018 AmR ce-pce D068  + ([[File:Ce1;1Dig;2GMS;3D;4Ama.png|290px]])
• SUIT-003 O2 ce D037  + ([[File:Ce1;ce1Glc;ce2(Omy);ce3U;ce4Ama.png|350px]])
• SUIT-003 O2 ce-pce D018  + ([[File:Ce1;ce1P;ce2Omy;ce3U;ce4Glc;ce5Rot;ce6S;1Dig;1U;1c;2Ama;3AsTm;4Azd.png|600px]])
• SUIT-003 O2 ce D012  + ([[File:Ce1;ce1P;ce2Omy;ce3U;ce4Rot;ce5Ama.png|400px]])
• SUIT-003 Ce1;ce1SD;ce3U;ce4Rot;ce5Ama  + ([[File:Ce1;ce1SD;ce3U;ce4Rot;ce5Ama.png|200px]])

• SUIT-003  + ([[File:Ce1;ce2(Omy);ce3U-.png|250px]] [[File:Ce5S;1Dig;1c-.png|250px]])

• SUIT-003 O2 ce D038  + ([[File:Ce1;ce2(Omy);ce3U;ce3Glc;ce3'U;ce4Ama.png|350px]])
• SUIT-003 Ce1;ce2U;ce3Rot;ce4S;ce5Ama  + ([[File:Ce1;ce2U;ce3Rot;ce4S;ce5Ama.png|200px]])
• SUIT-003 Ce1;ce3U;ce4Rot;ce5S;ce6Ama  + ([[File:Ce1;ce3U;ce4Rot;ce5S;ce6Ama.png|200px]])
• Cell Symposia  + ([[File:CellSymposiaLogo.jpg|90px]] Organized by the editors of Cell Press's leading journals, '''Cell Symposia''' bring together exceptional speakers and scientists to discuss topics at the forefront of scientific research.)
• Chemical background  + ([[File:Chb.png|100px|https://wiki.oroboros … [[File:Chb.png|100px|https://wiki.oroboros.at/index.php/File:Chb.png]] '''Chemical background''' ''Chb'' is due to autooxidation of the reagents. During CIV assays, ascorbate and TMPD are added to maintain cytochrome ''c'' in a reduced state. External cytochrome ''c'' may be included in the CIV assay. The autooxidation of these compounds is linearly oxygen-dependent down to approximately 50 µM oxygen and responsible for the chemical background oxygen flux after the inhibition of CIV. Oxygen flux due to the chemical reaction of autooxidation must be corrected for the [[Oxygen flux - instrumental background|instrumental O2 background]]. The correction for chemical background is necessary to determine CIV activity, in which case the instrumental O2 background and chemical background may be combined in an overall correction term.be combined in an overall correction term.)
• Citrate  + ([[File:Citrate 300 (1).png|left|100px|citr … [[File:Citrate 300 (1).png|left|100px|citrate]]'''citrate''', C₆H₅O₇^-3, is a tricarboxylic acid trianion, intermediate of the TCA cycle, obtained by deprotonation of the three carboxy groups of citric acid. Citrate is formed from [[oxaloacetate]] and acetyl-CoA through the catalytic activity of the [[citrate synthase]]. In the TCA cycle, citrate forms isocitrate by the activity of the [[aconitase]]. Citrate can be transported out of the mitochondria by the tricarboxylate transport, situated in the inner mitochondrial membrane. The transport occurs as an antiport of malate from the cytosol and it is a key process for fatty acid and oxaloacetate synthesis in the cytosol. <br>ol and it is a key process for fatty acid and oxaloacetate synthesis in the cytosol. <br>)
• Coenzyme Q2  + ([[File:Coenzyme Q2.png|left|200px|CoQ<s … [[File:Coenzyme Q2.png|left|200px|CoQ₂]]'''Coenzyme Q₂''' or ubiquinone-2 (CoQ₂) is a [[quinone]] derivate composed of a benzoquinone ring with an isoprenoid side chain consisting of two isoprenoid groups, with two methoxy groups, and with one methyl group. In HRR it is used as a Q-mimetic to detect the redox changes of [[coenzyme Q]] at the [[Q-junction]] in conjunction with the [[Q-Module]], since the naturally occurring long-chain coenzyme Q (e.g. CoQ₁₀) is trapped within membrane boundaries. CoQ₂ can react both with mitochondrial complexes (e.g. [[CI]], [[CII]] and [[CIII]]) at their quinone-binding sites and with the [[Three-electrode system |detecting electrode]].[[Three-electrode system |detecting electrode]].)
• Company of Scientists  + ([[File:Company-of-Scientists logo.jpg|left|140px|link=http://www.company-of-scientists.com|Company of Scientists]] The '''Company of Scientists''' evolves as a concept for implementing scientific innovations on the market.)
• Unit  + ([[File:Count-vs-number.png|right|120px|lin … [[File:Count-vs-number.png|right|120px|link=Elementary entity]]</br>A '''unit''' is defined as 'a single individual thing' in Euclid's ''Elements'' (Book VII). This defines the [[elementary entity]] ''U''_''X'' of entity-type ''X'' (thing). The [[International System of Units]] defines the unit as 'simply a particular example of the quantity concerned which is used as a reference'. Then the ''value'' of a quantity ''Q'' is the product of a number ''N'' and a unit ''u''_''Q''. The symbols ''U''_''X'' and ''u''_''Q'' are chosen here with ''U'' and ''u'' for 'unit': ''U''_''X'' is the Euclidean or entetic unit ('eunit'), and ''u''_''Q'' is the abstract unit ('aunit'). Subscripts ''X'' and ''Q'' for 'entity-type' and 'quantity-type' reflect perhaps even more clearly than words the contrasting meanings of the two fundamental definitions of an entetic versus abstract 'unit'. The term 'unit' with its dual meanings is used and confused in practical language and the scientific literature today. In the elementary entity ''U''_''X'', the unit (the 'one') relates to the entity-type ''X'', to the single individual thing (single individual or undivided; the root of the word ''thing'' has the meaning of 'assembly'). The quantity involved in the unit of a single thing is the ''count'', ''N''_''X'' = ''N''·''U''_''X'' [x]. In contrast to counting, a unit ''u''_''Q'' is linked to the measurement of quantities ''Q''_''u'' = ''N''·''u''_''Q'', such as volume, mass, energy; and these quantities — and hence the units ''u''_''Q'' — are abstracted from entity-types, pulled away from the world of real things. The new SI (2019-05-20) has completed this total abstraction of units, from the previous necessity to not only provide a quantitative definition but also a physical realization of a unit in the form of an 'artefact', such as the international prototype (IPK) for the unit kilogram. The new definitions of the base SI units are independent of any physical realization: ''u''_''Q'' is separate from ''X''. The classical unit of Euklid is the elementary unit for counting, entirely independent of measuring. Therefore, the quantity [[count]] is unique with respect to two properties: (''1'') in contrast to all other quantities in the metric system, the count depends on quantization of entities ''X''; and (''2'') in the SI, the '''N'''umber 1 is the '''U'''nit of the '''C'''ount of '''entities''' — NUCE.ntrast to all other quantities in the metric system, the count depends on quantization of entities ''X''; and (''2'') in the SI, the '''N'''umber 1 is the '''U'''nit of the '''C'''ount of '''entities''' — NUCE.)
• Elementary entity  + ([[File:Count-vs-number.png|right|120px|lin … [[File:Count-vs-number.png|right|120px|link=Unit]]</br>An '''elementary entity''' is an [[entity]] of type ''X'', distinguished as a single ''[[unit]]'' of countable objects (''X'' = molecules, cells, organisms, particles, parties, items) or events (''X'' = beats, collisions, emissions, decays, celestial cycles, instances, occurrences, parties). "An elementary entity may be an atom, a molecule, an ion, an electron, any other particle or specified group of particles" ([[Bureau International des Poids et Mesures 2019 The International System of Units (SI) |Bureau International des Poids et Mesures 2019)]]. An elementary entity, therefore, needs to be distinguished from non-countable entities and the general class of entities ''X''. This distinction is emphasized by the term 'elementary' (synonymous with 'elementary entity') with symbol ''U''_''X'' and [[unit |elementary unit]] [x].</br></br>If an object is defined as an assembly of particles (a party of two, a molecule as the assembly of a stoichiometric number of atoms), then the elementary is the assembly but not the assembled particle. A number of defined elementaries ''U''_''X'' is a [[count]], ''N''_''X'' = ''N''·''U''_''X'' [x], where ''N'' is a number, and as such ''N'' is dimensionless, and ''N'' is a ''number'' (stop) and is not 'a number of ..'. Elementaries are added as items to a count. The elementary ''U''_''X'' has the [[dimension]] U of the [[count]] ''N''_''X''. The elementary ''U''_''X'' has the same unit [x] as the count ''N''_''X'', or more accurately it gives the count the defining 'counting-unit', which is the 'elementary unit' [x]. From the definition of count as the number (''N'') of elementaries (''U'') of entity type ''X'', it follows that count divided by elementary is a pure number, ''N'' = ''N''_''X''·''U''_''X''^-1. The unit x of a count can neither be the entity ''X'' nor a number. The elementary of type ''X'' defines the identity ''X'' of the elementary ''U''_''X'' with the unit 'elementary unit' with symbol [x]. Since a count ''N''_''X'' is the number of elementary entities, the elementary ''U''_''X'' is not a count (''U''_''X'' is not identical with ''N''·''U''_''X'').''N''_''X'' is the number of elementary entities, the elementary ''U''_''X'' is not a count (''U''_''X'' is not identical with ''N''·''U''_''X'').)
• Count  + ([[File:Count-vs-number.png|right|120px|lin … [[File:Count-vs-number.png|right|120px|link=Number]]</br>'''Count''' ''N''_''X'' is the [[number]] ''N'' of elementary entities of [[entity]]-type ''X''. The single [[elementary entity]] ''U''_''X'' is a countable object or event. ''N''_''X'' is the number of objects of type ''X'', whereas the term 'entity' and symbol ''X'' are frequently used and understood in dual-message code indicating both (''1'') the entity-type ''X'' and (''2'') a count of ''N''_''X'' = 1 x for a single elementary entity ''U''_''X''. 'Count' is synonymous with 'number of entities' (number of particles such as molecules, or objects such as cells). Count is one of the most fundamental quantities in all areas of physics to biology, sociology, economy and philosophy, including all perspectives of the statics of countable objects to the dynamics of countable events. The term 'number of entities' can be used in short for 'number of elementary entities', since only elementary entities can be counted, and as long as it is clear from the context, that it is not the number of different entity types that are the object of the count.rom the context, that it is not the number of different entity types that are the object of the count.)
• Elementary unit  + ([[File:Count-vs-number.png|right|120px|lin … [[File:Count-vs-number.png|right|120px|link=Elementary entity]]The '''elementary unit''' [x] is the unit of a [[count]] ''N''_''X'' [x]. The [[International System of Units]] defines the unit of a count as 1. Then the '''N'''umber 1 is the '''U'''nit of the '''C'''ount of '''E'''ntities — NUCE. This causes a number of formal inconsistencies which are resolved by introducing the elementary unit [x] as the abstracted unit of Euclid’s unit, which is an [[elementary entity]] ''U''_''X'' [x], and as the unit of Euclid’s number, which is a count ''N''_''X'' [x].it of Euclid’s number, which is a count ''N''_''X'' [x].)
• DORA  + ([[File:Dorabadge5.png|150px|right]] The Declaration on Research Assessment '''DORA''' recognizes the need to improve the ways in which researchers and the outputs of scholarly research are evaluated.)
• Level flow  + ([[File:E.jpg |link=ET capacity]] '''Level … [[File:E.jpg |link=ET capacity]] '''Level flow''' is a [[steady state]] of a system with an input process coupled to an output process (coupled system), in which the output force is zero. ''Clearly, energy must be expended to maintain level flow, even though output is zero'' (Caplan and Essig 1983; referring to zero output force, while output flow may be maximum). force, while output flow may be maximum).)
• Noncoupled respiration  + ([[File:E.jpg |link=ET capacity]] '''Noncou … [[File:E.jpg |link=ET capacity]] '''Noncoupled respiration''' is distinguished from general (pharmacological or mechanical) [[uncoupled respiration]], to give a label to an effort to reach the state of maximum uncoupler-activated respiration without inhibiting respiration. Noncoupled respiration, therefore, yields an estimate of [[ET capacity]]. Experimentally uncoupled respiration may fail to yield an estimate of ET capacity, due to inhibition of respiration above optimum uncoupler concentrations or insufficient stimulation by sub-optimal uncoupler concentrations. Optimum uncoupler concentrations for evaluation of (noncoupled) ET capacity require inhibitor titrations ([[Steinlechner-Maran 1996 Am J Physiol Cell Physiol]]; [[Huetter 2004 Biochem J]]; [[Gnaiger 2008 POS]]). </br></br>Noncoupled respiration is maximum [[electron flow]] in an open-transmembrane proton circuit mode of operation (see [[ET capacity]]).</br>» [[#Is_respiration_uncoupled_-_noncoupled_-_dyscoupled.3F |'''MiPNet article''']][#Is_respiration_uncoupled_-_noncoupled_-_dyscoupled.3F |'''MiPNet article''']])
• State 3u  + ([[File:E.jpg |link=ET capacity]] Noncouple … [[File:E.jpg |link=ET capacity]] Noncoupled state of [[ET capacity]]. '''State 3u''' (u for uncoupled) has been used frequently in bioenergetics, without sufficient emphasis [[Villani 1998 J Biol Chem|(e.g. Villani et al 1998)]] on the fundamental difference between [[OXPHOS capacity]] (''P'', coupled with an uncoupled contribution; State 3) and noncoupled [[ET capacity]] (''E''; State 3u) ([[Gnaiger 2009 Int J Biochem Cell Biol|Gnaiger 2009]]; [[Rasmussen 2000 Mol Cell Biochem|Rasmussen and Rasmussen 2000]]).[[Rasmussen 2000 Mol Cell Biochem|Rasmussen and Rasmussen 2000]]).)
• ET capacity  + ([[File:E.jpg]] '''T capacity''' is the res … [[File:E.jpg]] '''T capacity''' is the respiratory electron-transfer-pathway capacity ''E'' of mitochondria measured as oxygen consumption in the noncoupled state at optimum [[uncoupler]] concentration. This optimum concentration is obtained by stepwise titration of an established protonophore to induce maximum oxygen flux as the determinant of ET capacity. The experimentally induced noncoupled state at optimum uncoupler concentration is thus distinguished from (''1'') a wide range of uncoupled states at any experimental uncoupler concentration, (''2'') physiological uncoupled states controlled by intrinsic uncoupling (e.g. UCP1 in brown fat), and (''3'') pathological dyscoupled states indicative of mitochondrial injuries or toxic effects of pharmacological or environmental substances. ET capacity in mitochondrial preparations requires the addition of defined fuel substrates to establish an ET-pathway competent state.</br>» [[#Why ET capacity, why not State 3u.3F | '''MiPNet article''']][#Why ET capacity, why not State 3u.3F | '''MiPNet article''']])
• EUROMIT  + ([[File:EUROMIT.jpg|left|250px]] '''EUROMIT''' is a group based in Europe for organizing '''International Meetings on Mitochondrial Pathology'''.)
• Ethanol  + ([[File:Ethanol.png|left|80px|Ethanol]] < … [[File:Ethanol.png|left|80px|Ethanol]]</br><div></br></div><div>'''Ethanol''' or ethyl alcohol, C₂H₆O or EtOH, is widely used in the laboratory, particularly as a solvent and cleaning agent. There are different grades of high purity ethanol. Up to a purity of 95.6 % ethanol can be separated from water by destillation. Higher concentrations than 95% require usage of additives that disrupt the azeotrope composition and allow further distillation. Ethanol is qualified as "absolute" if it contains no more than one percent water. Whenever 'ethanol abs.' is mentioned without further specification in published protocols, it refers to ≥ 99 % ethanol a.r. (analytical reagent grade).</br></br></div><div></br></br></div><div></div>s to ≥ 99 % ethanol a.r. (analytical reagent grade). </div><div> </div><div></div>)
• Glutamate-anaplerotic pathway control state  + ([[File:G.jpg|left|200px|G]] '''G''': [[Glu … [[File:G.jpg|left|200px|G]] '''G''': [[Glutamate]] is an [[Anaplerotic pathway control state |anaplerotic]] [[Electron-transfer-pathway state |NADH-linked type 4 substrate]] (N). When supplied as the sole fuel substrate in the '''glutamate-anaplerotic pathway control state''', G is transported by the electroneutral glutamate-/OH- exchanger, and is oxidised via mt-[[glutamate dehydrogenase]] in the mitochondrial matrix. The G-pathway plays an important role in [[glutaminolysis]].[[glutaminolysis]].)
• GM-pathway control state  + ([[File:GM.jpg|left|200px|GM]] '''GM''': [[ … [[File:GM.jpg|left|200px|GM]] '''GM''': [[Glutamate]] & [[Malate]].</br></br>'''MitoPathway control state:''' [[NADH electron transfer-pathway state]]</br></br>The '''GM-pathway control state''' (glutamate-malate pathway control state) is established when glutamate&malate are added to isolated mitochondria, permeabilized cells and other mitochondrial preparations. Glutamate and transaminase are responsible for the metabolism of [[oxaloacetate]], comparable to the metabolism with acetyl-CoA and citrate synthase.e metabolism with acetyl-CoA and citrate synthase.)
• GMS-pathway control state  + ([[File:GMS.jpg|left|200px|GMS]]'''GMS''': … [[File:GMS.jpg|left|200px|GMS]]'''GMS''': [[Glutamate]] & [[Malate]] & [[Succinate]].</br></br>'''MitoPathway control:''' NS</br></br>Transaminase catalyzes the reaction from oxaloacetate to 2-oxoglutarate, which then establishes a cycle without generation of citrate. OXPHOS is higher with GS (CI&II) compared to GM (CI) or SRot (CII). This documents an additive effect of convergent CI&II electron flow to the Q-junction, with consistent results obtained with permeabilized muscle fibres and isolated mitochondria (Gnaiger 2009).ed muscle fibres and isolated mitochondria (Gnaiger 2009).)
• Glutamate  + ([[File:Glutamic_acid.jpg|left|100px|Glutam … [[File:Glutamic_acid.jpg|left|100px|Glutamic acid]]'''Glutamic acid''', C₅H₉NO₄, is an amino acid which occurs under physiological conditions mainly as the anion '''glutamate^-, G''', with ''p''K_a1 = 2.1, ''p''K_a2 = 4.07 and ''p''K_a3 = 9.47. Glutamate&malate is a substrate combination supporting an N-linked pathway control state, when glutamate is transported into the mt-matrix via the [[glutamate-aspartate carrier]] and reacts with [[oxaloacetate]] in the transaminase reaction to form aspartate and [[oxoglutarate]]. Glutamate as the sole substrate is transported by the electroneutral glutamate^-/OH^- exchanger, and is oxidized in the mitochondrial matrix by [[glutamate dehydrogenase]] to α-ketoglutarate ([[oxoglutarate|2-oxoglutarate]]), representing the [[glutamate-anaplerotic pathway control state]]. Ammonia (the byproduct of the reaction) passes freely through the mitochondrial membrane.[glutamate-anaplerotic pathway control state]]. Ammonia (the byproduct of the reaction) passes freely through the mitochondrial membrane.)
• Glycerophosphate shuttle  + ([[File:Gp-shuttle.jpg|left|200px|Gp]] The … [[File:Gp-shuttle.jpg|left|200px|Gp]]</br>The '''glycerophosphate shuttle''' makes cytoplasmic NADH available for mitochondrial oxidative phosphorylation. Cytoplasmic NADH reacts with dihydroxyacetone phosphate catalyzed by cytoplasmic glycerophosphate dehydrogenase. On the outer face of the inner mitochondrial membrane, [[glycerophosphate dehydrogenase complex]] (mitochondrial glycerophosphate dehydrogenase) oxidizes glycerophosphate back to dihydroxyacetone phosphate, a reaction not generating NADH but reducing a flavin prosthesic group. The reduced flavoprotein transfers its reducing equivalents into the [[Q-junction]], thus representing a [[Electron-transfer-pathway state|ET pathway level 3 control state]].[[Electron-transfer-pathway state|ET pathway level 3 control state]].)
• Water  + ([[File:H2O.jpg|left|60px|Water]] '''Water' … [[File:H2O.jpg|left|60px|Water]]</br>'''Water''', H₂O, is widely used in the laboratory, particularly as a solvent and cleaning agent. Chemically pure water is prepared in various grades of purification: double distilled water (ddH₂O) versus distilled water (dH₂O or [[aqua destillata]], a.d.) and deionized or demineralized water (diH₂O) with various combination purification methods. When H₂O is mentioned without further specification in published protocols, it is frequently assumed that the standards of each laboratory are applied as to the quality of purified water. Purification is not only to be controlled with respect to salt content and corresponding electrical conductivity (ultra-pure water: 5.5 μS/m due to H⁺ and OH^- ions), but also in terms of microbial contamination. 5.5 μS/m due to H⁺ and OH^- ions), but also in terms of microbial contamination.)
• Hydrogen peroxide  + ([[File:H2O2.jpg|left|60px|Hydrogen peroxid … [[File:H2O2.jpg|left|60px|Hydrogen peroxide]]</br>'''Hydrogen peroxide''', H₂O₂ or dihydrogen dioxide, is one of several reactive oxygen intermediates generally referred to as [[reactive oxygen species]] (ROS). It is formed in various enzyme-catalyzed reactions (''e.g.'', [[superoxide dismutase]]) with the potential to damage cellular molecules and structures. H₂O₂ is dismutated by [[catalase]] to water and [[oxygen]]. H₂O₂ is produced as a signaling molecule in aerobic metabolism and passes membranes more easily compared to other ROS. is produced as a signaling molecule in aerobic metabolism and passes membranes more easily compared to other ROS.)
• International Mito Patients (IMP)  + ([[File:IMP LOGO.JPG|150px]]The '''Internat … [[File:IMP LOGO.JPG|150px]]The '''International Mito Patients''' is a network of national patient organizations involved in mitochondrial disease. Mitochondrial disease is a rare disease with a limited number of patients per country. The national patient organizations which are a member of IMP each are active and powerful in their own countries. By joining forces IMP can represent a large group of patients and as such be their voice on an international level. be their voice on an international level.)
• IRDiRC  + ([[File:IRDiRC.png|150px]] The Internationa … [[File:IRDiRC.png|150px]] The International Rare Diseases Research Consortium (IRDiRC) teams up researchers and organizations investing in rare diseases research in order to achieve two main objectives by the year 2020, namely to deliver 200 new therapies for rare diseases and means to diagnose most rare diseases. and means to diagnose most rare diseases.)
• International Society for Mountain Medicine  + ([[File:ISMM.jpg|150px|left|ISMM]]The '''International Society for Mountain Medicine''' is an interdisciplinary society comprising about xx members worldwide. Its purpose is ..)
• International Society on Oxygen Transport to Tissue  + ([[File:ISOTT LOGO.jpg|200px|left]] The ''' … [[File:ISOTT LOGO.jpg|200px|left]]</br>The '''International Society on Oxygen Transport to Tissue''' is an interdisciplinary society comprising about 250 members worldwide. Its purpose is to further the understanding of all aspects of the processes involved in the transport of oxygen from the air to its ultimate consumption in the cells of the various organs of the body. Founded in 1973, the society has been the leading platform for the presentation of many of the technological and conceptual developments within the field both at the meetings themselves and in the proceedings of the society.ves and in the proceedings of the society.)
• Isocitrate  + ([[File:Isocitrate.png|left|100px|isocitrat … [[File:Isocitrate.png|left|100px|isocitrate]]'''isocitrate''', C₆H₅O₇^-3, is a tricarboxylic acid trianion, intermediate of the [[tricarboxylic acid cycle|TCA cycle]], obtained by isomerization of citrate. The process is catalyzed by [[aconitase]], forming the enzyme-bound intermediate ''cis''-aconitate.[[aconitase]], forming the enzyme-bound intermediate ''cis''-aconitate.)
• E-L coupling efficiency  + ([[File:J(E-L).jpg|50 px|E-L coupling effic … [[File:J(E-L).jpg|50 px|E-L coupling efficiency]] The '''''E-L'' coupling efficiency''', ''j_E-L'' = (''E-L'')/''E'' = 1-''L/E'', is 0.0 at zero coupling (''L''=''E'') and 1.0 at the limit of a fully coupled system (''L''=0). The background state is the [[LEAK respiration|LEAK]] state which is stimulated to flux in the [[electron transfer pathway]] reference state by [[uncoupler]] titration. LEAK states ''L''_N or ''L''_T may be stimulated first by saturating ADP (rate ''P'' in the OXPHOS state) with subsequent uncoupler titration to the ET state with maximum rate ''E''. The ''E-L'' coupling efficiency is based on measurement of a [[coupling-control ratio]] ([[LEAK-control ratio]], ''L/E''), whereas the thermodynamic or [[ergodynamic efficiency]] of coupling between ATP production (phosphorylation of ADP to ATP) and oxygen consumption is based on measurement of the output/input flux ratio (P»/O₂ ratio) and output/input force ratio (Gibbs force of phosphorylation/Gibbs force of oxidation). The [[biochemical coupling efficiency]] expressed as the ''E-L'' coupling efficiency is independent of kinetic control by the ''E-P'' control efficiency, and is equal to the [[P-L control efficiency |''P-L'' control efficiency]] if ''P=E'' as evaluated in a [[coupling-control protocol]].</br>» [[#Biochemical_coupling_efficiency:_from_0_to_.3C1 | '''MiPNet article''']]#Biochemical_coupling_efficiency:_from_0_to_.3C1 | '''MiPNet article''']])
• Biochemical coupling efficiency  + ([[File:J(E-L).jpg|50 px|link=E-L coupling … [[File:J(E-L).jpg|50 px|link=E-L coupling efficiency |''E-L'' coupling efficiency]] The '''biochemical coupling efficiency''' is the [[E-L coupling efficiency |''E-L'' coupling efficiency]], (''E-L'')/''E'' = 1-''L/E''. This is equivalent to the [[P-L control efficiency |''P-L'' control efficiency]], (''P-L'')/''P'' = 1-''L/P'', only at zero [[E-P excess capacity |''E-P'' excess capacity]], when ''P'' = ''E''). The biochemical coupling efficiency is independent of kinetic control by the phosphorylation system.tic control by the phosphorylation system.)
• E-P control efficiency  + ([[File:J(E-P).jpg|50 px|E-P control effici … [[File:J(E-P).jpg|50 px|E-P control efficiency]] The '''''E-P'' control efficiency''', ''j_E-P'' = (''E-P'')/''E'' = 1-''P/E'', is an expression of the relative limitation of [[OXPHOS capacity]] by the capacity of the [[phosphorylation system]]. It is the normalized ''E-P'' excess capacity. ''j_E-P'' = 0.0 when OXPHOS capacity is not limited by the phosphorylation system at zero ''E-P'' excess capacity, ''P''=''E'', when the phosphorylation system does not exert any control over OXPHOS capacity. ''j_E-P'' increases with increasing control of the phosphorylation system over OXPHOS capacity. ''j_E-P'' = 1 at the limit of zero phosphorylation capacity. The [[OXPHOS]] state of mt-preparations is stimulated to [[electron transfer pathway]] capacity ''E'' by [[uncoupler]] titration, which yields the [[E-P excess capacity |''E-P'' excess capacity]].[[E-P excess capacity |''E-P'' excess capacity]].)
• P-L control efficiency  + ([[File:J(P-L).jpg|50 px|P-L control effici … [[File:J(P-L).jpg|50 px|P-L control efficiency]] The '''''P-L'' control efficiency''' (''P-L'' flux control efficiency) is defined as ''j_P-L'' = (''P-L'')/''P'' = 1-''L/P''. [[OXPHOS capacity]] corrected for [[LEAK respiration]] is the [[P-L net OXPHOS capacity]], ''P-L''. The ''P-L'' control efficiency is the ratio of net to total OXPHOS capacity, which is equal to the biochemical ''E-L'' coupling efficiency, if ''P''=''E''. ''j_P-L'' = 1.0 for a fully coupled system (when RCR approaches infinity); ''j_P-L'' = 0.0 (RCR=1) for a system with zero respiratory phosphorylation capacity (''P-L''=0) or zero [[E-L coupling efficiency |''E-L'' coupling efficiency]] (''E-L''=0 when ''L''=''P''=''E''). If [[State 3]] is measured at saturating concentrations of ADP and P_i (State 3 = ''P''), then the [[respiratory acceptor control ratio]] RCR equals ''P/L''. Under these conditions, the respiratory control ratio and ''P-L'' control efficiency are related by a hyperbolic function, ''j_P-L'' = 1-RCR^-1.</br>» [[#Cell ergometry: OXPHOS-control and ET-coupling efficiency |'''MiPNet article''']][#Cell ergometry: OXPHOS-control and ET-coupling efficiency |'''MiPNet article''']])
• R-L control efficiency  + ([[File:J(R-L).jpg|50 px|R-L ROUTINE-coupli … [[File:J(R-L).jpg|50 px|R-L ROUTINE-coupling efficiency]]</br>The '''''R-L'' control efficiency''', ''j_R-L'' = (''R-L'')/''R'' = 1-''L/R'', is the fraction of [[ROUTINE respiration]] coupled to phosphorylation in living cells. ROUTINE respiration is corrected for [[LEAK respiration]] to obtain the [[R-L net ROUTINE capacity |''R-L'' net ROUTINE capacity]]. The flux control efficiency ''j_R-L'' is the ''R-L'' net ROUTINE capacity normalized for the reference rate ''R''. The background state is the [[LEAK respiration|LEAK]] state, and the flux control variable is stimulation to ROUTINE respiration by physiologically controlled ATP turnover in living cells.ration by physiologically controlled ATP turnover in living cells.)
• Japanese Society of Mitochondrial Research and Medicine  + ([[File:J-mit.png|100px|left]]The '''Japane … [[File:J-mit.png|100px|left]]The '''Japanese Society of Mitochondrial Research and Medicine''' (J-mit) was founded to share the latest knowledge on mitochondrial research. J-mit is the biggest Asian society of mitochondrial research and medicine and is a member of [[ASMRM]].[[ASMRM]].)
• State 4  + ([[File:L.jpg |link=LEAK respiration]] '''S … [[File:L.jpg |link=LEAK respiration]] '''State 4''' is the [[respiratory state]] obtained in isolated mitochondria after [[State 3]], when added [[ADP]] is phosphorylated maximally to [[ATP]] driven by electron transfer from defined respiratory substrates to O₂ ([[Chance 1955 JBC-III|Chance and Williams, 1955]]). State 4 represents [[LEAK respiration]], ''L''_T (''L'' for [[LEAK respiration]]; T for ATP), or an overestimation of LEAK respiration if [[ATPase]] activity prevents final accumulation of ATP and maintains a continuous stimulation of respiration by recycled ADP. This can be tested by inhibition of ATP synthase by [[oligomycin]]; ''L''_Omy). In the [[LEAK state]] (state of non-phosphorylating resting respiration; static head), oxygen flux is decreased to a minimum (corrected for [[ROX]]), and the [[mt-membrane potential]] is increased to a maximum for a specific substrate or substrate combination.] is increased to a maximum for a specific substrate or substrate combination.)
• Static head  + ([[File:L.jpg |link=LEAK respiration]] '''S … [[File:L.jpg |link=LEAK respiration]] '''Static head''' is a [[steady state]] of a system with an input process coupled to an output process (coupled system), in which the output force is maximized at constant input or driving force up to a level at which the conjugated output flow is reduced to zero. ''In an incompletely coupled system, energy must be expended to maintain static head, even though the output is zero'' (Caplan and Essig 1983; referring to output flow at maximum output force). [[LEAK respiration]] is a measure of input flow at static head, when the output flow of phosphorylation (ADP->ATP) is zero at maximum phosphorylation potential (Gibbs force of phosphorylation; [[Gnaiger_1993_Hypoxia|Gnaiger 1993a]]). </br></br>In a completely coupled system, not only the output flux but also the input flux are zero at static head, which then is a state of ''[[ergodynamic equilibrium]]'' ([[Gnaiger_1993_Pure_Appl_Chem |Gnaiger 1993b]]). Whereas the output force is maximum at ergodynamic equilibrium compensating for any given input force, all forces are zero at ''[[thermodynamic equilibrium]]''. Flows are zero at both types of equilibria, hence entropy production or power (power = flow x force) are zero in both cases, i.e. at thermodynamic equilibrium in general, and at ergodynamic equilibrium of a completely coupled system at static head.f a completely coupled system at static head.)
• LEAK state without adenylates  + ([[File:L.jpg |link=LEAK respiration]] In t … [[File:L.jpg |link=LEAK respiration]] In the '''LEAK state without adenylates''' mitochondrial LEAK respiration, ''L''(n) (n for no adenylates), is measured after addition of substrates, which decreases slowly to the [[LEAK state]] after oxidation of endogenous substrates with no [[adenylates]]. ''L''(n) is distinguished from ''L''(T) and ''L''(Omy).istinguished from ''L''(T) and ''L''(Omy).)
• LEAK state with ATP  + ([[File:L.jpg |link=LEAK respiration]] The … [[File:L.jpg |link=LEAK respiration]] The '''LEAK state with ATP''' is obtained in mt-preparations without ATPase activity after ADP is maximally phosphorylated to ATP ([[State 4]]; Chance and Williams 1955) or after addition of high ATP in the absence of ADP ([[Gnaiger 2000 Proc Natl Acad Sci U S A |Gnaiger et al 2000]]). Respiration in the LEAK state with ATP, ''L''(T), is distinguished from ''L''(n) and ''L''(Omy).istinguished from ''L''(n) and ''L''(Omy).)
• LEAK state with oligomycin  + ([[File:L.jpg |link=LEAK respiration]] The … [[File:L.jpg |link=LEAK respiration]] The '''LEAK state with oligomycin''' is a [[LEAK state]] induced by inhibition of ATP synthase by [[oligomycin]]. ADP and ATP may or may not be present. LEAK respiration with oligomycin, ''L''(Omy), is distinguished from ''L''(n) and ''L''(T). distinguished from ''L''(n) and ''L''(T).)
• LEAK respiration  + ([[File:L.jpg]] '''EAK respiration''' or LE … [[File:L.jpg]] '''EAK respiration''' or LEAK oxygen flux ''L'' compensating for [[proton leak]], [[proton slip]], cation cycling and [[electron leak]], is a dissipative component of respiration which is not available for performing biochemical work and thus related to heat production. LEAK respiration is measured in the LEAK state, in the presence of reducing substrate(s), but absence of ADP - abbreviated as ''L''(n) (theoretically, absence of inorganic phosphate presents an alternative), or after enzymatic inhibition of the [[phosphorylation system]], which can be reached with the use of [[oligomycin]] - abbreviated as ''L''(Omy). The '''LEAK state''' is the non-phosphorylating resting state of intrinsic [[Uncoupler|uncoupled]] or [[Dyscoupled respiration|dyscoupled respiration]] when oxygen flux is maintained mainly to compensate for the proton leak at a high chemiosmotic potential, when ATP synthase is not active. In this non-phosphorylating resting state, the electrochemical proton gradient is increased to a maximum, exerting feedback control by depressing oxygen flux to a level determined mainly by the proton leak and the H⁺/O₂ ratio. In this state of maximum protonmotive force, LEAK respiration, ''L'', is higher than the LEAK component of [[OXPHOS capacity]], ''P''. The conditions for measurement and expression of respiration vary ([[oxygen flux]] in the LEAK state, ''J''_O₂''L'', or [[oxygen flow]], ''I''_O₂''L''). If these conditions are defined and remain consistent within a given context, then the simple symbol ''L'' for respiratory rate can be used as a substitute for the more explicit expression for respiratory activity.</br>» [[LEAK respiration#LEAK respiration: concept-linked terminology of respiratory states |'''MiPNet article''']][LEAK respiration#LEAK respiration: concept-linked terminology of respiratory states |'''MiPNet article''']])
• Malate-anaplerotic pathway control state  + ([[File:M.jpg|left|200px|M]] '''M''': [[Mal … [[File:M.jpg|left|200px|M]] '''M''': [[Malate]] alone does not support respiration of mt-preparations if [[oxaloacetate]] cannot be metabolized further in the absence of a source of acetyl-CoA. Transport of oxaloacetate across the inner mt-membrane is restricted particularly in liver. Mitochondrial citrate and 2-oxoglutarate (α-ketoglutarate) are depleted by antiport with malate. [[Succinate]] is lost from the mitochondria through the dicarboxylate carrier. OXPHOS capacity with malate alone is only 1.3% of that with [[PM |Pyruvate&Malate]] in isolated rat skeletal muscle mitochondria. However, many mammalian and non-mammalian mitochondria have a mt-isoform of NADP^+- or NAD(P)<big>+</big>-dependent [[malic enzyme]] (mtME), the latter being particularly active in proliferating cells. Then the [[anaplerotic pathway control state]] with malate alone (aN) supports high respiratory activities comparable to the NADH-linked pathway control states (N) with pyruvate&malate or glutamate&malate substrate combinations ([[PM-pathway control state]], [[GM-pathway control state]]).[GM-pathway control state]]).)
• PM-pathway control state  + ([[File:M.jpg|left|200px|PM]] '''PM''': [[P … [[File:M.jpg|left|200px|PM]] '''PM''': [[Pyruvate]] & [[Malate]].</br></br>'''MitoPathway control state:''' [[NADH Electron transfer-pathway state]]</br></br></br>Upstream of the NAD-junction, [[Pyruvate]] (P) is oxidatively decarboxylated to acetyl-CoA and CO₂, yielding [[NADH]] catalyzed by pyruvate dehydrogenase. [[Malate]] (M) is oxidized to oxaloacetate by mt-malate dehydrogenase located in the mitochondrial matrix. Condensation of oxaloacate with acetyl-CoA yields citrate (citrate synthase). 2-oxoglutarate (α-ketoglutarate) is formed from isocitrate (isocitrate dehydrogenase).ate) is formed from isocitrate (isocitrate dehydrogenase).)
• MITOEAGLE in MitoGlobal  + ([[File:MITOEAGLE-representation.jpg|150px|left]] The objective of the '''MitoEAGLE''' network is to improve our knowledge on mitochondrial function in health and disease related to Evolution, Age, Gender, Lifestyle and Environment.)
• MitoKit-CII  + ([[File:MITOKIT-CII.jpg|right|180px]]'''Cel … [[File:MITOKIT-CII.jpg|right|180px]]'''Cell permeable prodrugs''', composed of [[MitoKit-CII/Succinate-nv]] and [[MitoKit-CII/Malonate-nv]], stimulates (Snv) or inhibits (Mnanv) mitochondrial respiration in CI-deficient human blood cells, fibroblasts and heart fibres, acting on Complex II of the electron transfer system.omplex II of the electron transfer system.)
• Rare New England  + ([[File:MNE.jpg|left|110px|MNE]] MNE has tr … [[File:MNE.jpg|left|110px|MNE]]</br>MNE has transitioned into RNE (Rare New England). Rare New England is an organization providing access to support groups, gatherings, events and resources for those affected by Rare Disease and living in the New England area.isease and living in the New England area.)
• Mitochondria Research Society  + ([[File:MRS LOGO.JPG|250px|left]] The '''Mi … [[File:MRS LOGO.JPG|250px|left]]</br>The '''Mitochondria Research Society''' (MRS) is a nonprofit international organization of scientists and physicians. The purpose of MRS is to find a cure for mitochondrial diseases by promoting research on basic science of mitochondria, mitochondrial pathogenesis, prevention, diagnosis and treatment through out the world.nosis and treatment through out the world.)
• Malate  + ([[File:Malic_acid.jpg|left|100px|Malic aci … [[File:Malic_acid.jpg|left|100px|Malic acid]]</br>'''Malic acid''', C₄H₆O₅, occurs under physiological conditions as the anion '''malate^2-, M''', with p''K''_a1 = 3.40 and p''K''_a2 = 5.20. L-Malate is formed from fumarate in the [[TCA cycle]] in the mitochondrial matrix, where it is the substrate of [[malate dehydrogenase]] oxidized to [[oxaloacetate]]. Malate is also formed in the cytosol. It cannot permeate through the lipid bilayer of membranes and hence requires a carrier ([[dicarboxylate carrier]], [[tricarboxylate carrier]] and 2-oxoglutarate carrier). Malate alone cannot support respiration of [[Mitochondrial preparations|mt-preparations]] from most tissues, since oxaloacetate accumulates in the absence of [[pyruvate]] or [[glutamate]].</br>Malate is a [[NADH electron transfer-pathway state |type N substrate]] (N) required for the [[Fatty acid oxidation pathway control state| FAO-pathway]]. In the presence of [[Malate-anaplerotic pathway control state|anaplerotic pathways]] (''e.g.'', [[Malic enzyme|mitochondrial malic enzyme, mtME]]) the capacity of the FAO-pathway can be overestimated due to a contribution of NADH-linked respiration, F(N) (see [[SUIT-002]]).[[SUIT-002]]).)